ANTI-CD45 ANTIBODIES AND RELATED THERAPEUTICS Earlier application This application claims priority from United Kingdom application number GB2015235.1, filed 25 September 2020. The priority application is hereby incorporated by reference in its entirety and for any and all purposes as if fully set forth herein. Field of the invention The present invention relates to novel antibodies, biparatopic antibodies, and fragments thereof, which specifically bind human CD45. The invention also relates to antibody drug conjugates comprising the antibodies. Also provided are uses of the antibodies, antibody drug conjugates and biparatopic antibodies and pharmaceutical compositions comprising the antibodies, antibody drug conjugates and biparatopic antibodies. BACKGROUND Many patients with blood cancers or diseases curable by hematopoietic stem cell transplantation (HSCT) or gene therapy are ineligible for treatments because of toxic conditioning regimes. Bone marrow transplant (BMT) from a genetically matched sibling or close relative is a well-established procedure for curing a broad range haematological (blood) disorders including haemoglobinopathies, bone marrow failure, primary immunodeficiency (PID), blood cancers and metabolic diseases. HSCT is also curative for a wide variety of severe genetic (congenital) diseases. However, many patients are ineligible for HSCT or gene therapy, or are unwilling to accept therapy for haematological cancer, specifically because they cannot tolerate the required conditioning due to age or comorbidity. The intensive systemic conditioning with chemo/radiotherapy required to achieve myeloablation (eradication of the patient’s own bone marrow/haemopoietic stem cells or HSCs), and thus create a niche for the incoming graft or gene-corrected stem cells, is highly toxic resulting in gut toxicity (mucositis), liver complications including veno-occlusive disease, alopecia, lung toxicity and haemorrhagic cystitis. There are also a number of common ‘late-onset’ adverse effects attributable to chemo/radiotherapy, such as growth retardation, infertility, cardiotoxicity and secondary malignancy. This is because these conditioning therapies are non-selective, i.e., they affect any dividing cell in the body. The short and long term toxicities of conventional conditioning techniques limits the application of HSCT and gene therapy particularly in the elderly and those with pre-existing organ toxicity as well as in specific subsets of patients who are more sensitive to chemo/radiotherapy e.g., those with DNA or telomere repair disorders. Non-toxic conditioning regimens for HSCT and gene therapy, and similar agents directly applied as therapeutics for haematological cancer, could therefore substantially improve the outlook for patients in a wide range of diseases, and could also widen the applicability of these therapies. The significant expansion of gene therapy as a viable option for a number of genetic diseases has increased the demand for non-toxic conditioning approaches. Accordingly there is a need for an efficacious, non-toxic conditioning approach, to enable transplant or gene therapy that would otherwise not have been carried out using existing chemo/radiotherapy-based conditioning methods, and also in blood cancers where chemotherapy is currently a primary treatment approach. Such agents could be used directly as anti-cancer agents or as part of conditioning prior to allogeneic/autologous HSCT in haematological malignancies (including acute myeloid leukaemia, acute lymphoblastic leukaemia, chronic myeloid leukaemia, chronic lymphocytic leukaemia, myelodysplasia, myeloproliferative diseases, myeloma, non- Hodgkin’s lymphoma and Hodgkin’s disease). There is a particular need in cases of non- immediately life-threatening conditions curable with transplant or gene therapy, or for conditions in which the current conditioning methods are prohibitively toxic. One key indication for antibody- based conditioning will be in allogeneic transplant and gene therapy for non-malignant conditions. For example, only a tiny fraction of patients are currently transplanted to treat haemoglobinopathies, such as sickle cell disease and beta-thalassaemia major, as intensive chemotherapy is a major barrier to treatment. Other potential disease that could be targeted with transplant or gene therapy if an effective non-toxic conditioning regimen was available include primary immunodeficiencies (e.g., SCID (e.g., newborn SCID), chronic granulomatous disease, Wiskott-Aldrich syndrome, CD40L deficiency, XLP, MHC Class II deficiency, primary haemophagocytic lymphohistiocytosis), bone marrow failure syndromes (e.g., idiopathic aplastic anaemia, Fanconi anaemia, dyskeratosis congenita, Shwachman-Diamond Syndrome, severe congenital neutropenia, Diamond-Blackfan anaemia) and genetically based metabolic disorders (e.g., Hurler syndrome, X-linked adrenoleukodystrophy, metachromatic leukodystrophy, Sanfilippo disease, alpha- mannosidosis, osteopetrosis). Finally, these agents could also reduce the toxicity and hence expand the applicability of autologous HSCT for autoimmune diseases, including systemic sclerosis, systemic lupus erythematosus, juvenile inflammatory arthritis and relapsing/remitting multiple sclerosis, for which a non-toxic conditioning regime could be an ‘enabler’ for an entire field. Traditional conditioning regimes and chemotherapies are non-selective; they preferentially target dividing cells over non-dividing cells, but still affect many other cells in the body resulting in severe systemic toxicity. Antibody-based technologies may be useful in selectively targeting and eliminating existing HSCs, with fewer side effects. Since antibodies can be engineered to very selectively target antigens (proteins or other molecules), which are expressed only the surface of bone marrow stem cells and not on other cell types, they may be an effective means of stem cell ablation. Antibodies can perform targeted cell killing, for example, through complement- dependent cytotoxicity (CDC) or using antibody-drug conjugates (ADCs). Three key factors are required in developing a targeted, non-toxic conditioning regime for HSCT and gene therapy: (a) relevant antigens on HSCs to use as targets; (b) efficacious antibody constructs that can produce optimal, targeted HSC cytotoxicity; and (c) short half-life such that they clear from the circulation before the new HSCs are engrafted. Anti-CD45 rat IgG2b Fc antibodies YTH24.5 and YTH54.12 (see WO 1995/013093) were shown to be rapidly cleared from circulation (Krance, R. A., et al. (2003), Biol Blood Marrow Transplant 9(4): 273-281.3). In a clinical study from the present inventors, anti-CD45 antibodies YTH24.5 and YTH54.12, together with Alemtuzumab (an anti-CD52 MAb) were shown to provide an effective a minimal-intensity conditioning regimen in paediatric subjects with PID (Straathof, K. C., et al. (2009), Lancet 374(9693): 912-920.4). WO 2020/146432 exemplifies the use of an anti- CD45 ADC having an amanitin warhead to promote acceptance of CAR-T cell therapy. The present inventors have identified particular anti-CD45 antibodies, and antibody-drug conjugates comprising these antibodies, that provide highly effective, non-toxic conditioning in patients, for HSCT or gene therapy, and for treating blood cancers. SUMMARY OF THE INVENTION The present invention provides a monoclonal antibody or fragment thereof that specifically binds human CD45, comprising a light chain variable domain and a heavy chain variable domain, wherein: (a) the light chain variable domain comprises a light chain complementarity determining region (LCDR) 1, a LCDR2 and a LCDR3, and wherein the heavy chain variable domain comprises a heavy chain complementarity determining region (HCDR) 1, a HCDR2 and a HCDR3, wherein the antibody comprises the complementarity determining region (CDR) sequences of the light chain variable domain sequence SEQ ID NO: 1 and the heavy chain variable domain sequence SEQ ID NO: 2; (b) the light chain variable domain comprises a light chain complementarity determining region (LCDR) 1, a LCDR2 and a LCDR3, and wherein the heavy chain variable domain comprises a heavy chain complementarity determining region (HCDR) 1, a HCDR2 and a HCDR3, wherein LCDR1 comprises the sequence of SEQ ID NO: 3, LCDR2 comprises the sequence of SEQ ID NO: 4, and LCDR3 comprises the sequence of SEQ ID NO: 5, and HCDR1 comprises the sequence of SEQ ID NO: 6, HCDR2 comprises the sequence of SEQ ID NO: 7, and HCDR3 comprises the sequence of SEQ ID NO: 8; (c) the light chain variable domain comprises a sequence of SEQ ID NO: 1, and wherein the heavy chain variable domain comprises a sequence of SEQ ID NO: 2; or (d) the antibody comprises a light chain comprising a sequence of SEQ ID NO: 9 and a heavy chain comprising a sequence of SEQ ID NO: 10. The present invention further provides a monoclonal antibody or fragment thereof that specifically binds human CD45, comprising a light chain variable domain and a heavy chain variable domain, wherein: (a) the light chain variable domain comprises a light chain complementarity determining region (LCDR) 1, a LCDR2 and a LCDR3, and wherein the heavy chain variable domain comprises a heavy chain complementarity determining region (HCDR) 1, a HCDR2 and a HCDR3, wherein the antibody comprises the complementarity determining region (CDR) sequences of the light chain variable domain sequence SEQ ID NO: 11 and the heavy chain variable domain sequence SEQ ID NO: 12; (b) the light chain variable domain comprises a light chain complementarity determining region (LCDR) 1, a LCDR2 and a LCDR3, and wherein the heavy chain variable domain comprises a heavy chain complementarity determining region (HCDR) 1, a HCDR2 and a HCDR3, wherein LCDR1 comprises the sequence of SEQ ID NO: 13, LCDR2 comprises the sequence of SEQ ID NO: 14, and LCDR3 comprises the sequence of SEQ ID NO: 15, and HCDR1 comprises the sequence of SEQ ID NO: 16, HCDR2 comprises the sequence of SEQ ID NO: 17, and HCDR3 comprises the sequence of SEQ ID NO: 18; (c) the light chain variable domain comprises a sequence of SEQ ID NO: 11, and wherein the heavy chain variable domain comprises a sequence of SEQ ID NO: 12; or (d) the antibody comprises a light chain comprising a sequence of SEQ ID NO: 19 and a heavy chain comprising a sequence of SEQ ID NO: 20. The present invention further provides a biparatopic antibody or biparatopic fragment thereof, that specifically binds human CD45, comprising a first antigen binding domain and a second antigen binding domain, wherein: A. (i) the first antigen binding domain comprises a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a LCDR1 comprising the sequence of SEQ ID NO: 3, a LCDR2 comprising the sequence of SEQ ID NO: 4, and a LCDR3 comprising the sequence of SEQ ID NO: 5, and wherein the heavy chain variable domain comprises a HCDR1 comprising the sequence of SEQ ID NO: 6, a HCDR2 comprising the sequence of SEQ ID NO: 7, and a HCDR3 comprising the sequence of SEQ ID NO: 8; and (ii) the second antigen binding domain comprises a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a LCDR1 comprising the sequence of SEQ ID NO: 13, a LCDR2 comprising the sequence of SEQ ID NO: 14, and a LCDR3 comprising the sequence of SEQ ID NO: 15, and wherein the heavy chain variable domain comprises a HCDR1 comprising the sequence of SEQ ID NO: 16, a HCDR2 comprising the sequence of SEQ ID NO: 17, and a HCDR3 comprising the sequence of SEQ ID NO: 18; or B. (i) the first antigen binding domain comprises a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a sequence of SEQ ID NO: 1, and wherein the heavy chain variable domain comprises a sequence of SEQ ID NO: 2; and (ii) the second antigen binding domain comprises a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a sequence of SEQ ID NO: 11, and wherein the heavy chain variable domain comprises a sequence of SEQ ID NO: 12. The present invention further provides a biparatopic antibody or biparatopic fragment thereof, that specifically binds human CD45, comprising a first antigen binding domain and a second antigen binding domain, wherein: A. the first antigen binding domain comprises a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a LCDR1 comprising the sequence of SEQ ID NO: 3, a LCDR2 comprising the sequence of SEQ ID NO: 4, and a LCDR3 comprising the sequence of SEQ ID NO: 5, and wherein the heavy chain variable domain comprises a HCDR1 comprising the sequence of SEQ ID NO: 6, a HCDR2 comprising the sequence of SEQ ID NO: 7, and a HCDR3 comprising the sequence of SEQ ID NO: 8; or B. the first antigen binding domain comprises a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a LCDR1 comprising the sequence of SEQ ID NO: 13, a LCDR2 comprising the sequence of SEQ ID NO: 14, and a LCDR3 comprising the sequence of SEQ ID NO: 15, and wherein the heavy chain variable domain comprises a HCDR1 comprising the sequence of SEQ ID NO: 16, a HCDR2 comprising the sequence of SEQ ID NO: 17, and a HCDR3 comprising the sequence of SEQ ID NO: 18; or C. the first antigen binding domain comprises a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a sequence of SEQ ID NO: 1, and wherein the heavy chain variable domain comprises a sequence of SEQ ID NO: 2; or D. the first antigen binding domain comprises a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a sequence of SEQ ID NO: 11, and wherein the heavy chain variable domain comprises a sequence of SEQ ID NO: 12. The second antigen binding domain may be a CD45 binding domain (i.e., specifically binds CD45) that binds CD45 at an epitope that does not overlap with the binding epitope of the first antigen binding domain. The second antigen binding domain may be a CD45 binding domain that does not compete with the first antigen binding domain for binding to CD45. The second antigen binding domain may be a CD45 binding domain that does not cross-block and/or is not cross-blocked by, the first antigen binding domain in binding to CD45. The first and second antigen binding domains of the biparatopic antibody typically bind at distinct, non-overlapping epitopes on CD45. The second antigen binding domain typically comprises a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a LCDR1, a LCDR2, and a LCDR3, and wherein the heavy chain variable domain comprises a HCDR1, a HCDR2, and a HCDR3. The present invention also provides a biparatopic antibody or biparatopic fragment thereof, comprising a first antigen binding domain that specifically binds human CD45, and a second antigen binding domain that specifically binds human CD45, wherein the first or second antigen binding domain comprises the CDR sequences, or the light and heavy chain variable domain sequences, of an antibody as disclosed herein. The present invention also provides an antibody drug conjugate of formula (I): Ab – (L–D)p (I) wherein Ab is an antibody, or fragment thereof, of the invention; wherein L is a linker connecting Ab to D; wherein D is an anti-cancer agent, a cytotoxic agent or a cytostatic agent; wherein p is from 1 to 8; and wherein D is not a pyrrolobenzodiazepine (PBD). The present invention also provides pharmaceutical compositions comprising the antibodies or antibody drug conjugates of the invention. Further provided are methods of treating haematological cancer, methods of preparing a subject for transplantation of haematopoietic stem cells, and methods of engrafting stem cells in a subject, which utilise the antibodies or antibody drug conjugates of the invention. DESCRIPTION OF THE FIGURES Figure 1: Higher expression levels of CD45 compared to c-Kit on human HSCs. Antigen density per cell is represented by the average number of molecules of each antigen determined using QuantiBRITE PE beads. Levels of c-Kit (left) are shown for the human AML cell line, OCIM1, bulk CD34+ progenitor cells and immunophenotypically defined HSCs, multipotent progenitors (MPPs) and multilymphoid progenitors (MLPs) from G-CSF mobilised peripheral blood of normal donors. Levels of CD45 on peripheral blood mononuclear cells (PBMCs), T cells, bulk CD34+ cells, HSCs, MPPs and MLPs are shown on the right panel. In contrast to c-kit, CD45 antigen density on HSCs is high, making it an attractive candidate for antibody-based conditioning. Figure 2: Anti-CD45 monoclonal antibodies completely prevent colony formation via CDC. Evidence for targeting CD45 as a method of specifically killing HSCs via CDC was shown using a clonogenic in vitro assay , in which CD34+ cells were incubated either with no antibody, an isotype control antibody (which does not cross-react with CD34+ cells) and with the combination of a rat IgG2b antibody having variable domains of SEQ ID NOs 1 and 2 (YTH 24.5; also referred to herein as Ab1) and a rat IgG2b antibody having variable domains of SEQ ID NOs 11 and 12 (YTH 54.12; also referred to herein as Ab2), either without serum (i.e., with no complement proteins) or with serum (i.e., containing complement proteins). The combination of antibodies as applied to HSCs, in the presence of complement proteins in serum completely abrogated cell colony formation, demonstrating potent cytolytic activity against haematopoietic progenitors. Figure 3: Ex vivo treatment of human CD34+ cells with anti-CD45 Mab abrogates engraftment. Human CD34+ cells were incubated with control antibodies or the combination of anti-CD45 Ab1 + Ab2, either in the presence or absence of complement. The cells were then transplanted into NSG (immunodeficient) mice. Pre-incubation of human CD34+ cells with the anti-CD45 antibodies and complement resulted in complete abrogation of engraftment, demonstrating that this antibody combination is highly effective in killing human HSCs through complement mediated cytotoxicity. Figure 4: Anti-human CD45 monoclonal antibodies internalise and are processed via a lysosomal pathway. Live-imaging microscopy was carried out using CD45+ human OCIM1 cells labelled with a lysosomal marker. Substantial co-localisation of anti-CD45 antibodies and lysosomes was observed. This demonstrates that these antibodies are substantially internalised providing the basis for an ADC-based (antibody drug conjugate-based) approach. Figure 5: Schematic showing considerations for development of anti-CD45 antibody drug conjugates. Figure 6: Comparison of clearance rate of rat IgG2b vs human IgG1-AAA anti-CD45 MAbs in NSG mice. Clearance rates following injections of 5mg/kg to NSG mice were compared between rat IgG2b Ab1 and human IgG1-AAA Ab1, and between rat IgG2bAb2 and human IgG1- AAA Ab2. Human IgG1-AAA is a mutant form of human IgG1, which does not bind the human neonatal Fc receptor and therefore confers short in vivo half-life. Monitoring of plasma clearance at an equivalent dose of rat and human-mutant antibodies showed that the anti-CD45 antibodies in the human IgG1-AAA constant region format are cleared from immunodeficient NSG mice quicker than rat IgG2b antibodies, although both formats are cleared relatively rapidly. Figure 7: Exemplary first and second group anti-CD45 antibodies do not cross-react with non-human primate CD45. Binding of rat IgG2b anti-CD45 Ab1 and Ab2 antibodies was tested in the human OCIM1 cell line and in PBMC cells from Rhesus macaque (primate) cells. The rat IgG2b Ab1 and Ab2 antibodies showed no or only very weak binding to non-human primate cells. Figure 8: Data showing the effects of the rat IgG2b Ab1 and Ab2 antibodies with or without anti-rat IgG-saporin. Cell viability assay at 72h using Jurkat cells incubated with anti-CD45 Ab1 and Ab2 or isotype control, with or without anti-rat IgG saporin conjugate. X-axis shows the monoclonal antibody concentration. In the presence of anti-rat IgG saporin both anti-CD45 antibodies are able to efficiently kill CD45+ cell line targets at subnanomolar levels. Figure 9: Specific killing of human CD45+ (OCIM1 and Jurkat) and not human CD45- (Nalm6) cells by anti-CD45-PNU ADCs. Cells were cultured (in triplicate) for 5 days in presence or absence of A) YTH24.5-PNU or MOPC21-PNU and B) YTH54.12-PNU or MOPC21-PNU. Mean cell viability ± s.d. was determined relative to untreated cells. Figure 10: Specific killing of human CD45 + (OCIM1 and Jurkat) and not human CD45- (Nalm6) cells by anti-CD45-Maytansine derivative (May) ADCs. Cells were cultured (in triplicate) for 5 days in presence or absence of A) YTH24.5-May or MOPC21-May and B) YTH54.12-May or MOPC21-May. Mean cell viability ± s.d. was determined relative to untreated cells. Figure 11: Modest killing of human CD45+ (OCIM1 and Jurkat) and not human CD45- (Nalm6) cells by anti-CD45-Dxd ADCs. Cells were cultured (in triplicate) for 5 days in presence or absence of A) YTH24.5-Dxd or MOPC21-Dxd and B) YTH54.12-Dxd or MOPC21-Dxd. Mean cell viability ± s.d. was determined relative to untreated cells. Figure 12: Modest killing of human CD45+ (OCIM1 and Jurkat) and not human CD45- (Nalm6) cells by anti-CD45-Duocarmycin (Duo) ADCs. Cells were cultured (in triplicate) for 5 days in presence or absence of A) YTH24.5-Duo or MOPC21-Duo and B) YTH54.12-Duo or MOPC21-Duo. Mean cell viability ± s.d. was determined relative to untreated cells. Figure 13: Killing of human CD45+ Jurkat but not OCIM1 or human CD45- (Nalm6) cells by anti-CD45-MMAE ADCs. Cells were cultured (in triplicate) for 5 days in presence or absence of A) YTH24.5-MMAE vs MOPC21-MMAE and B) YTH54.12- MMAE vs MOPC21- MMAE. Mean cell viability ± s.d. was determined. Figure 14: Anti-CD45 ADCs specifically inhibit colony formation of healthy donor CD34+ haematopoietic stem and progenitor cells. CD34+ cells were cultured in presence of ADCs for 2 hours before culture in semi-solid medium plus cytokines for 14 days. Total colonies were enumerated and expressed relative to untreated control. A) Anti-CD45-PNU. B) Anti-CD45- Duocarmycin. Mean ± s.d. are plotted. Figure 15: YTH24.5-PNU delays onset of tumour development and prolongs survival in an NSG model of AML. Mice were injected with fLuc+ OCIM1 cells on day 0, followed by antibody or ADC on the following day. Mice were monitored for tumour development. A) Quantification of bioluminescence signal in mice. B) Survival curve for all groups. Figure 16: Generation of a biparatopic anti-CD45 antibody. A) Schematic showing the structure of the V5-CD45 FL and the V5-CD45Δ2 constructs. B) HEK293T cells expressing V5- CD45 FL or V5-CD45Δ2 were stained with monospecific antibodies, YTH54.12-F405L.HA and YTH24.5-S370K-K409R.His, or biparatopic YTH24.5-S370K-K409R.His x YTH54.12-F540L.HA followed by anti-HA-PE-Cy7 and anti-His-APC to differentiate between monospecific or biparatopic binding to GFP+/V5-PE+ cells. DETAILED DESCRIPTION Haematopoietic stem cell transplantation (HSCT) may be curative for subjects with a wide range of malignant (e.g., cancers including acute myeloid leukaemia, acute lymphoblastic leukaemia, Non- Hodgkin’s lymphoma, and myeloma) and non-malignant (e.g. haemoglobinopathies and bone marrow failure) haematological disorders, autoimmune disease (e.g., systemic sclerosis, multiple sclerosis) as well as genetic disorders, such as primary immunodeficiency (PID) and metabolic diseases. It is also increasingly possible to use gene therapy, for example with autologous haematopoietic stem cells (HSCs) virally transduced with a corrected transgene, to treat such genetic disorders. For both HSCT and gene therapy, a conditioning regimen is required to eradicate the subject’s own HSCs and create a niche for the incoming graft, typically HLA- matched donor HSCs. Such conditioning regimens typically use non-targeted approaches such as total body irradiation and broadly toxic chemotherapies. The present antibodies and antibody drug conjugates provide a targeted conditioning approach that selectively ablates the endogenous hematopoietic stem cell population, avoiding non-haematological toxicity. The present invention provides an antibody, or fragment thereof, that specifically binds human CD45. CD45 represents an attractive target for antibodies and corresponding antibody drug conjugates (see e.g., WO 2020/146432) for conditioning, as it is selectively expressed on all leucocytes and haematopoietic progenitors, but is absent on non-haematopoietic tissues (Straathof, K. C., et al., Lancet 2009: 374: 912-20). The present invention relates broadly to two families of antibodies, or fragments thereof, that specifically bind human CD45. Antibodies The term “antibody” as referred to herein includes whole antibodies and any antigen binding fragment (i.e., “antigen-binding portion”) or single chains thereof. An antibody refers to a glycoprotein comprising at least two heavy (H) chains and two light (L) chains inter-connected by disulfide bonds. There are two types of light chain, lambda (λ) and kappa (κ). There are five main heavy chain classes (or isotypes) which determine the functional activity of an antibody molecule: IgM, IgD, IgG, IgA and IgE. The disclosed antibodies can be class switched. Each heavy chain is comprised of a heavy chain variable region (abbreviated herein as VH) and a heavy chain constant region. Each light chain is comprised of a light chain variable region (abbreviated herein as VL) and a light chain constant region. The variable regions of the heavy and light chains contain a binding domain that interacts with an antigen. The VH and VL regions can be further subdivided into regions of hypervariability, termed complementarity determining regions (CDR), interspersed with regions that are more conserved, termed framework regions (FR). The CDRs are primarily responsible for antigen binding. The CDRs of each chain are typically referred to as CDR1, CDR2, and CDR3 (from the N-terminus to C-terminus), and are also typically identified by the chain in which the particular CDR is located. Light chain CDRs can be referred to as LCDR1, LCDR2 and LCDR3. Heavy chain CDRs can be referred to as HCDR1, HCDR2 and HCDR3. The CDR sequences are typically ordered on the light chain variable domain in an N- terminal to C-terminal direction: LCDR1, LCDR2, and LCDR3, and on the heavy chain variable domain in an N-terminal to C-terminal direction: HCDR1, HCDR2, and HCDR3. The sequences of the framework regions of different light or heavy chains are relatively conserved within a species. The framework region of an antibody, that is the combined framework regions of the constituent light and heavy chains, serves to position and align the CDRs in three-dimensional space. The constant regions of the antibodies may mediate the binding of the immunoglobulin to host tissues or factors, including various cells of the immune system (e.g., effector cells) and the first component (Clq) of the classical complement system. An antibody of the invention is preferably a “monoclonal antibody”. Monoclonal antibodies are immunoglobulin molecules that are identical to each other and have a single binding specificity and affinity for a particular epitope. Monoclonal antibodies (mAbs) of the present invention can be produced by a variety of techniques, including conventional monoclonal antibody methodology, for example those disclosed in “Monoclonal Antibodies; A manual of techniques”, H Zola (CRC Press, 1988) and in “Monoclonal Hybridoma Antibodies: Techniques and Application”, SGR Hurrell (CRC Press, 1982). The term “fragment” of an antibody, typically refers to an “antigen-binding fragment” of said antibody, i.e., one or more fragments of an antibody that retain the ability to specifically bind to an antigen. The present antibody fragments retain the ability to specifically bind to human CD45. Examples of antigen-binding fragments of an antibody include a Fab, a Fab', a F(ab)' ₂ , a Fd, a Fv, a single chain Fab (scFab), a single chain Fv protein (scFv), a tandem scFv protein, a disulfide stabilized Fv protein (dsFv), or a scFv-Fc protein. The antibody fragments of the invention include a Fab, a Fab', a F(ab)' ₂ , a Fd, a Fv, a single chain Fab (scFab), a single chain Fv protein (scFv), a tandem scFv protein, a disulfide stabilized Fv protein (dsFv), or a scFv-Fc protein that specifically binds human CD45. These antibody fragments may be obtained using conventional techniques known to those of skill in the art. For example, antibody fragments can be produced by the modification of whole antibodies or synthesized de novo using recombinant DNA methodologies. The term "binding affinity" refers to the tendency of an antibody molecule to bind or not to bind to a target. Binding affinity may be quantified by determining the dissociation constant (Kd) for an antibody and its target. Similarly, the specificity of binding of an antibody to its target may be defined in terms of the comparative dissociation constants (Kd) of the antibody for its target as compared to the dissociation constant with respect to the antibody and another, non-target molecule. Typically, the Kd for the antibody with respect to the target will be 2-fold, preferably 5- fold, more preferably 10-fold less than Kd with respect to the other, non-target molecule. More preferably, the Kd will be 50- fold less, even more preferably 100-fold less, and yet more preferably 200-fold less. The value of this dissociation constant can be determined directly by well-known methods, and can be computed even for complex mixtures by methods such as those, for example, set forth in Caceci et al. (Byte 9:340-362, 1984). Methods for the evaluation of binding affinity of the antibodies of the invention for CD45 preferably include ELISA or Biacore (i.e., surface plasmon resonance). An antibody of the invention binds (e.g., specifically binds) to human CD45, that is preferably they bind to human CD45 but they do not bind, or bind at a lower affinity, to other molecules. “Specifically binding” means that an antibody binds to human CD45 with greater affinity than to another target. An antibody of the invention is preferably capable of binding to human CD45 with an affinity that is at least two-fold, 10-fold, 50-fold, 100-fold or greater than its affinity for binding to another non-target molecule. Preferably, an antibody of the invention may have a binding affinity (i.e., K _D ) for human CD45 of 1 x10 ^-9 M or less. In some aspects, the monoclonal antibodies specifically bind human CD45 with a KD of about 1 x10 ^-9 M or less, about 1 x 10 ^-10 M or less, about 1 x 10 ^-11 M or less, or about 1 x 10 ^-12 M or less. The sequence of human CD45 is set out in SEQ ID NO: 37. An antibody of the present invention may have some binding affinity for CD45 from other mammals, for example primate or murine e.g. mouse or rat CD45. The binding affinity of the antibodies of the invention for CD45 from other species becomes progressively weaker as the binding epitope becomes less conserved with phylogenetic distance. The monoclonal antibodies preferably bind (e.g., specifically bind) to the extracellular domain of human CD45. The sequence of the extracellular domain of human CD45 is set out in SEQ ID NO: 38. The antibodies are capable of binding to human CD45 on the surface of human hematopoietic cells. An antibody of the invention typically binds to the same epitope as the antibody having heavy and light chain variable region sequences of SEQ ID NOs 1 and 2 or SEQ ID NOs 11 and 12, respectively; preferably having heavy and light chain sequences of SEQ ID NOs 9 and 10 or SEQ ID NOs 19 and 20, respectively. As used herein, the term "epitope" generally refers to the site on a target antigen which is recognised by the antibody. The location of an epitope may be identified by routine methods. For example, the general location of an epitope may be determined by assessing the ability of an antibody to bind to different fragments or variant CD45 polypeptides, and for example by measuring binding following mutagenesis of particular residues in CD45. Additionally, the antibody and target molecule may be combined and the antibody/target complex may be crystallised. The crystal structure of the complex may be determined and used to identify specific sites of interaction between the antibody and its target. An antibody of the invention may cross-compete for binding to human CD45 with another antibody of the invention, preferably an antibody having heavy and light chain variable region sequences of SEQ ID NOs 1 and 2, or SEQ ID NOs 11 and 12, respectively; or the antibody having heavy and light chain sequences of SEQ ID NOs 9 and 10, or SEQ ID NOs 19 and 20, respectively. Such cross-competing antibodies can be identified based on their ability to cross-compete with a known antibody of the invention in standard binding assays, such as Biacore analysis, ELISA assays and flow cytometry. The present invention relates broadly to two families of antibodies, or fragment thereof, that specifically bind human CD45. In some aspects, the antibody comprises a light chain variable domain comprising a LCDR1, a LCDR2 and a LCDR3, and a heavy chain variable domain comprising a HCDR1, a HCDR2 and a HCDR3, wherein the antibody comprises the CDR sequences of the light chain variable domain sequence SEQ ID NO: 1 and the heavy chain variable domain sequence SEQ ID NO: 2. Typically, the antibody comprises all six CDR sequences of SEQ ID NO: 1 and SEQ ID NO: 2, preferably the CDR sequences will be arranged as in SEQ ID NOs 1 and 2 on the light and heavy chains of the antibody and in the same order from N- to C- termini. In some other aspects, the antibody comprises a light chain variable domain comprising a LCDR1, a LCDR2 and a LCDR3, and a heavy chain variable domain comprising a HCDR1, a HCDR2 and a HCDR3, wherein the antibody comprises the CDR sequences of the light chain variable domain sequence SEQ ID NO: 11 and the heavy chain variable domain sequence SEQ ID NO: 12. Typically, the antibody comprises all six CDR sequences of SEQ ID NO: 11 and SEQ ID NO: 12, preferably the CDR sequences will be arranged as in SEQ ID NOs 11 and 12 on the light and heavy chains of the antibody and in the same order from N- to C- termini. The CDRs of SEQ ID NOs 1 and 2 (i.e., the CDR sequences found within the heavy and light chain sequences of SEQ ID NOs 1 and 2), or the CDRs of SEQ ID NOs 11 and 12 (i.e., the CDR sequences found within the heavy and light chain sequences of SEQ ID NOs 11 and 12), may be identified by any suitable method known in the art, for example using any suitable antibody numbering scheme. In some aspects the CDRs are identified using any of the Kabat numbering scheme (Kabat et al., U.S. Department of Health and Human Services, 1991), the Chothia numbering scheme (Chothia C, Lesk A M. J Mol Biol. (1987) 196:901-17), or the IMGT numbering scheme (Giudicelli V, et al. Nucleic Acids Res. (1997) 25:206-11; Lefranc MP. Immunol Today (1997) 18:509). The skilled person will appreciate that these different CDR labelling systems can give slightly different results, but in each case the CDRs can be easily identified by the skilled person. The CDR sequences set out in SEQ ID NOs 3-8 are the LCDR1-3 and HCDR1-3 sequences of SEQ ID NOs 1 and 2 as defined using the Kabat numbering scheme. The CDR sequences set out in SEQ ID NOs 13-18 are the LCDR1-3 and HCDR1-3 sequences of SEQ ID NOs 11 and 12 as defined using the Kabat numbering scheme. Sequence identity, including determination of sequence complementarity for nucleic acid or polynucleotide sequences, may be determined by sequence comparison and alignment algorithms known in the field. To determine the percent identity of two nucleic acid sequences (or polynucleotide sequences), the sequences are aligned for optimal comparison purposes (e.g., gaps can be introduced in the first sequence or second sequence for optimal alignment). The nucleotides at corresponding nucleotide positions are then compared. When a position in the first sequence is occupied by the same residue as the corresponding position in the second sequence, then the molecules are identical at that position. The percent identity between the two sequences is a function of the number of identical positions shared by the sequences (i.e., % homology= # of identical positions/total # of positions*100), optionally penalizing the score for the number of gaps introduced and/or length of gaps introduced. The comparison of sequences and determination of percent identity between two sequences can be accomplished using a mathematical algorithm. In one embodiment, the alignment generated over a certain portion of the sequence aligned having sufficient identity but not over portions having low degree of identity (i.e., a local alignment). A preferred, non-limiting example of a local alignment algorithm utilised for the comparison of sequences is the algorithm of Karlin and Altschul (1990) Proc. Natl. Acad. Sci. USA 87:2264-68, modified as in Karlin and Altschul (1993) Proc. Natl. Acad. Sci. USA 90:5873-77. Such an algorithm is incorporated into the BLAST programs (version 2.0) of Altschul, et al. (1990) J. Mol. Biol.215:403-10. In another embodiment, the alignment is optimised by introducing appropriate gaps and percent identity is determined over the length of the aligned sequences (i.e., a gapped alignment). To obtain gapped alignments for comparison purposes, Gapped BLAST can be utilized as described in Altschul et al., (1997) Nucleic Acids Res.25(17):3389-3402. In another embodiment, the alignment is optimised by introducing appropriate gaps and percent identity is determined over the entire length of the sequences aligned (i.e., a global alignment). A preferred, non-limiting example of a mathematical algorithm utilized for the global comparison of sequences is the algorithm of Myers and Miller, CABIOS (1989). Such an algorithm is incorporated into the ALIGN program (version 2.0) which is part of the GCG sequence alignment software package. A “polypeptide” is used herein in its broadest sense to refer to a compound of two or more subunit amino acids, amino acid analogs, or other peptidomimetics. The term “polypeptide” thus includes short peptide sequences and also longer polypeptides and proteins. As used herein, the term “amino acid” refers to either natural and/or unnatural or synthetic amino acids, including glycine and both the D or L optical isomers, and amino acid analogs and peptidomimetics. An antibody of the invention may alternatively comprise a variant of one or more of the specified sequences. A ‘variant’ may be a substitution, deletion or addition variant of any of the above amino acid sequences. A variant antibody may comprise 1, 2, 3, 4, 5, up to 10, up to 20, up to 30 or more amino acid substitutions and/or deletions from the specific sequences and fragments discussed above, whilst maintaining the activity of the antibodies described herein. “Deletion” variants may comprise the deletion of, for example, 1, 2, 3, 4 or 5 individual amino acids. "Substitution" variants preferably involve the replacement of one or more amino acids with the same number of amino acids and making conservative amino acid substitutions. For example, an amino acid may be substituted with an alternative amino acid having similar properties, for example, another basic amino acid, another acidic amino acid, another neutral amino acid, another charged amino acid, another hydrophilic amino acid, another hydrophobic amino acid, another polar amino acid, another aromatic amino acid or another aliphatic amino acid. Some properties of the 20 main amino acids which can be used to select suitable substituents are as follows: Preferred "derivatives" or "variants" include those in which instead of the naturally occurring amino acid the amino acid which appears in the sequence is a structural analog thereof. Amino acids used in the sequences may also be derivatized or modified, e.g. labelled, providing the function of the antibody is not significantly adversely affected. Derivatives and variants as described above may be prepared during synthesis of the antibody or by post- production modification, or when the antibody is in recombinant form using the known techniques of site- directed mutagenesis, random mutagenesis, or enzymatic cleavage and/or ligation of nucleic acids. Specifically, in some aspects the invention provides cysteine-modified variants of the antibodies described herein, for example wherein one or more amino acid residues within the antibody sequence are each substituted with cysteine. In some aspects 1, 2, 3, 4, 5, 6, 7, 8, or more amino acid residues within the antibody sequence are each substituted with cysteine, preferably 2-8, more preferably 4-8, most preferably 4 amino acid residues within the antibody sequence are each substituted with cysteine. First antibody group (exemplary antibody YTH 24.5 (WO1995/013093); also referred to herein as Ab1) In some aspects where the antibody comprises the CDR sequences of the light chain variable domain sequence SEQ ID NO: 1 and the heavy chain variable domain sequence SEQ ID NO: 2, the antibody may comprise the CDR sequences of SEQ ID NOs: 3, 4, 5, 6, 7 and 8. These CDR sequences are defined using the Kabat numbering scheme. As will be appreciated by the skilled person, the exact CDR sequences may differ depending on the numbering scheme used (e.g., Kabat, Chothia or IMGT). In some preferred aspects, an antibody of the invention comprises a light chain variable domain comprising a LCDR1, a LCDR2 and a LCDR3, and a heavy chain variable domain comprising a HCDR1, a HCDR2 and a HCDR3, wherein LCDR1 comprises the sequence of SEQ ID NO: 3, LCDR2 comprises the sequence of SEQ ID NO: 4, and LCDR3 comprises the sequence of SEQ ID NO: 5, and HCDR1 comprises the sequence of SEQ ID NO: 6, HCDR2 comprises the sequence of SEQ ID NO: 7, and HCDR3 comprises the sequence of SEQ ID NO: 8. Even more preferably, the antibody comprises a light chain variable domain comprising a LCDR1, a LCDR2 and a LCDR3, and a heavy chain variable domain comprising a HCDR1, a HCDR2 and a HCDR3, wherein LCDR1 consists of the sequence of SEQ ID NO: 3, LCDR2 consists of the sequence of SEQ ID NO: 4, and LCDR3 consists of the sequence of SEQ ID NO: 5, and HCDR1 consists of the sequence of SEQ ID NO: 6, HCDR2 consists of the sequence of SEQ ID NO: 7, and HCDR3 consists of the sequence of SEQ ID NO: 8. In addition to the CDR sequence described herein, the light and heavy chain variable regions of the antibodies may comprise framework regions. Specifically the light chain variable region may comprise a light chain framework region (LCFR) 1, a LCFR2, a LCFR3, and an LCFR4 arranged from N- to C-terminus on the light chain variable domain; and the heavy chain variable region may comprise a heavy chain framework region (HCFR) 1, a HCFR2, a HCFR3, and an HCFR4 arranged from N- to C-terminus on the heavy chain variable domain. Typically, LCFR1 is N- terminal of LCDR1, LCFR2 is between LCDR1 and LCDR2, LCFR3 is between LCDR2 and LCDR3, and LCFR4 is C-terminal of LCDR3. Typically, HCFR1 is N-terminal of HCDR1, HCFR2 is between HCDR1 and HCDR2, HCFR3 is between HCDR2 and HCDR3, and HCFR4 is C-terminal of HCDR3. In the antibody of the invention, the light chain variable domain may comprise a LCFR1 comprising a sequence having at least 80%, at least 90%, or preferably at least 95%, sequence identity to SEQ ID NO: 21; an LCFR2 comprising a sequence having at least 80%, at least 90%, or preferably at least 95%, sequence identity to SEQ ID NO: 22; an LCFR3 comprising a sequence having at least 80%, at least 90%, or preferably at least 95%, sequence identity to SEQ ID NO: 23; and an LCFR4 comprising a sequence having at least 80%, at least 90%, or preferably at least 95%, sequence identity to SEQ ID NO: 24. In the antibody of the invention, the light chain variable domain may comprise a LCFR1 comprising the sequence of SEQ ID NO: 21; an LCFR2 comprising the sequence of SEQ ID NO: 22; an LCFR3 comprising the sequence of SEQ ID NO: 23; and an LCFR4 comprising the sequence of SEQ ID NO: 24, wherein the LCFR sequence may comprise up to 10 amino acid substitutions, additions or deletions. In the antibody of the invention, the heavy chain variable domain may comprise a HCFR1 comprising a sequence having at least 80%, at least 90%, or preferably at least 95%, sequence identity to SEQ ID NO: 25; an HCFR2 comprising a sequence having at least 80%, at least 90%, or preferably at least 95%, sequence identity to SEQ ID NO: 26; an HCFR3 comprising a sequence having at least 80%, at least 90%, or preferably at least 95%, sequence identity to SEQ ID NO: 27; and an HCFR4 comprising a sequence having at least 80%, at least 90%, or preferably at least 95%, sequence identity to SEQ ID NO: 28. In the antibody of the invention, the light chain variable domain may comprise a HCFR1 comprising the sequence of SEQ ID NO: 25; an HCFR2 comprising the sequence of SEQ ID NO: 26; an HCFR3 comprising the sequence of SEQ ID NO: 27; and an HCFR4 comprising the sequence of SEQ ID NO: 28, wherein the HCFR sequence may comprise up to 10 amino acid substitutions, additions or deletions. The antibody or fragment thereof may comprise a light chain variable domain that comprises a sequence having at least 80%, at least 85%, at least 90%, preferably at least 95%, or most preferably at least 98% sequence identity to SEQ ID NO: 1. The antibody or fragment thereof may comprise a heavy chain variable domain that comprises a sequence having at least 80%, at least 85%, at least 90%, preferably at least 95%, or most preferably at least 98% sequence identity to SEQ ID NO: 2. In some aspects the antibody or fragment thereof comprises a light chain variable domain that comprises a sequence having at least 95% sequence identity to SEQ ID NO: 1, and a heavy chain variable domain that comprises a sequence having at least 95% sequence identity to SEQ ID NO: 2. In some aspects, the antibody or fragment thereof comprises a light chain variable domain that consists of a sequence of SEQ ID NO: 1, and a heavy chain variable domain that consists of a sequence of SEQ ID NO: 2. In some aspects, an antibody of the invention comprises a light chain variable domain comprising a LCDR1, a LCDR2 and a LCDR3, and a heavy chain variable domain comprising a HCDR1, a HCDR2 and a HCDR3, wherein LCDR1 comprises the sequence of SEQ ID NO: 3, LCDR2 comprises the sequence of SEQ ID NO: 4, and LCDR3 comprises the sequence of SEQ ID NO: 5, and HCDR1 comprises the sequence of SEQ ID NO: 6, HCDR2 comprises the sequence of SEQ ID NO: 7, and HCDR3 comprises the sequence of SEQ ID NO: 8; and wherein the light chain variable domain comprises, or consists of, a sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, preferably at least 95 %, most preferably at least 98%, sequence identity to SEQ ID NO: 1. In some aspects, an antibody of the invention comprises a light chain variable domain comprising a LCDR1, a LCDR2 and a LCDR3, and a heavy chain variable domain comprising a HCDR1, a HCDR2 and a HCDR3, wherein LCDR1 comprises the sequence of SEQ ID NO: 3, LCDR2 comprises the sequence of SEQ ID NO: 4, and LCDR3 comprises the sequence of SEQ ID NO: 5, and HCDR1 comprises the sequence of SEQ ID NO: 6, HCDR2 comprises the sequence of SEQ ID NO: 7, and HCDR3 comprises the sequence of SEQ ID NO: 8; and wherein the heavy chain variable domain comprises, or consists of, a sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, preferably at least 95 %, most preferably at least 98%, sequence identity to SEQ ID NO: 2. In some preferred aspects, an antibody of the invention comprises a light chain variable domain comprising a LCDR1, a LCDR2 and a LCDR3, and a heavy chain variable domain comprising a HCDR1, a HCDR2 and a HCDR3, wherein LCDR1 comprises the sequence of SEQ ID NO: 3, LCDR2 comprises the sequence of SEQ ID NO: 4, and LCDR3 comprises the sequence of SEQ ID NO: 5, and HCDR1 comprises the sequence of SEQ ID NO: 6, HCDR2 comprises the sequence of SEQ ID NO: 7, and HCDR3 comprises the sequence of SEQ ID NO: 8; wherein the light chain variable domain comprises, or consists of, a sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, preferably at least 95 %, most preferably at least 98%, sequence identity to SEQ ID NO: 1; and wherein the heavy chain variable domain comprises, or consists of, a sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, preferably at least 95 %, most preferably at least 98%, sequence identity to SEQ ID NO: 2. The antibody or fragment thereof may comprise a light chain variable domain that comprises, or consists of, a sequence of SEQ ID NO: 1. The antibody or fragment thereof may comprise a heavy chain variable domain that comprises, or consists of, a sequence of SEQ ID NO: 2. In some aspects the antibody or fragment thereof comprises a light chain variable domain that comprises a sequence of SEQ ID NO: 1, and a heavy chain variable domain that comprises a sequence of SEQ ID NO: 2. In some aspects, the antibody or fragment thereof comprises a light chain variable domain that consists of a sequence of SEQ ID NO: 1, and a heavy chain variable domain that consists of a sequence of SEQ ID NO: 2. In some aspects the antibody or fragment thereof comprises a light chain comprising a sequence have at least 80%, at least 90%, preferably at least 95%, most preferably at least 98% sequence identity to SEQ ID NO: 9. In some aspects the antibody or fragment thereof comprises a heavy chain comprising a sequence have at least 80%, at least 90%, preferably at least 95%, most preferably at least 98% sequence identity to SEQ ID NO: 10. In some aspects the antibody or fragment thereof comprises a light chain comprising a sequence have at least 80%, at least 90%, preferably at least 95%, most preferably at least 98% sequence identity to SEQ ID NO: 9; and a heavy chain comprising a sequence have at least 80%, at least 90%, preferably at least 95%, most preferably at least 98% sequence identity to SEQ ID NO: 10. In some aspects the antibody or fragment thereof comprises a light chain comprising a sequence of SEQ ID NO: 9. In some aspects the antibody or fragment thereof comprises a heavy chain comprising a sequence of SEQ ID NO: 10. In some aspects the antibody or fragment thereof comprises a light chain comprising a sequence of SEQ ID NO: 9 and a heavy chain comprising a sequence of SEQ ID NO: 10. In some aspects the antibody or fragment thereof comprises a light chain consisting of a sequence of SEQ ID NO: 9. In some aspects the antibody or fragment thereof comprises a heavy chain consisting of a sequence of SEQ ID NO: 10. In some aspects the antibody or fragment thereof comprises a light chain consisting of a sequence of SEQ ID NO: 9 and a heavy chain consisting of a sequence of SEQ ID NO: 10. Second antibody group (exemplary antibody YTH 54.12 (WO1995/013093); also referred to herein as Ab2) In some aspects where the antibody comprises the CDR sequences of the light chain variable domain sequence SEQ ID NO: 11 and the heavy chain variable domain sequence SEQ ID NO: 12, the antibody may comprise the CDR sequences of SEQ ID NOs: 13, 14, 15, 16, 17 and 18. These CDR sequences are defined using the Kabat numbering scheme. As will be appreciated by the skilled person, the exact CDR sequences may differ depending on the numbering scheme used (e.g., Kabat, Chothia or IMGT). In some preferred aspects, an antibody of the invention comprises a light chain variable domain comprising a LCDR1, a LCDR2 and a LCDR3, and a heavy chain variable domain comprising a HCDR1, a HCDR2 and a HCDR3, wherein LCDR1 comprises the sequence of SEQ ID NO: 13, LCDR2 comprises the sequence of SEQ ID NO: 14, and LCDR3 comprises the sequence of SEQ ID NO: 15, and HCDR1 comprises the sequence of SEQ ID NO: 16, HCDR2 comprises the sequence of SEQ ID NO: 17, and HCDR3 comprises the sequence of SEQ ID NO: 18. Even more preferably, the antibody comprises a light chain variable domain comprising a LCDR1, a LCDR2 and a LCDR3, and a heavy chain variable domain comprising a HCDR1, a HCDR2 and a HCDR3, wherein LCDR1 consists of the sequence of SEQ ID NO: 13, LCDR2 consists of the sequence of SEQ ID NO: 14, and LCDR3 consists of the sequence of SEQ ID NO: 15, and HCDR1 consists of the sequence of SEQ ID NO: 16, HCDR2 consists of the sequence of SEQ ID NO: 17, and HCDR3 consists of the sequence of SEQ ID NO: 18. In addition to the CDR sequence described herein, the light and heavy chain variable regions of the antibodies may comprise framework regions. Specifically the light chain variable region may comprise a light chain framework region (LCFR) 1, a LCFR2, a LCFR3, and an LCFR4 arranged from N- to C-terminus on the light chain variable domain; and the heavy chain variable region may comprise a heavy chain framework region (HCFR) 1, a HCFR2, a HCFR3, and an HCFR4 arranged from N- to C-terminus on the heavy chain variable domain. Typically, LCFR1 is N- terminal of LCDR1, LCFR2 is between LCDR1 and LCDR2, LCFR3 is between LCDR2 and LCDR3, and LCFR4 is C-terminal of LCDR3. Typically, HCFR1 is N-terminal of HCDR1, HCFR2 is between HCDR1 and HCDR2, HCFR3 is between HCDR2 and HCDR3, and HCFR4 is C-terminal of HCDR3. In the antibody of the invention, the light chain variable domain may comprise a LCFR1 comprising a sequence having at least 80%, at least 90%, or preferably at least 95%, sequence identity to SEQ ID NO: 29; an LCFR2 comprising a sequence having at least 80%, at least 90%, or preferably at least 95%, sequence identity to SEQ ID NO: 30; an LCFR3 comprising a sequence having at least 80%, at least 90%, or preferably at least 95%, sequence identity to SEQ ID NO: 31; and an LCFR4 comprising a sequence having at least 80%, at least 90%, or preferably at least 95%, sequence identity to SEQ ID NO: 32. In the antibody of the invention, the light chain variable domain may comprise a LCFR1 comprising the sequence of SEQ ID NO: 29; an LCFR2 comprising the sequence of SEQ ID NO: 30; an LCFR3 comprising the sequence of SEQ ID NO: 31; and an LCFR4 comprising the sequence of SEQ ID NO: 32, wherein the LCFR sequence may comprise up to 10 amino acid substitutions, additions or deletions. In the antibody of the invention, the heavy chain variable domain may comprise a HCFR1 comprising a sequence having at least 80%, at least 90%, or preferably at least 95%, sequence identity to SEQ ID NO: 33; an HCFR2 comprising a sequence having at least 80%, at least 90%, or preferably at least 95%, sequence identity to SEQ ID NO: 34; an HCFR3 comprising a sequence having at least 80%, at least 90%, or preferably at least 95%, sequence identity to SEQ ID NO: 35; and an HCFR4 comprising a sequence having at least 80%, at least 90%, or preferably at least 95%, sequence identity to SEQ ID NO: 36. In the antibody of the invention, the light chain variable domain may comprise a HCFR1 comprising the sequence of SEQ ID NO: 33; an HCFR2 comprising the sequence of SEQ ID NO: 34; an HCFR3 comprising the sequence of SEQ ID NO: 35; and an HCFR4 comprising the sequence of SEQ ID NO: 36, wherein the HCFR sequence may comprise up to 10 amino acid substitutions, additions or deletions. The antibody or fragment thereof may comprise a light chain variable domain that comprises a sequence having at least 80%, at least 85%, at least 90%, preferably at least 95%, or most preferably at least 98% sequence identity to SEQ ID NO: 11. The antibody or fragment thereof may comprise a heavy chain variable domain that comprises a sequence having at least 80%, at least 85%, at least 90%, preferably at least 95%, or most preferably at least 98% sequence identity to SEQ ID NO: 12. In some aspects the antibody or fragment thereof comprises a light chain variable domain that comprises a sequence having at least 95% sequence identity to SEQ ID NO: 11, and a heavy chain variable domain that comprises a sequence having at least 95% sequence identity to SEQ ID NO: 12. In some aspects, the antibody or fragment thereof comprises a light chain variable domain that consists of a sequence of SEQ ID NO: 11, and a heavy chain variable domain that consists of a sequence of SEQ ID NO: 12. In some aspects, an antibody of the invention comprises a light chain variable domain comprising a LCDR1, a LCDR2 and a LCDR3, and a heavy chain variable domain comprising a HCDR1, a HCDR2 and a HCDR3, wherein LCDR1 comprises the sequence of SEQ ID NO: 13, LCDR2 comprises the sequence of SEQ ID NO: 14, and LCDR3 comprises the sequence of SEQ ID NO: 15, and HCDR1 comprises the sequence of SEQ ID NO: 16, HCDR2 comprises the sequence of SEQ ID NO: 17, and HCDR3 comprises the sequence of SEQ ID NO: 18; and wherein the light chain variable domain comprises, or consists of, a sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, preferably at least 95 %, most preferably at least 98%, sequence identity to SEQ ID NO: 11. In some aspects, an antibody of the invention comprises a light chain variable domain comprising a LCDR1, a LCDR2 and a LCDR3, and a heavy chain variable domain comprising a HCDR1, a HCDR2 and a HCDR3, wherein LCDR1 comprises the sequence of SEQ ID NO: 13, LCDR2 comprises the sequence of SEQ ID NO: 14, and LCDR3 comprises the sequence of SEQ ID NO: 15, and HCDR1 comprises the sequence of SEQ ID NO: 16, HCDR2 comprises the sequence of SEQ ID NO: 17, and HCDR3 comprises the sequence of SEQ ID NO: 18; and wherein the heavy chain variable domain comprises, or consists of, a sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, preferably at least 95 %, most preferably at least 98%, sequence identity to SEQ ID NO: 12. In some preferred aspects, an antibody of the invention comprises a light chain variable domain comprising a LCDR1, a LCDR2 and a LCDR3, and a heavy chain variable domain comprising a HCDR1, a HCDR2 and a HCDR3, wherein LCDR1 comprises the sequence of SEQ ID NO: 13, LCDR2 comprises the sequence of SEQ ID NO: 14, and LCDR3 comprises the sequence of SEQ ID NO: 15, and HCDR1 comprises the sequence of SEQ ID NO: 16, HCDR2 comprises the sequence of SEQ ID NO: 17, and HCDR3 comprises the sequence of SEQ ID NO: 18; wherein the light chain variable domain comprises, or consists of, a sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, preferably at least 95 %, most preferably at least 98%, sequence identity to SEQ ID NO: 11; and wherein the heavy chain variable domain comprises, or consists of, a sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, preferably at least 95 %, most preferably at least 98%, sequence identity to SEQ ID NO: 12. The antibody or fragment thereof may comprise a light chain variable domain that comprises, or consists of, a sequence of SEQ ID NO: 11. The antibody or fragment thereof may comprise a heavy chain variable domain that comprises, or consists of, a sequence of SEQ ID NO: 12. In some aspects the antibody or fragment thereof comprises a light chain variable domain that comprises a sequence of SEQ ID NO: 11, and a heavy chain variable domain that comprises a sequence of SEQ ID NO: 12. In some aspects, the antibody or fragment thereof comprises a light chain variable domain that consists of a sequence of SEQ ID NO: 11, and a heavy chain variable domain that consists of a sequence of SEQ ID NO: 12. In some aspects the antibody or fragment thereof comprises a light chain comprising a sequence have at least 80%, at least 90%, preferably at least 95%, most preferably at least 98% sequence identity to SEQ ID NO: 19. In some aspects the antibody or fragment thereof comprises a heavy chain comprising a sequence have at least 80%, at least 90%, preferably at least 95%, most preferably at least 98% sequence identity to SEQ ID NO: 20. In some aspects the antibody or fragment thereof comprises a light chain comprising a sequence have at least 80%, at least 90%, preferably at least 95%, most preferably at least 98% sequence identity to SEQ ID NO: 19; and a heavy chain comprising a sequence have at least 80%, at least 90%, preferably at least 95%, most preferably at least 98% sequence identity to SEQ ID NO: 20. In some aspects the antibody or fragment thereof comprises a light chain comprising a sequence of SEQ ID NO: 19. In some aspects the antibody or fragment thereof comprises a heavy chain comprising a sequence of SEQ ID NO: 20. In some aspects the antibody or fragment thereof comprises a light chain comprising a sequence of SEQ ID NO: 19 and a heavy chain comprising a sequence of SEQ ID NO: 20. In some aspects the antibody or fragment thereof comprises a light chain consisting of a sequence of SEQ ID NO: 19. In some aspects the antibody or fragment thereof comprises a heavy chain consisting of a sequence of SEQ ID NO: 20. In some aspects the antibody or fragment thereof comprises a light chain consisting of a sequence of SEQ ID NO: 19 and a heavy chain consisting of a sequence of SEQ ID NO: 20. Other features of the antibodies of the invention In some aspects the antibodies of the invention are advantageously adapted so that when administered to a subject, preferably a human patient, in need thereof, they are rapidly cleared from the subject’s system, in order to minimise the residual toxicity to any CD45-positive cells that may subsequently administered to the subject, for example as part of the treatment regime. Thus, the antibodies of the invention may have a short half-life in the subject of interest, preferably a human subject. In some aspects the antibody or fragment thereof may comprise a constant region. In some aspects the antibody or fragment thereof may comprise a full-length constant region. The monoclonal antibody can be of any isotype. The antibody may be, for example, IgA1, IgA2, IgD, IgE, IgG1, IgG2, IgG3, IgG4 or IgM. Preferably, the antibody may be an IgM or an IgG antibody. Most preferably, the antibody may be an IgG1, an IgG2 or an IgG3 antibody. In some aspects the antibody is a full-length antibody. The antibody may be a non-human antibody. The antibody may be a rodent antibody, i.e., a rat or mouse antibody. The antibody may be a monkey antibody. In some aspects the antibody is a rat IgG2 antibody, more preferably a rat IgG2b antibody. Such non-human antibodies, preferably rat antibodies, have the advantage that they result in rapid clearance of the antibody from the system of human subjects, as described above. In some aspects where the antibody is a biparatopic or bispecific antibody as described herein, the antibody may be a human isotype hybrid antibody (such as for example, a human IgG2/IgG4 hybrid antibody) or a rat/mouse hybrid antibody (such as for example, a mouse IgG2a/rat IgG2b hybrid antibody). The antibody may be a humanised antibody. A “humanised” antibody is an antibody including a human framework region and one or more CDRs from a non-human antibody (e.g., a monkey, mouse, rat, or synthetic antibody). The non-human antibody providing the CDRs is the “donor”, and the human antibody providing the framework is the “acceptor”. Preferably, all six CDR sequences in the humanised antibody are from the donor antibody. The humanised antibody may not comprise a constant region. If constant regions are present in the humanised antibody they are typically substantially identical to human antibody constant regions, such as having at least 85%, at least 90%, at least 95%, at least 98%, or about 100% sequence identity with a human constant region; preferably having at least 90%, or most preferably having at least 95%, sequence identity with a human constant region. Thus, in preferred aspects all parts of a humanised antibody, except the CDRs, are substantially identical to (i.e., have at least 90% and preferably at least 95% sequence identity with) corresponding parts of natural human antibody sequences. A “humanised antibody” can include a humanised light chain and a humanised heavy chain. A humanised antibody binds to the same antigen as the donor antibody that provides the CDRs. The acceptor framework of a humanised antibody may have a limited number of substitutions (typically between about 1-50, 1-40, 1-30, 1- 20, 1-10 or 1-5 substitutions, preferably 1-20 and most preferably 1-10 substitutions) with amino acids taken from the donor framework. Humanised or other monoclonal antibodies can have additional conservative amino acid substitutions which have substantially no effect on antigen binding or other immunoglobulin functions. Humanised immunoglobulins can be constructed by means of genetic engineering (for example, see U.S. Patent No. 5,585,089). In some aspects, the antibodies of the present invention are humanised. In some aspects the antibody is a humanised antibody and comprises one or more human framework regions. The antibody may be a chimeric antibody. A “chimeric” antibody is an antibody that includes sequences from two different antibodies, which typically are of different species. For example, a chimeric antibody may comprise heavy and light chain variable regions derived from a first species and heavy and light chain constant regions derived from a second species. In other aspects, the variable and constant regions of the light chain may be derived from a first species while the variable region of the heavy chain may be derived from the first species and the constant region of the heavy chain is derived from a second species. In other aspects, the variable and constant regions of the light chain may be derived from a first species while the variable and constant regions of the heavy chain may be derived from a second species. In some aspects the antibody is a chimeric antibody and comprises rat and human regions. In some aspects, the antibody may be a chimeric antibody comprising heavy and light chain variable regions derived from rat and heavy and light chain constant regions derived from human. In some aspects the antibody may comprise a non-human constant region, preferably a rat constant region. In some aspects, the antibody (which may be humanised or chimeric) comprises a modified constant region wherein the modified constant region comprises one or more mutations that reduce or substantially eliminate binding to the human Fc receptor, preferably the human neonatal Fc receptor (FcRn). In some aspects said binding is measured by enzyme-linked immunosorbent assay (ELISA), bio-layer interferometry (BLI), or Biacore/SPR (surface plasmon resonance), wherein the level of binding exhibited by the wild-type constant region to the human Fc receptor (or human FcRn) is 100% binding, and the modified constant region exhibits reduced binding relative to said wild-type constant region. For example, the modified constant region may exhibit less than 80%, less than 70%, less than 60%, less than 50%, less than 40%, less than 30%, less than 20%, less than 10% of the binding to the human Fc receptor (or human FcRn) as exhibited by the corresponding wild-type human constant region to the human Fc receptor (or human FcRn), preferably less than 50% and most preferably less than 20% of said binding. In some aspects, the modified constant region is an IgG, preferably an IgG1, most preferably a human IgG1. In some aspects, the modified constant region is a human constant region. Preferably, said modified constant region is a mutant form of human IgG1 (preferably IgG1-AAA), which does not bind the human (e.g., human neonatal) Fc receptor. “IgG1-AAA” refers to a human IgG1 comprising alanine substitutions at positions Ile253, His310 and His435 (i.e., the IgG1 comprises the following mutations: I253A, H310A and H435A), which is also known as the ‘IHH mutation’. Such modified constant regions, which have reduced binding to the human Fc receptor (or human FcRn), have the advantage that they result in rapid clearance of the antibody from the system of human subjects, as described above. In some aspects, the antibody (which may be humanised or chimeric) comprises a modified human constant region wherein the modified constant region has enhanced complement-dependent cytotoxicity (CDC), antibody-dependent cellular cytotoxicity (ADCC) and/or antibody-dependent cellular phagocytosis (ADCP), preferably enhanced complement-dependent cytotoxicity (CDC). In some aspects, the antibody comprises a modified constant region that comprises one or more mutations that increase the binding affinity between the constant region and human complement (i.e., human C1q). In some aspects, the modified constant region may be a chimeric constant region comprising portions of two or more different human immunoglobulin isotypes (i.e., immunoglobulin classes), to enhance recruitment of human complement. In some aspects, the modified constant region may be a chimeric constant region comprising IgG3, IgG1, IgG2, IgG4 and/or IgM portions, for example the modified constant region may be a chimeric constant region comprising a IgG3 portion and a IgG1 portion. In some aspects, the antibody comprises a modified constant region that comprises one or more mutations in the hinge region and/or the CH2 domain that increase the recruitment of human complement, e.g., by increasing the affinity of the interaction between the constant region and human complement. In some aspects said binding affinity is measured by enzyme-linked immunosorbent assay (ELISA), bio-layer interferometry (BLI), or Biacore/SPR (surface plasmon resonance). In some aspects, the binding affinity of the modified constant region to human complement is increased as compared to the binding affinity of the corresponding unmodified constant region to human complement. For example, the binding affinity of the modified constant region to human complement may increase at least 2 fold, 3 fold, 4 fold, 5 fold, 10 fold, 15 fold, 20 fold, 30 fold, 40 fold, 50 fold, 60 fold, 70 fold, 80 fold, 90 fold, 100 fold, 150 fold, 200 fold, 300 fold or 500 fold, preferably at least 2 fold, most preferably at least 10 fold, as compared to the binding affinity of the corresponding unmodified constant region to human complement. In some aspects, the antibodies of the invention may comprise a modified constant region that has increased CDC activity as compared to the corresponding unmodified constant region. The CDC activity may be measured as % cell lysis in a target human CD45-expressing cell line treated with the antibody in the presence of human C1q. The skilled person would be readily capable of measuring cell lysis using a suitable assay, such as the MTT cell viability assay or ⁵¹ Cr release assay. In some aspects, an antibody of the invention comprising a modified constant region described herein may show at least 1.2 fold, 1.5 fold, 1.8 fold, 2 fold, 3 fold, 4 fold, 5 fold, 6 fold, 7 fold, 8 fold, 9 fold, 10 fold, 15 fold, 20 fold, or higher, preferably at least 2 fold, most preferably at least 5 fold, increase in % cell lysis of target cells in an in vitro cell viability assay as compared to an antibody of the invention comprising the corresponding unmodified constant region. In some aspects, the modified constant region is a human constant region, preferably human IgG, most preferably human IgG1. Such modified human constant regions, which have enhanced CDC activity, have the advantage that antibodies of the invention comprising such modified constant region have enhanced levels of cell killing of target cancer cells. In some aspects the antibody or fragment thereof may be modified or engineered to include one or more cysteine residues, for example site-specifically inserted into the antibody sequence. In some aspects the antibody or fragment thereof may be modified or engineered to include one or more unnatural amino acid(s) (such as acetyl-phenylalanine, p-acetyl-L-phenylalanine (pAcF), selenocysteine, or para-azidomethyl-l-phenylalanine), for example site-specifically inserted into the antibody sequence. Such cysteine residues or unnatural amino acids may provide a site for conjugation to an effect molecule or toxin, as described further herein. In some aspects the antibody or fragment thereof is isolated. In some aspects the antibody or fragment thereof may be an antibody fragment or a single chain antibody, optionally wherein, the fragment is a Fab fragment, a Fab' fragment, a F(ab)'2 fragment, a single chain Fab (scFab) fragment, a single chain Fv protein (scFv), a tandem scFv protein, or a disulfide stabilized Fv protein (dsFv), or a scFv-Fc protein. In some preferred aspects, the antibody or fragment thereof may be a scFv, a Fab, a scFab, a scFv-Fc or a single domain fragment. Where the antibody or fragment thereof is a biparatopic or bispecific antibody or fragment thereof as described herein, the antibody or fragment thereof may preferably be a scFab or a scFv-Fc. Advantageously, scFv-Fc typically show faster clearance following administration to a subject (such as a human subject), than whole IgGs. In some aspects, the antibody or fragment thereof may be a bispecific antibody, for example comprising a first and a second antigen binding domains, wherein the first antigen binding domain corresponds to an antibody of the invention and specifically binds human CD45, and wherein the second antigen binding domain specifically binds a different target antigen. In some aspects, the antibody or fragment thereof may be a biparatopic antibody, for example comprising a first antigen binding domain and a second antigen binding domain, wherein the first antigen binding domain is a first antibody of the invention, and wherein the second antigen binding domain is a second, different antibody of the invention, wherein the first and second antigen binding domains specifically bind human CD45 and recognise distinct, non-overlapping epitopes. In some aspects, the antibody or fragment thereof may be comprised in a multi-specific antibody. In some aspects, the antibody of the invention is a bispecific antibody or bispecific fragment thereof, comprising a first antigen binding domain and a second antigen binding domain, wherein the first antigen binding domain specifically binds human CD45, and wherein the first antigen binding domain comprises a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a LCDR1 comprising the sequence of SEQ ID NO: 3, a LCDR2 comprising the sequence of SEQ ID NO: 4, and a LCDR3 comprising the sequence of SEQ ID NO: 5, and wherein the heavy chain variable domain comprises a HCDR1 comprising the sequence of SEQ ID NO: 6, a HCDR2 comprising the sequence of SEQ ID NO: 7, and a HCDR3 comprising the sequence of SEQ ID NO: 8; preferably wherein the light chain variable domain comprises a sequence of SEQ ID NO: 1, and wherein the heavy chain variable domain comprises a sequence of SEQ ID NO: 2. In some other aspects, the antibody of the invention is a bispecific antibody or bispecific fragment thereof, comprising a first antigen binding domain and a second antigen binding domain, wherein the first antigen binding domain specifically binds human CD45, and wherein the first antigen binding domain comprises a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a LCDR1 comprising the sequence of SEQ ID NO: 13, a LCDR2 comprising the sequence of SEQ ID NO: 14, and a LCDR3 comprising the sequence of SEQ ID NO: 15, and wherein the heavy chain variable domain comprises a HCDR1 comprising the sequence of SEQ ID NO: 16, a HCDR2 comprising the sequence of SEQ ID NO: 17, and a HCDR3 comprising the sequence of SEQ ID NO: 18; preferably wherein the light chain variable domain comprises a sequence of SEQ ID NO: 11, and wherein the heavy chain variable domain comprises a sequence of SEQ ID NO: 12. In some aspects, the second antigen binding domain specifically binds a target selected from human c- Kit (CD117), human CD300F, human CD33, human BCMA or human CD20; preferably human c- Kit. In some aspects, the bispecific antibody may be for treating acute myeloid leukaemia (AML) and the second antigen binding domain may specifically bind human CD33. In some aspects, the bispecific antibody may be for treating myeloma and the second antigen binding domain may specifically bind human BCMA. In some aspects, the bispecific antibody may be for treating non- Hodgkins lymphoma and the second antigen binding domain may specifically bind human CD20. In some aspects, the antibody of the invention is a biparatopic antibody or biparatopic fragment thereof, that specifically binds human CD45, comprising a first antigen binding domain and a second antigen binding domain, wherein: (i) the first antigen binding domain comprises a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a LCDR1 comprising the sequence of SEQ ID NO: 3, a LCDR2 comprising the sequence of SEQ ID NO: 4, and a LCDR3 comprising the sequence of SEQ ID NO: 5, and wherein the heavy chain variable domain comprises a HCDR1 comprising the sequence of SEQ ID NO: 6, a HCDR2 comprising the sequence of SEQ ID NO: 7, and a HCDR3 comprising the sequence of SEQ ID NO: 8; preferably wherein the light chain variable domain comprises a sequence of SEQ ID NO: 1, and wherein the heavy chain variable domain comprises a sequence of SEQ ID NO: 2; and (ii) the second antigen binding domain comprises a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a LCDR1 comprising the sequence of SEQ ID NO: 13, a LCDR2 comprising the sequence of SEQ ID NO: 14, and a LCDR3 comprising the sequence of SEQ ID NO: 15, and wherein the heavy chain variable domain comprises a HCDR1 comprising the sequence of SEQ ID NO: 16, a HCDR2 comprising the sequence of SEQ ID NO: 17, and a HCDR3 comprising the sequence of SEQ ID NO: 18; preferably wherein the light chain variable domain comprises a sequence of SEQ ID NO: 11, and wherein the heavy chain variable domain comprises a sequence of SEQ ID NO: 12. The antibody of the invention may be a biparatopic antibody or biparatopic fragment thereof, that specifically binds human CD45, comprising a first antigen binding domain and a second antigen binding domain, wherein the first antigen binding domain specifically binds human CD45, and wherein the first antigen binding domain comprises a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a LCDR1 comprising the sequence of SEQ ID NO: 3, a LCDR2 comprising the sequence of SEQ ID NO: 4, and a LCDR3 comprising the sequence of SEQ ID NO: 5, and wherein the heavy chain variable domain comprises a HCDR1 comprising the sequence of SEQ ID NO: 6, a HCDR2 comprising the sequence of SEQ ID NO: 7, and a HCDR3 comprising the sequence of SEQ ID NO: 8; preferably wherein the light chain variable domain comprises a sequence of SEQ ID NO: 1, and wherein the heavy chain variable domain comprises a sequence of SEQ ID NO: 2. In some other aspects, the antibody of the invention is a biparatopic antibody or biparatopic fragment thereof, that specifically binds human CD45, comprising a first antigen binding domain and a second antigen binding domain, wherein the first antigen binding domain specifically binds human CD45, and wherein the first antigen binding domain comprises a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a LCDR1 comprising the sequence of SEQ ID NO: 13, a LCDR2 comprising the sequence of SEQ ID NO: 14, and a LCDR3 comprising the sequence of SEQ ID NO: 15, and wherein the heavy chain variable domain comprises a HCDR1 comprising the sequence of SEQ ID NO: 16, a HCDR2 comprising the sequence of SEQ ID NO: 17, and a HCDR3 comprising the sequence of SEQ ID NO: 18; preferably wherein the light chain variable domain comprises a sequence of SEQ ID NO: 11, and wherein the heavy chain variable domain comprises a sequence of SEQ ID NO: 12. In such aspects, the second antigen binding domain may specifically bind human CD45, typically at an epitope on human CD45 that does not overlap with the binding epitope of the first antigen binding domain. In some instances, the biparatopic antibody or biparatopic fragment thereof, that specifically binds human CD45, comprises a first antigen binding domain and a second antigen binding domain, wherein (i) the first antigen binding domain comprises a light chain, or a heavy chain, or preferably a light chain and a heavy chain, and/or (ii) the second antigen binding domain comprises a light chain, or a heavy chain, or preferably a light chain and a heavy chain. Where the first and second antigen binding domains comprise a heavy chain, the heavy chains of the first and second antigen binding domains may comprise mutations to enhance dimerization or binding of the two heavy chains. The mutations may increase the efficiency of the formation of a biparatopic antibody. The mutations typically facilitate controlled Fab-arm exchange (cFAE) of the antibodies. In some instances, the heavy chains of the first and second antigen binding domains may be rat IgG2b heavy chains. Suitable mutations are described, for example, in Labrijn et al, 2017, and particularly preferred mutations are set out herein. The first antigen binding domain may comprise a heavy chain comprising a mutations at K409 (preferably a K409R mutation), as numbered according to the EU-numbering system, and the second antigen binding domain may comprise a heavy chain comprising a mutation at F405 (preferably an F405L mutation), as numbered according to the EU-numbering system. Alternatively, the second antigen binding domain may comprise a heavy chain comprising a mutation at K409 (preferably a K409R mutation), as numbered according to the EU-numbering system, and the first antigen binding domain may comprise a heavy chain comprising a mutation at F405 (preferably an F405L mutation), as numbered according to the EU-numbering system. The first antigen binding domain may comprise a heavy chain comprising mutations at S370 or K409, preferably at S370 and K409 (most preferably S370K and K409R mutations), as numbered according to the EU-numbering system, and the second antigen binding domain may comprise a heavy chain comprising a mutation at F405 (preferably an F405L mutation), as numbered according to the EU-numbering system. The second antigen binding domain may comprise a heavy chain comprising mutations at S370 or K409, preferably at S370 and K409 (most preferably S370K and K409R mutations), as numbered according to the EU-numbering system, and the first antigen binding domain may comprise a heavy chain comprising a mutation at F405 (preferably an F405L mutation), as numbered according to the EU-numbering system. The first antigen binding domain may comprise a heavy chain comprising mutations at S370 or K409, preferably at S370 and K409 (most preferably S370K and K409R mutations), as numbered according to the EU-numbering system, and the second antigen binding domain may comprise a heavy chain comprising mutations at F405 or N411, preferably at F405 and N411 (most preferably F405L and N411T mutations), as numbered according to the EU-numbering system. The second antigen binding domain may comprise a heavy chain comprising mutations at S370 or K409, preferably at S370 and K409 (most preferably S370K and K409R mutations), as numbered according to the EU-numbering system, and the first antigen binding domain may comprise a heavy chain comprising mutations at F405 or N411, preferably at F405 and N411 (most preferably F405L and N411T mutations), as numbered according to the EU-numbering system. In some aspects, the antibody may be linked to an effector molecule; for example, the antibody that specifically binds human CD45, may be covalently linked to an effector molecule or to a toxin. The linkage can be by chemical means or recombinant means (e.g., a peptide linker). Where the linkage is chemical, a reaction may have occurred to produce a covalent bond linking the antibody or fragment thereof with the effector molecule. The linkage may comprise a peptide linker comprising, for example, 1-50, 1-40, 1-30, 1-20, or preferably 1-10 amino acids. The antibody, optionally linked to an effector molecule, may be further linked to a lipid, protein, polypeptide or carbohydrate that increases or preferably decreases its half-life in the body. The effector molecule may be selected from the group consisting of: an anti-cancer agent, a cytotoxic agent, a cytostatic agent, a drug, a radioisotope, a detectable label, an enzyme, a fluorophore, a fluorescent protein, a chemiluminescent agent, a radioactive label, a heavy metal or any other detectable compound known to the skilled person. In preferred aspects, the antibody may be conjugated to an anti-cancer agent, a cytotoxic agent, or a cytostatic agent. The antibody may be conjugated to MMAE, Maytansine, Maytansine derivative, a maytansinoid, DM1, Dxd, Duocarmycin, PNU, an anthracycline, amanitin, Duocarmycin, calicheamycin, camptothecin, Pseudomonas exotoxin A or alpha sarcin. In some aspects, the antibody may be conjugated to MMAE, an anthracycline, amanitin, Duocarmycin, calicheamycin, camptothecin, Pseudomonas exotoxin A or alpha sarcin. Preferably, the antibody may be conjugated to MMAE, Maytansine, Maytansine derivative, Dxd, Duocarmycin or PNU. The antibody may be conjugated to Duocarmycin SA, PNU159682 (anthracycline / nemorubicin metabolite), Maytansine derivative, MMAE (auristatin derivative), DX8951 (Exatecan derivative), or C6 Alpha amanitin. Maytansine and Maytansine derivative are typically understood to be maytansinoids. In some aspects the Maytansine derivative, including a suitable linker for antibody conjugation, may comprise the following structure: Other maytansinoids include DM1 (also known as Mertansine or in some forms emtasine), Ansamitocin, and DM4 (also known as Ravtansine or soravtansine). Exemplary structures of Maytansine and DM1 are shown below: Dxd, as used herein, may be understood to be a derivative of Exatecan (DX-8951). PNU (an anthracycline), as used herein, is typically understood to be PNU-159682, which is a metabolite of the anthracycline nemorubicin and is a DNA topoisomerase I inhibitor. Most preferably, the antibody may be conjugated to PNU. The antibody may be conjugated to saporin. The antibody may be bound to an antibody-saporin conjugate (such as an anti-rat IgG saporin conjugate), wherein the antibody-saporin conjugate specifically binds to the species and isotype of the antibody. Notwithstanding the above, the antibody of the invention is not conjugated to a pyrrolobenzodiazepine (PBD). PBDs are of the general structure: PBDs may differ in the number, type and position of substituents, in the aromatic A ring and the pyrrolo C ring, and in the degree of saturation of the C ring. In the B-ring there is either an imine (N=C), a carbinolamine(NH-CH(OH)), or a carbinolamine methyl ether (NH-CH(OMe)) at the N10-C11 position. PBDs typically have an (S)-configuration at the chiral C11a position, which provides a right-handed twist when viewed from the C ring towards the A ring. A number of naturally occurring PBDs have been identified, and over 10 synthetic routes have been developed to a variety of analogues (see, e.g., Thurston, et al., Chem. Rev.1994, 433-465 (1994); Antonow, D. and Thurston, D.E., Chem. Rev.2011111 (4), 2815-2864). The term “PBD” may be understood to include PBD dimers. Antibody drug conjugates Antibody drug conjugates (i.e., immunoconjugates) allow for targeted delivery of cytotoxic or cytostatic agents (i.e., drugs that kill or inhibit growth and division of cells, such as drugs useful in the treatment of cancer) to cells, such as haematopoietic cells or cancer cells. The conjugates may be internalised by the target cells, typically haematopoietic cells or cancer cells, resulting in intracellular accumulation of the drug. Systemic administration of the unconjugated drugs typically results in unacceptable levels of toxicity to normal or non-target cells. Thus, the present invention provides antibody drug conjugates that target delivery of the drug units to CD45 positive cells. The CD45 positive cells may be cancer cells or haematopoietic cells, including haematopoietic stem cells (HSCs). The present invention therefore provides conjugates comprising an antibody of the invention that specifically binds human CD45, as defined above, and a drug, wherein the drug is an anti-cancer agent, a cytotoxic agent or a cytostatic agent. Thus, the present invention provides an antibody drug conjugate of formula (I): Ab – (L–D)p (I) wherein Ab is an antibody of the invention as described herein; wherein L is a linker connecting Ab to D; wherein D is an anti-cancer agent, a cytotoxic agent or a cytostatic agent; wherein p is preferably from 1 to 8; and wherein D is not a pyrrolobenzodiazepine (PBD), such as a PBD dimer. In some aspects, L may be absent, or simply a covalent bond between the antibody (Ab) and the drug (D). As discussed above, PBDs are of the general structure: PBDs may differ in the number, type and position of substituents, in the aromatic A ring and the pyrrolo C ring, and in the degree of saturation of the C ring. In the B-ring there is either an imine (N=C), a carbinolamine(NH-CH(OH)), or a carbinolamine methyl ether (NH-CH(OMe)) at the N10-C11 position. PBDs typically have an (S)-configuration at the chiral C11a position, which provides a right-handed twist when viewed from the C ring towards the A ring. A number of naturally occurring PBDs have been identified, and over 10 synthetic routes have been developed to a variety of analogues (see, e.g., Thurston, et al., Chem. Rev.1994, 433-465 (1994); Antonow, D. and Thurston, D.E., Chem. Rev.2011111 (4), 2815-2864). The anti-CD45 antibody drug conjugates described herein have several advantageous features. Following administration to a subject in need thereof, the antibody drug conjugates may be rapidly cleared from the subject’s system, in order to minimise the residual toxicity to any CD45-positive donor cells (e.g., CD45-positive haematopoietic stem cells) that are subsequently administered to the subject. Typically, this rapid clearance may be achieved in a human subject, for example by the antibody (Ab) being a non-human antibody, such as a rat antibody, preferably a rat IgG2 antibody. Alternatively, the antibody (Ab) may comprise a modified human constant region that comprises mutations that reduce or substantially eliminate binding to the human Fc receptor (e.g., the IgG1- AAA constant region), optionally this antibody may be a humanised antibody. Additionally, the antibody (Ab) may be otherwise selected, modified, or engineered to have a short half-life in the subject of interest. The antibody drug conjugates of the invention are highly specific, targeted and potent agents that achieve very high levels of lysis of the subject’s CD45-positive haematopoietic stem cells, such as a cell population characterised as CD45+CD34+CD38-Lin-CD45RA-CD90+. Typically said cell population exhibits lower levels of other potential targets for antibody-based conditioning such as c-kit, and may therefore be difficult to target. The present antibody drug conjugates described herein address this problem of inadequate lysis levels from existing therapies, and provide improved transplant outcomes. Antibodies (Ab) In the antibody drug conjugates of the invention, Ab may be any antibody or fragment thereof of the invention, as described herein. All of the description of the antibodies or fragments thereof of the invention may be applied directly to the antibody Ab within the antibody drug conjugates of the invention. Any of the features of the antibodies or fragments thereof of the invention described herein applies to the antibody Ab of the antibody drug conjugates of the invention. Specifically any of the antibodies or fragments thereof described herein may be incorporated into the antibody drug conjugates of the invention. The antibody Ab of the antibody drug conjugate of the invention is the antibody or fragment thereof of the invention. For example, in some aspects, the antibody (Ab) may be a monoclonal antibody or fragment thereof that specifically binds human CD45, comprising a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a LCDR1, a LCDR2 and a LCDR3, and wherein the heavy chain variable domain comprises a HCDR1, a HCDR2 and a HCDR3, wherein LCDR1 comprises the sequence of SEQ ID NO: 3, LCDR2 comprises the sequence of SEQ ID NO: 4, and LCDR3 comprises the sequence of SEQ ID NO: 5, and HCDR1 comprises the sequence of SEQ ID NO: 6, HCDR2 comprises the sequence of SEQ ID NO: 7, and HCDR3 comprises the sequence of SEQ ID NO: 8; preferably wherein the light chain variable domain comprises a sequence of SEQ ID NO: 1, and wherein the heavy chain variable domain comprises a sequence of SEQ ID NO: 2. In some other aspects, the antibody (Ab) may be a monoclonal antibody or fragment thereof that specifically binds human CD45, comprising a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a LCDR1, a LCDR2 and a LCDR3, and wherein the heavy chain variable domain comprises a HCDR1, a HCDR2 and a HCDR3, wherein LCDR1 comprises the sequence of SEQ ID NO: 13, LCDR2 comprises the sequence of SEQ ID NO: 14, and LCDR3 comprises the sequence of SEQ ID NO: 15, and HCDR1 comprises the sequence of SEQ ID NO: 16, HCDR2 comprises the sequence of SEQ ID NO: 17, and HCDR3 comprises the sequence of SEQ ID NO: 18; preferably wherein the light chain variable domain comprises a sequence of SEQ ID NO: 11, and wherein the heavy chain variable domain comprises a sequence of SEQ ID NO: 12. In some other aspects, the antibody (Ab) may be a biparatopic antibody or biparatopic fragment thereof, that specifically binds human CD45, comprising a first antigen binding domain and a second antigen binding domain, wherein: A. (i) the first antigen binding domain comprises a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a LCDR1 comprising the sequence of SEQ ID NO: 3, a LCDR2 comprising the sequence of SEQ ID NO: 4, and a LCDR3 comprising the sequence of SEQ ID NO: 5, and wherein the heavy chain variable domain comprises a HCDR1 comprising the sequence of SEQ ID NO: 6, a HCDR2 comprising the sequence of SEQ ID NO: 7, and a HCDR3 comprising the sequence of SEQ ID NO: 8; preferably wherein the light chain variable domain comprises a sequence of SEQ ID NO: 1, and wherein the heavy chain variable domain comprises a sequence of SEQ ID NO: 2; and (ii) the second antigen binding domain comprises a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a LCDR1 comprising the sequence of SEQ ID NO: 13, a LCDR2 comprising the sequence of SEQ ID NO: 14, and a LCDR3 comprising the sequence of SEQ ID NO: 15, and wherein the heavy chain variable domain comprises a HCDR1 comprising the sequence of SEQ ID NO: 16, a HCDR2 comprising the sequence of SEQ ID NO: 17, and a HCDR3 comprising the sequence of SEQ ID NO: 18; preferably wherein the light chain variable domain comprises a sequence of SEQ ID NO: 11, and wherein the heavy chain variable domain comprises a sequence of SEQ ID NO: 12; or B. the first or second antigen binding domain comprises a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a LCDR1 comprising the sequence of SEQ ID NO: 3, a LCDR2 comprising the sequence of SEQ ID NO: 4, and a LCDR3 comprising the sequence of SEQ ID NO: 5, and wherein the heavy chain variable domain comprises a HCDR1 comprising the sequence of SEQ ID NO: 6, a HCDR2 comprising the sequence of SEQ ID NO: 7, and a HCDR3 comprising the sequence of SEQ ID NO: 8; preferably wherein the light chain variable domain comprises a sequence of SEQ ID NO: 1, and wherein the heavy chain variable domain comprises a sequence of SEQ ID NO: 2; or C. the first or second antigen binding domain comprises a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a LCDR1 comprising the sequence of SEQ ID NO: 13, a LCDR2 comprising the sequence of SEQ ID NO: 14, and a LCDR3 comprising the sequence of SEQ ID NO: 15, and wherein the heavy chain variable domain comprises a HCDR1 comprising the sequence of SEQ ID NO: 16, a HCDR2 comprising the sequence of SEQ ID NO: 17, and a HCDR3 comprising the sequence of SEQ ID NO: 18; preferably wherein the light chain variable domain comprises a sequence of SEQ ID NO: 11, and wherein the heavy chain variable domain comprises a sequence of SEQ ID NO: 12. In a clinical study (Straathof, K. C., et al. (2009), Lancet 374(9693): 912-920), two anti-CD45 monoclonal antibodies were used for myelosuppression together with alemtuzumab (an anti-CD52 antibody) and fludarabine, and low dose cyclophosphamide for immunosuppression, in a minimal- intensity conditioning regimen. This was shown to achieve curative engraftment in 13/16 paediatric subjects with primary immunodeficiency disorders. However, myeloid engraftment was sub-optimal in some subjects, possibly caused by inadequate lysis of true haematopoietic stem cells (HSC) (e.g., CD45+CD34+CD38-Lin-CD45RA-CD90+ cells), meaning that an insufficient niche was created for donor HSC engraftment. The antibody drug conjugates of the invention have all of the advantages of the antibodies alone, but have further enhanced potency of cell killing, which may allow extension of a conditioning approach to adults and subjects without underlying immunodeficiency. Drug units The antibody drug conjugates of the invention comprise any antibody described herein (Ab) conjugated to (i.e., linked to or fused to) an anti-cancer agent, a cytotoxic agent or a cytostatic agent (D). Thus, D is an anti-cancer agent, a cytotoxic agent or a cytostatic agent. An anticancer agent (also called an antineoplastic agent) is any agent, small molecule or biologic, that is effective in the treatment of cancer. A cytotoxic agent is any agent that results in cell killing, preferably cancer cell killing, and tumour shrinkage. A cytostatic agent is any agent that inhibits, reduces or prevents cell growth or division, preferably of cancer cells, and inhibits tumour growth. D may be a known anti-cancer therapeutic with proven anti-cancer, cytotoxic or cytostatic properties. The drug loading is the average number of drug units (D) per antibody (Ab), and is represented by p. The average number of drugs per antibody in preparations of antibody drug conjugates from conjugation reactions may be characterized by conventional means such as UV, reverse phase HPLC, HIC, mass spectroscopy, ELISA assay, and electrophoresis. In some instances, separation, purification, and characterization of homogeneous antibody drug conjugates where p is a certain value from antibody drug conjugates with other drug loadings may be achieved by means such as reverse phase HPLC or electrophoresis. Drug loading (p) is typically limited by the number of attachment sites for the drugs and linkers on the antibody. An attachment site may be understood to mean the site on the antibody at which a drug unit is attached usually via a linker. For example, the antibody may have 1, 2, 3, 4, 5, 6, 7 or 8 attachment sites to which the drug linker may be attached. In some aspects, the antibody has 1-8, 1-6, 1-4 or 1-2 such attachment sites, preferably 1- 8 and most preferably 1-4 such attachment sites. Typically, fewer than the theoretical maximum of drug moieties are conjugated to an antibody during a conjugation reaction. The loading (drug/antibody ratio) of an ADC may be controlled in several different manners, including: (i) limiting the molar excess of drug-linker intermediate (D-L) or linker reagent relative to antibody, and (ii) limiting the conjugation reaction time or temperature. The antibody-drug conjugate compositions of the invention include mixtures of antibody-drug conjugates where the antibody has one or more drug units attached and where the drug units may be attached to the antibody at various different sites, such as at different amino acid residues. The drug unit is typically attached to the antibody through a linker. Suitable linkers are described further herein. Suitable means for attaching or conjugating the antibody to the linker are also described further herein. In some aspects, the average number of drug units (D) per antibody (Ab) in the antibody drug conjugates of the invention is in the range of 1 to 8. In some aspects, the range is selected from 1 to 4, 2 to 4, 1 to 3, 2 to 3, or 1 to 2, preferably 1 to 4. In some aspects, there are one or two drug units (D) per antibody (Ab) in the antibody drug conjugates of the invention. In some aspects p is 1 to 8, preferably 1 to 4. In some aspects p is about 2. In some aspects, each D is independently selected from the group consisting of a tubulin inhibitor, a DNA damaging agent, a topoisomerase I inhibitor, a DNA alkylator, a DNA cross-linker and an RNA polymerase II inhibitor. Each D may be independently selected from the group consisting of MMAE, Maytansine, Maytansine derivative, a maytansinoid, DM1, Dxd, Duocarmycin, PNU, an anthracycline, amanitin, Duocarmycin, calicheamycin, camptothecin, Pseudomonas exotoxin A, and alpha sarcin. In some preferred aspects, each D is independently selected from the group consisting of Monomethyl auristatin E (MMAE) (tubulin inhibition and bystander effect), anthracyclines (DNA alkylation and DNA cross-linking), amanitin (RNA polymerase II inhibitor), Duocarmycin (DNA alkylator), calicheamycin (DNA damaging agent), camptothecin (topoisomerase inhibition), Pseudomonas exotoxin A, and alpha sarcin. In most preferred aspects, D is MMAE, an anthracycline, amanitin, Duocarmycin, calicheamycin, or camptothecin. Preferably, D is MMAE, Maytansine, Maytansine derivative, Dxd, Duocarmycin or PNU. D may be Duocarmycin SA, PNU159682 (anthracycline / nemorubicin metabolite), Maytansine derivative, MMAE (auristatin derivative), DX8951 (Exatecan derivative), or C6 Alpha amanitin. Most preferably, D is PNU. D may saporin. Preferably, each D within an antibody drug conjugate is the same. Other possible drugs from which D may be selected include: MMAE, mc-vc-PAB-MMAE (MMAE, linked via the lysosomally cleavable dipeptide, valine-citrulline (vc), MC- betaglucuronide-MMAE-2 (MMAE linked via the cleavable ADC linker MC-betaglucuronide), Maytansine, Maytansine derivative, DM1, Dxd, Duocarmycin, PNU, dolastatin 10, a vinca alkaloid, vinblastine, vincristine, a taxane diterpene, taxol, an anthracycline, cyclophosphamide, methotrexate, pemetrexed, proguanil, pyrimethamine, trimethoprim, doxorubicin, calicheamycin, maytansine analogs, auristatins and auristatin analogs, SN-38, α-amanitin, amanitin, paclitaxel, epothilones, discodermolide, taccalonolides, maytansinoids, vinflunine, halichondrin B, eribulin msylate, cryptophycins, dolastatins, colchicine, 2-methoxyestradiol, sulphonamides, docetaxel, cyclostreptin, eleutherobin, ABI-007, ixabepilone, patupilone, BMS-310705, laulimalide, saporin, peloruside A, alpha sarcin, diphtheria toxin, Pseudomonas exotoxin, ricin A chain and gelonin. In the antibody drug conjugates of the invention the antibody Ab is not conjugated to a pyrrolobenzodiazepine (PBD), i.e., in some aspects D is not a PBD, such as a PBD dimer. In some aspects, in the antibody drug conjugates of the invention the antibody Ab is not conjugated to saporin, i.e., in some aspects D is not saporin. Preferably, within the antibody drug conjugate, each D conjugated to the antibody (Ab) may be the same. Alternatively, within the antibody drug conjugate there may be different drugs D conjugated to the antibody (Ab). For example the antibody Ab may be conjugated to ‘p’ copies of D, wherein each D is the same drug. Alternatively, the antibody Ab may be conjugated to ‘x’ copies of D ₁ and ‘y’ copies of D ₂ , wherein x + y = p, and D ₁ and D ₂ are different drugs. In some aspects, each (L-D) in the antibody drug conjugate is the same. In some aspects the antibody drug conjugate comprises at least two, preferably two, different species of (L–D) (e.g., (L-D ₁ ) and (L-D ₂ ), (L ₁ -D) and (L ₂ -D) or (L ₁ -D ₁ ) and (L ₂ -D ₂ ), wherein the subscripts 1 and 2 denote different species of linker L or drug D). Also described herein are compositions comprising different species of antibody drug conjugates. For example, a composition may comprise antibody drug conjugates comprising the same antibody, but conjugated to different drugs; or a composition may comprise antibody drug conjugates comprising the same drug, but conjugated to two different antibodies. These will be described further herein. Linkers L is a linker connecting the antibody Ab to the drug D. L may be any linker suitable for connecting, covalently linking or conjugating the antibody Ab to the drug D. The linker L may be cleavable or non-cleavable. The linker L is preferably stable extracellularly. Thus, before transport or delivery into a cell, the antibody drug conjugate of the invention is preferably stable and remains intact, i.e. the antibody Ab remains linked to the drug D. In some aspects, the linker L is stable outside the target cell (i.e., in an extracellular environment), but is cleaved inside the cell (i.e., in an intracellular environment), to release the drug D from the antibody Ab. Thus, the antibody Ab targets the anticancer, cytotoxic and/or cytostatic drug D to the target cells expressing CD45. Typically the cleavage of the linker occurs at a fast enough rate to allow the drug to have an anti-cancer, cytotoxic or cytostatic effect on the target cell. The linker may be cleaved at any point following internalisation of the antibody drug conjugate by the target cell. In some aspects the linker may be cleaved preferentially in a particular intracellular compartment within the target cell. For example, the linker L may be preferentially cleaved within the lysozyme. An effective linker will: (i) maintain the specific binding properties of the antibody; (ii) allow intracellular delivery of the conjugate and/or drug; (iii) remain stable and intact, i.e. not cleaved, until the conjugate and/or drug has been delivered or transported to its target site; and (iv) maintain a cytotoxic, anti-cancer, cell-killing and/or cytostatic effect of the drug D. Stability of the antibody drug conjugate may be measured by standard analytical techniques such as mass spectroscopy, HPLC, and the separation/analysis technique LC/MS. The linker may be a non-cleavable linker, i.e., a linker that is not readily cleavable for example by enzyme activity, such as protease activity, or under specific conditions, such as acidic conditions. In some preferred aspects, L is a cleavable linker, i.e., a linker that is susceptible to cleavage when in the presence of a suitable cleavage moiety or under particular conditions. L may be selected from the group consisting of an acid-cleavable linker, a protease-cleavable linker, a disulfide linker, an enzyme cleavable linker, a pH-sensitive linker, a thiol-sensitive linker, or a reactive oxygen species sensitive linker; preferably L may be a pH-sensitive linker (such as an acid-cleavable linker) or a protease-cleavable linker. L may be any suitable linker that allows for targeted delivery of the drug unit to a CD45-positive cell. Suitable linkers are described for example in Yang et al. Med Res Rev.2020; 1–32, and the skilled person would be capable of selecting a suitable linker. A pH sensitive linker is susceptible to cleavage, and may be cleaved, upon a change in pH. Preferably, the pH sensitive linker is susceptible to cleavage, and may be cleaved, under acidic or low pH conditions (i.e., in environments having a lower pH than that of normal tissue which is about pH 7.4), such as those found within the endosome (about pH 5.5-6.0) or the lysosome (about pH 4.5-5.0) or in tumour tissues (about pH 6-7). Examples of pH-sensitive linkers include: imine linkers, hydrazone linkers, acyl hydrazone linkers (e.g., 4‐(4‐acetylphenoxy) butanoic acid (AcBut)-acyl hydrazone), oxime linkers, phosphoramidate linkers, acetal-based linkers, NEBI linkers, and maleic acid-derived linkers. A protease-cleavable linker is susceptible to cleavage, and may be cleaved, in the presence of selected proteases, such as those found within a target cell, e.g., a CD45-positive haematopoietic cell, or within a lysosome. In some aspects the protease-cleavable linker may be susceptible to cleavage, and may be cleaved, in the presence of a protease selected from: cathepsin, a metalloproteinase, matrix metalloproteinase 2 (MMP‐2), chymotrypsin, caspase 3, and urokinase plasminogen activator. An enzyme-cleavable linker is susceptible to cleavage, and may be cleaved, in the presence of selected enzymes, such as those found within a target cell, e.g., a CD45-positive haematopoietic cell, or within a lysosome. In some aspects, the enzyme may be β-D-glucuronidase. A thiol-sensitive linker, such as a disulfide linker, is susceptible to cleavage, and may be cleaved, under reducing conditions (e.g., in the presence of GSH), such as those found in the intracellular environment following internalisation of the antibody drug conjugate by the target cell, e.g., a CD45-positive haematopoietic cell. A reactive oxygen species (ROS)-sensitive linker is susceptible to cleavage, and may be cleaved, in oxidative environments generated by ROS. Examples of ROS-sensitive linkers include: aryl boronic acid and boronate‐ based linkers, thioketal‐based linkers and thioether‐based linkers. In some aspects, L is cleavable in the lysosome, i.e., L is designed to be cleaved under the conditions present in a lysosome within a target cell, e.g., a CD45-positive haematopoietic cell. The linker L may comprise a peptide portion. For example at least a portion of the linker L may comprise a short peptide of 1-20, 1-10, 1-8, 1-5, 1-4, 1-3, or 1-2 amino acids, preferably 1-10 and most preferably 1-5 amino acids. In some aspects the peptide portion of the linker L may comprise a target sequence for a protease, such that the peptide sequence may be cleaved by a particular protease. In some aspects, the linker may consist essentially of a short peptide that is covalently linked to the antibody (Ab) at one terminus and to the drug (D) at the other terminus. Thus, the linker L may comprise, or consist essentially of, a short peptide of 1-20, 1-10, 1-8, 1-5, 1-4, 1-3, or 1-2 amino acids, preferably 1-10 and most preferably 1-5 amino acids. Suitable methods for covalently or chemically linking a short peptide to the antibody (Ab) and the drug (D) are known to the person skilled in the art. In some aspects, each L may be selected from the group consisting of an acid-cleavable hydrazone linker, a cathepsin labile linker, valine-citrulline (Val-Cit), phenylalanine-lysine (Phe-Lys), MHH, DSDM, Sulfo-SPDB, MC-VC-PABC, SMCC (non- cleavable), Mal-PEG-NHS (non-cleavable) and GBC. Preferably, each L within an antibody drug conjugate is the same. In some aspects the linker L may be selected from the group consisting of: SMCC noncleavable thioether linker, MC non-cleavable linker, VC-seco, Fleximer®, AS269 noncleavable, VA-PABC, VC protease-cleavable linker, VA linker, MCC noncleavable, (AcBut)- N-acyl acid-labile hydrazone linker, SPDB disulfide cleavable linker, VA and maleimide cleavable linker, noncleavable alkyl hydrazide linker, MC-VC-PAB linker, CL2A pH sensitive (Benzylcarbonate site) carbonate linker, AcLys-VC-PABC linker, SPP disulfide cleavable linker, PEG8-va linker, cathepsin-B cleavable dipeptide linker, Sulfo-SPDB disulfide cleavable linker, and cleavable VC-PABC-linker. The conjugates of antibodies and cytotoxic agents may be prepared using any suitable methods as disclosed in the art, e.g., in “Bioconjugate Techniques”, G.T. Hermanson, 3rd Ed., Elsevier Inc., 2013. The linker may be conjugated to the antibody (Ab) using for example cleavable disulphide or non-cleavable thioether linker chemistry. The linker may be attached to a lysine residue in the antibody, the lysine may be native or engineered. The linker may be attached to a cysteine residue in the antibody. The cysteine may be native, for example a cysteine of one of the interchain disulphide bridges in the antibody, or the cysteine may be engineered, i.e., site-specifically inserted into the antibody sequence at the desired conjugation site. The linker may be attached to an unnatural amino acid (such as acetyl-phenylalanine, p-acetyl-L-phenylalanine (pAcF), selenocysteine, or para-azidomethyl-l-phenylalanine) in the antibody, for example by an oxime linkage. The antibody may be engineered to include an unnatural amino acid at the desired conjugation site. Chemoenzymatic site direct conjugation may also be used. For example, an azide group may be formed, for example at an asparagine residue in the antibody constant region, and linked with a drug unit using for example a copper-mediated click reaction. An azide group may be formed in a selective hydrolysis reaction mediated by an Endo-beta-N-acetylglucosaminidase (EndoS) chemoenzyme. Other strategies for site-specific conjugation of linkers and their attached drug units are known in the art and are extensively covered in G. T. Hermanson “Bioconjugate Techniques”, 2013, Elsevier Inc. In some aspects the linker L may be: (a) IIa , wherein Q is: where Q ^X is such that Q is an amino-acid residue, a dipeptide residue or a tripeptide residue; X is: where a = 0 to 5, b = 0 to 16, c = 0 or 1, d = 0 to 5; and G ^LL is a linker group connected to Ab; or (b) X— G ^LL , where X and G ^LL are as defined above. In some aspects the linker L may be: (a) IIa , wherein Q is: where Q ^X is such that Q is an amino-acid residue, a dipeptide residue, a tripeptide residue, or a tetrapeptide residue; X is: where a = 0 to 5, b1 = 0 to 16, b2 = 0 to 16, c1 = 0 or 1, c2 = 0 or 1, d = 0 to 5, wherein at least b1 or b2 = 0 (i.e. only one of b1 and b2 may not be 0) and at least c1 or c2 = 0 (i.e. only one of c1 and c2 may not be 0); and G ^LL is a linker group connected to Ab; or (b) X— G ^LL , where X and G ^LL are as defined above. In some aspects, Q comprises or preferably is an amino acid residue. The amino acid residue may be a natural amino acid or a non-natural amino acid. Q may be selected from: Phe, Lys, Val, Ala, Cit, Leu, Ile, Arg, and Trp, where Cit is citrulline. In some aspects, Q comprises or preferably is a dipeptide residue. The amino acids in the dipeptide may be any combination of natural amino acids and non-natural amino acids. Preferably, Q comprises or is a dipeptide comprising natural amino acids. In some aspects the linker is a cathepsin labile linker, and the dipeptide is the site of action for cathepsin-mediated cleavage (i.e., the dipeptide is a recognition site for cathepsin). In some aspects, Q is selected from: ^C=O -Phe-Lys- ^NH , ^C=O -Val-Ala- ^NH , ^C=O -Val-Lys- ^NH , ^C=O -Ala-Lys- ^NH , ^C=O -Val-Cit- ^NH , ^C=O -Phe-Cit- ^NH , ^C=O -Leu-Cit- ^NH , ^C=O -Ile-Cit- ^NH , ^C=O -Phe-Arg- ^NH , ^C=O -Trp-Cit- ^NH , and ^C=O -Gly-Val- ^NH ; where Cit is citrulline. Preferably, Q is selected from: ^C=O -Phe-Lys- ^NH , ^C=O -Val- Ala- ^NH , ^C=O -Val-Lys- ^NH , ^C=O -Ala-Lys- ^NH , and ^C=O -Val-Cit- ^NH . Most preferably, Q is selected from: ^C=O -Phe-Lys- ^NH , ^C=O -Val-Cit- ^NH or ^C=O -Val-Ala- ^NH . Other dipeptide combinations of interest include: ^C=O -Gly-Gly- ^NH , ^C=O -Gly-Val- ^NH , ^C=O -Pro-Pro- ^NH , and ^C=O -Val-Glu- ^NH . Other dipeptide combinations may be used, including those described by Dubowchik et al., Bioconjugate Chemistry, 2002, 13,855- 869. In some aspects, Q comprises or preferably is a tripeptide residue. The amino acids in the tripeptide may be any combination of natural amino acids and non-natural amino acids. Preferably, Q comprises or is a tripeptide comprising natural amino acids. The linker may be a cathepsin labile linker, where the tripeptide is the site of action for cathepsin-mediated cleavage (i.e., the tripeptide is a recognition site for cathepsin). Tripeptide linkers of particular interest are: ^C=O -Glu-Val-Ala- ^NH , C ^=O -Glu-Val-Cit- ^NH , ^C=O -αGlu-Val-Ala- ^NH , and ^C=O -αGlu-Val-Cit- ^NH . Q may comprise, or preferably may be, a tetrapeptide residue. The amino acids in the tetrapeptide may be any combination of natural amino acids and non-natural amino acids. Preferably, Q may comprise, or preferably may be, a tetrapeptide comprising natural amino acids. The linker may be a cathepsin labile linker, where the tetrapeptide is the site of action for cathepsin-mediated cleavage (i.e., the tetrapeptide is a recognition site for cathepsin). Tetrapeptide linkers of particular interest are: ^C=O -Gly-Gly-Phe-Gly- ^NH ; and ^C=O -Gly-Phe-Gly-Gly- ^NH , preferably ^C=O -Gly-Gly-Phe-Gly- ^NH . In the above representations of peptide residues, ^C=O - represents where the residue binds to C=O in R ^LL , and - ^NH represents where the residue binds to NH in R ^LL . Glu represents the residue of glutamic acid, i.e.: αGlu represents the residue of glutamic acid when bound via the α-chain, i.e.: The amino acid side chain may be chemically protected, where appropriate. Protecting groups for the side chains of amino acids are well known in the art and are described in the Novabiochem Catalog. G ^LL may be selected from:

where Ar represents a C _5-6 arylene group, e.g. phenylene and X represents C _1-4 alkyl. In some aspects, G ^LL is selected from G ^LL1-1 and G ^LL1-2 ., preferably G ^LL is G ^LL1-1 . G ^LL may be G ^LL10 . The term “C _5-6 arylene”, as used herein, may be understood to refer to a divalent moiety obtained by removing two hydrogen atoms from an aromatic ring atom of an aromatic compound. The subscript numerals (e.g. C _5-6 ) denote the number of ring atoms, or range of number of ring atoms, whether carbon atoms or heteroatoms. The ring atoms may be all carbon atoms, as in “carboarylene groups”, in which case the group is phenylene (C ₆ ). Alternatively, the ring atoms may include one or more heteroatoms, as in “heteroarylene groups”. Examples of heteroarylene groups include, those derived from: N ₁ : pyrrole (azole) (C ₅ ), pyridine (azine) (C ₆ ); O ₁ : furan (oxole) (C ₅ ); S ₁ : thiophene (thiole) (C ₅ ); N ₁ O ₁ : oxazole (C ₅ ), isoxazole (C ₅ ), isoxazine (C ₆ ); N ₂ O ₁ : oxadiazole (furazan) (C ₅ ); N ₃ O ₁ : oxatriazole (C ₅ ); N ₁ S ₁ : thiazole (C ₅ ), isothiazole (C ₅ ); N ₂ : imidazole (1,3-diazole) (C ₅ ), pyrazole (1,2-diazole) (C ₅ ), pyridazine (1,2-diazine) (C ₆ ), pyrimidine (1,3-diazine) (C ₆ ) (e.g., cytosine, thymine, uracil), pyrazine (1,4-diazine) (C ₆ ); and N ₃ : triazole (C ₅ ), triazine (C ₆ ). The term “C _1-n alkyl” as used herein, may be understood to refer to a monovalent moiety obtained by removing a hydrogen atom from a carbon atom of a hydrocarbon compound having from 1 to n carbon atoms, which may be aliphatic or alicyclic, and which may be saturated or unsaturated (e.g. partially unsaturated, fully unsaturated). Thus, the term “alkyl” includes the sub-classes alkenyl, alkynyl, cycloalkyl, etc. For example, where n is 4, the term “C _1-4 alkyl” is used. X may be: , where a = 0 to 5, b = 0 to 16, c = 0 or 1, d = 0 to 5. a may be 0, 1, 2, 3, 4 or 5. In some aspects, a is 0 to 3, optionally a is 0 or 1, preferably a is 0. b may be 0, 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15 or 16. In some aspects, b is 0 to 12, optionally b is 0 to 8, and may preferably be 0, 2, 4 or 8. c may be 0 or 1. d may be 0, 1, 2, 3, 4 or 5. In some aspects, d is 0 to 3, optionally d is 1 or 2, preferably d is 2. In some aspects of X, a is 0, c is 1 and d is 2, and b may be from 0 to 8. In some of these aspects, b is 0, 4 or 8. X may be: where a = 0 to 5, b1 = 0 to 16, b2 = 0 to 16, c1 = 0 or 1, c2 = 0 or 1, d = 0 to 5. a may be 0, 1, 2, 3, 4 or 5. a may be 0 to 3, optionally 0 or 1. a may be 0. a may be 1. b1 may be 0, 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15 or 16. b1 may be 0 to 12, optionally 0 to 8 (e.g., 0, 2, 3, 4, 5 or 8). b1 may be 2. b2 may be 0, 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15 or 16. b2 may be 0 to 12, optionally 0 to 8 (e.g., 0, 2, 4, 5 or 8). b2 may be 8. Only one of b1 and b2 may not be 0. c1 may be 0 or 1. c2 may be 0 or 1. Only one of c1 and c2 may not be 0. d may be 0, 1, 2, 3, 4 or 5, optionally 0 to 3. d may be 1 or 2, optionally 2. d may be 5. In some aspects of X, a is 0, b1 is 0, c1 is 1, c2 is 0 and d is 2, and b2 may be from 0 to 8; optionally b2 is 0, 4, 5 or 8, preferably b2 is 8. In some aspects of X, a is 1, b2 is 0, c1 is 0, c2 is 1, d is 2, and b1 may be from 0 to 8, optionally b1 is 2. In some further instances of X, a = 0 to 5, b1 = 0, b2 = 0 to 16, c1 = 0 or 1, c2 = 0 and d = 0 to 5. In such cases: a may be 0, 1, 2, 3, 4 or 5, optionally a is 0 to 3, preferably a is 0 or 1. a may be 0. b2 may be 0, 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15 or 16. b2 may be 0 to 12, optionally b2 is 0 to 8 (e.g., 0, 2, 4 or 8). c1 may be 0 or 1. d may be 0, 1, 2, 3, 4 or 5, optionally d is 0 to 3. d may be 1 or 2, optionally 2. In some of these further instances of X, a is 0, c2 is 1 and d is 2, and b2 may be from 0 to 8, optionally b2 is 0, 4 or 8. In some aspects, the linker L may be a Gly3-PEG-N3 linker. In some such aspects, sortase- mediated conjugation of antibodies with a Gly3-PEG-N3 linker is used to generate an azide reactive intermediate. This intermediate may then be used to conjugate a drug unit to the antibody. The structure of the Gly3-PEG3-N3 linker is shown below: Pharmaceutical compositions The present invention also provides pharmaceutical compositions comprising the antibodies or antibody drug conjugates described herein. Preferably, the pharmaceutical compositions further comprise a pharmaceutically acceptable carrier. As used herein, "pharmaceutically acceptable carrier" includes any and all solvents, dispersion media, coatings, antibacterial and antifungal agents, isotonic and absorption delaying agents, and the like that are physiologically compatible. Preferably, the carrier is suitable for parenteral, e.g. intravenous, intramuscular or subcutaneous administration (e.g., by injection or infusion). Remington’s Pharmaceutical Sciences, by E. W. Martin, Mack Publishing Co., Easton, PA, 19th Edition, 1995, describes compositions and formulations suitable for pharmaceutical delivery of the antibodies or antibody drug conjugates described herein. Preferred pharmaceutically acceptable carriers comprise aqueous carriers or diluents. Examples of suitable aqueous carriers that may be employed in the pharmaceutical compositions of the invention include water, buffered water and saline. Examples of other carriers include aqueous dextrose, glycerol, ethanol, polyols (such as glycerol, propylene glycol, polyethylene glycol, and the like), and suitable mixtures thereof, vegetable oils, such as olive oil, and injectable organic esters, such as ethyl oleate. Proper fluidity can be maintained, for example, by the use of coating materials, such as lecithin, by the maintenance of the required particle size in the case of dispersions, and by the use of surfactants. In many cases, it will be preferable to include isotonic agents, for example, sugars, polyalcohols such as mannitol, sorbitol, or sodium chloride in the composition. Therapeutic compositions typically must be sterile and stable under the conditions of manufacture and storage. The composition can be formulated as a solution, microemulsion, liposome, or other ordered structure suitable to high drug concentration. Sterile injectable solutions can be prepared by incorporating the active agent (e.g. antibody) in the required amount in an appropriate solvent with one or a combination of ingredients enumerated above, as required, followed by sterilization microfiltration. Pharmaceutical compositions of the invention may comprise additional active ingredients as well as an antibody or antibody drug conjugate of the invention. For example, the pharmaceutical compositions may further comprise additional therapeutic or prophylactic agents. An antibody or fragment thereof, or an antibody drug conjugate, of the present invention, or a pharmaceutical composition comprising said antibody, fragment, or antibody drug conjugate, may be administered via one or more routes of administration using one or more of a variety of methods known in the art. As will be appreciated by the skilled artisan, the route and/or mode of administration will vary depending upon the desired results. Preferably, the antibodies, conjugates or pharmaceutical compositions of the invention may be administered by parenteral administration. The phrase "parenteral administration" as used herein means modes of administration other than enteral and topical administration, usually by injection. Preferred routes of administration for antibodies, conjugates or compositions of the invention include intravenous, intramuscular, intradermal, intraperitoneal, subcutaneous, spinal or other parenteral routes of administration, for example by injection or infusion. Alternatively, an antibody, conjugate or pharmaceutical composition of the invention can be administered via a non-parenteral route, such as a topical, epidermal or mucosal route of administration. Local administration is also possible, including peritumoral, juxtatumoral, intratumoral, intralesional, perilesional, intra cavity infusion, intravesicle administration, and inhalation. A suitable dosage of an antibody or antibody drug conjugate of the invention may be determined by a skilled medical practitioner. Actual dosage levels of the active ingredients in the pharmaceutical compositions of the present invention may be varied so as to obtain an amount of the active ingredient which is effective to achieve the desired therapeutic response for a particular patient, composition, and mode of administration, without being toxic to the patient. The selected dosage level will depend upon a variety of pharmacokinetic factors including the activity of the particular antibody employed, the route of administration, the time of administration, the rate of excretion of the antibody, the duration of the treatment, other drugs, compounds and/or materials used in combination with the particular compositions employed, the age, sex, weight, condition, general health and prior medical history of the patient being treated, and like factors well known in the medical arts. A suitable dose of an antibody or conjugate of the invention may be, for example, in the range of from about 100 ng/kg to about 25 mg/kg body weight of the patient to be treated per day. For example, a suitable dosage may be from about 1µg/kg to about 10mg/kg body weight per week, from about 100µg/kg to about 10mg/kg body weight per week or from about 10 µg/kg to about 5 mg/kg body weight per week. A suitable dosage may be from about 1µg/kg to about 10mg/kg body weight per day, from about 100µg/kg to about 10mg/kg body weight per day or from about 10 µg/kg to about 5 mg/kg body weight per day. Dosage regimens may be adjusted to provide the optimum desired response (e.g., a therapeutic response). For example, a single dose may be administered, several divided doses may be administered over time or the dose may be proportionally reduced or increased as indicated by the requirements of the therapeutic situation. It is especially advantageous to formulate compositions for parenteral administration in dosage unit form for ease of administration and uniformity of dosage. Dosage unit form as used herein refers to physically discrete units suited as unitary dosages for the subjects to be treated; each unit contains a predetermined quantity of active compound calculated to produce the desired therapeutic or conditioning effect in association with the required pharmaceutical carrier. The antibodies or antibody drug conjugates described herein may be administered in a single dose or in multiple doses. The multiple doses may be administered via the same or different routes and to the same or different locations. Alternatively, antibodies can be administered as a sustained release formulation, in which case less frequent administration is required. Dosage and frequency may vary depending on the half-life of the antibody in the patient and the duration of treatment that is desired. Described herein is a pharmaceutical composition comprising an antibody, or fragment thereof, of the invention and optionally a pharmaceutically acceptable carrier. The pharmaceutical composition may comprise any antibody of the invention as described herein. In some aspects, the pharmaceutical composition may comprise an antibody of the first antibody group as described herein and optionally a pharmaceutically acceptable carrier. In some aspects, the pharmaceutical composition may comprise an antibody of the second antibody group as described herein and optionally a pharmaceutically acceptable carrier. Thus, the pharmaceutical composition may comprise a single antibody species of the invention. In some aspects, the pharmaceutical composition may comprise a first antibody of the invention and a second, different antibody of the invention and optionally a pharmaceutically acceptable carrier; optionally wherein, the first antibody may be an antibody of the first antibody group as described herein and the second antibody may be an antibody of the second antibody group as described herein. Thus, the pharmaceutical composition may comprise two different species of the antibodies of the invention within the same composition. The present invention also provides for the concurrent administration of two different pharmaceutical compositions each comprising a single but different species of antibody of the invention, as will be described in more detail herein. Thus, in some aspects there is provided a pharmaceutical composition comprising a monoclonal antibody or fragment thereof that specifically binds human CD45, comprising a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a LCDR1, a LCDR2 and a LCDR3, and wherein the heavy chain variable domain comprises a HCDR1, a HCDR2 and a HCDR3, wherein LCDR1 comprises the sequence of SEQ ID NO: 3, LCDR2 comprises the sequence of SEQ ID NO: 4, and LCDR3 comprises the sequence of SEQ ID NO: 5, and HCDR1 comprises the sequence of SEQ ID NO: 6, HCDR2 comprises the sequence of SEQ ID NO: 7, and HCDR3 comprises the sequence of SEQ ID NO: 8, preferably wherein the light chain variable domain comprises a sequence of SEQ ID NO: 1, and wherein the heavy chain variable domain comprises a sequence of SEQ ID NO: 2 (i.e., an antibody of the first antibody group as described herein); and optionally a pharmaceutically acceptable carrier. In some aspects there is provided a pharmaceutical composition comprising a monoclonal antibody or fragment thereof that specifically binds human CD45, comprising a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a LCDR1, a LCDR2 and a LCDR3, and wherein the heavy chain variable domain comprises a HCDR1, a HCDR2 and a HCDR3, wherein LCDR1 comprises the sequence of SEQ ID NO: 13, LCDR2 comprises the sequence of SEQ ID NO: 14, and LCDR3 comprises the sequence of SEQ ID NO: 15, and HCDR1 comprises the sequence of SEQ ID NO: 16, HCDR2 comprises the sequence of SEQ ID NO: 17, and HCDR3 comprises the sequence of SEQ ID NO: 18, preferably wherein the light chain variable domain comprises a sequence of SEQ ID NO: 11, and wherein the heavy chain variable domain comprises a sequence of SEQ ID NO: 12 (i.e., an antibody of the second antibody group as described herein); and optionally a pharmaceutically acceptable carrier. In some aspects, there is provided a pharmaceutical composition comprising (i) a monoclonal antibody or fragment thereof that specifically binds human CD45, comprising a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a LCDR1, a LCDR2 and a LCDR3, and wherein the heavy chain variable domain comprises a HCDR1, a HCDR2 and a HCDR3, wherein LCDR1 comprises the sequence of SEQ ID NO: 3, LCDR2 comprises the sequence of SEQ ID NO: 4, and LCDR3 comprises the sequence of SEQ ID NO: 5, and HCDR1 comprises the sequence of SEQ ID NO: 6, HCDR2 comprises the sequence of SEQ ID NO: 7, and HCDR3 comprises the sequence of SEQ ID NO: 8, preferably wherein the light chain variable domain comprises a sequence of SEQ ID NO: 1, and wherein the heavy chain variable domain comprises a sequence of SEQ ID NO: 2; (i.e., an antibody of the first antibody group as described herein); (ii) a monoclonal antibody or fragment thereof that specifically binds human CD45, comprising a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a LCDR1, a LCDR2 and a LCDR3, and wherein the heavy chain variable domain comprises a HCDR1, a HCDR2 and a HCDR3, wherein LCDR1 comprises the sequence of SEQ ID NO: 13, LCDR2 comprises the sequence of SEQ ID NO: 14, and LCDR3 comprises the sequence of SEQ ID NO: 15, and HCDR1 comprises the sequence of SEQ ID NO: 16, HCDR2 comprises the sequence of SEQ ID NO: 17, and HCDR3 comprises the sequence of SEQ ID NO: 18, preferably wherein the light chain variable domain comprises a sequence of SEQ ID NO: 11, and wherein the heavy chain variable domain comprises a sequence of SEQ ID NO: 12; (i.e., an antibody of the second antibody group as described herein); and optionally (iii) a pharmaceutically acceptable carrier. There is also provided herein a pharmaceutical composition comprising a biparatopic antibody, or biparatopic fragment thereof, as disclosed herein, and optionally a pharmaceutically acceptable carrier. There is also provided herein a pharmaceutical composition comprising a bispecific antibody, or bispecific fragment thereof, as disclosed herein, and optionally a pharmaceutically acceptable carrier. In some aspects, there is provided a pharmaceutical composition comprising a biparatopic antibody or biparatopic fragment thereof, that specifically binds human CD45, comprising a first antigen binding domain and a second antigen binding domain, wherein: (i) the first antigen binding domain comprises a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a LCDR1 comprising the sequence of SEQ ID NO: 3, a LCDR2 comprising the sequence of SEQ ID NO: 4, and a LCDR3 comprising the sequence of SEQ ID NO: 5, and wherein the heavy chain variable domain comprises a HCDR1 comprising the sequence of SEQ ID NO: 6, a HCDR2 comprising the sequence of SEQ ID NO: 7, and a HCDR3 comprising the sequence of SEQ ID NO: 8; preferably wherein the light chain variable domain comprises a sequence of SEQ ID NO: 1, and wherein the heavy chain variable domain comprises a sequence of SEQ ID NO: 2; and (ii) the second antigen binding domain comprises a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a LCDR1 comprising the sequence of SEQ ID NO: 13, a LCDR2 comprising the sequence of SEQ ID NO: 14, and a LCDR3 comprising the sequence of SEQ ID NO: 15, and wherein the heavy chain variable domain comprises a HCDR1 comprising the sequence of SEQ ID NO: 16, a HCDR2 comprising the sequence of SEQ ID NO: 17, and a HCDR3 comprising the sequence of SEQ ID NO: 18; preferably wherein the light chain variable domain comprises a sequence of SEQ ID NO: 11, and wherein the heavy chain variable domain comprises a sequence of SEQ ID NO: 12. Thus, the present invention provides a pharmaceutical composition comprising one or more antibodies of the invention, or antibody drug conjugates thereof, and optionally a pharmaceutically acceptable carrier. The present invention provides a pharmaceutical composition comprising an antibody drug conjugate of the invention, and optionally a pharmaceutically acceptable carrier. For example, in such pharmaceutical compositions, the antibody (Ab) of the antibody drug conjugate may be an antibody of the first antibody group, an antibody of the second antibody group, a biparatopic antibody or a bispecific antibody as described herein, or any fragment thereof as described herein. Also provided is a pharmaceutical composition comprising a first antibody drug conjugate of the invention, and a second, different antibody drug conjugate of the invention; and optionally a pharmaceutically acceptable carrier. In such aspects, the second antibody drug conjugate may differ from the first by comprising a different antibody (Ab) or by comprising a different drug (D or (L-D)). For example, in some aspects the pharmaceutical composition may comprise a first antibody drug conjugate of the invention and a second, different antibody drug conjugate of the invention, wherein the antibody (Ab) of both the first and second antibody drug conjugates is an antibody of the first antibody group as described herein, and (L–D) of the first antibody drug conjugate is different from (L–D) of the second antibody drug conjugate. In some aspects the pharmaceutical composition may comprise a first antibody drug conjugate of the invention and a second, different antibody drug conjugate of the invention, wherein the antibody (Ab) of both the first and second antibody drug conjugates is an antibody of the second antibody group as described herein, and (L–D) of the first antibody drug conjugate is different from (L–D) of the second antibody drug conjugate. In some aspects the pharmaceutical composition may comprise a first antibody drug conjugate of the invention and a second, different antibody drug conjugate of the invention, wherein the antibody (Ab) of the first antibody drug conjugate is an antibody of the first antibody group as described herein, and the antibody (Ab) of the second antibody drug conjugate is an antibody of the second antibody group as described herein; and (L– D) of the first antibody drug conjugate is the same as (L–D) of the second antibody drug conjugate. In some aspects the pharmaceutical composition may comprise a first antibody drug conjugate of the invention and a second, different antibody drug conjugate of the invention, wherein the antibody (Ab) of the first antibody drug conjugate is an antibody of the first antibody group as described herein, and Ab of the second antibody drug conjugate is an antibody of the second antibody group as described herein; and (L–D) of the first antibody drug conjugate is different from (L–D) of the second antibody drug conjugate. Typically where (L-D) is different, it is the drug (D) that is different, thereby conferring possibly different properties on the antibody drug conjugate, but different drug may be attached by different linkers, such that the identity of (L-D) as a whole is different. As discussed above, in some aspects, the antibody of the first antibody group as described herein may be a monoclonal antibody or fragment thereof that specifically binds human CD45, comprising a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a LCDR1 comprising the sequence of SEQ ID NO: 3, a LCDR2 comprising the sequence of SEQ ID NO: 4, and a LCDR3 comprising the sequence of SEQ ID NO: 5, and the heavy chain variable domain comprises a HCDR1 comprising the sequence of SEQ ID NO: 6, a HCDR2 comprising the sequence of SEQ ID NO: 7, and a HCDR3 comprising the sequence of SEQ ID NO: 8, preferably wherein the light chain variable domain comprises a sequence of SEQ ID NO: 1, and wherein the heavy chain variable domain comprises a sequence of SEQ ID NO: 2. Similarly, in some aspects, the antibody of the second antibody group as described herein may be a monoclonal antibody or fragment thereof that specifically binds human CD45, comprising a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a LCDR1 comprising the sequence of SEQ ID NO: 13, a LCDR2 comprising the sequence of SEQ ID NO: 14, and a LCDR3 comprising the sequence of SEQ ID NO: 15, and the heavy chain variable domain comprises a HCDR1 comprising the sequence of SEQ ID NO: 16, a HCDR2 comprising the sequence of SEQ ID NO: 17, and a HCDR3 comprising the sequence of SEQ ID NO: 18, preferably wherein the light chain variable domain comprises a sequence of SEQ ID NO: 11, and wherein the heavy chain variable domain comprises a sequence of SEQ ID NO: 12. The present invention also provides a pharmaceutical composition comprising an antibody drug conjugate, and optionally a pharmaceutically acceptable carrier, wherein the antibody (Ab) of the antibody drug conjugate is a biparatopic antibody, or biparatopic fragment thereof, as described herein. The present invention also provides a pharmaceutical composition comprising an antibody drug conjugate, and optionally a pharmaceutically acceptable carrier, wherein the antibody (Ab) of the antibody drug conjugate is a bispecific antibody, or bispecific fragment thereof, as described herein. The present invention also provides a pharmaceutical composition comprising an antibody drug conjugate, and optionally a pharmaceutically acceptable carrier, wherein the antibody (Ab) of the antibody drug conjugate is a biparatopic antibody or biparatopic fragment thereof, that specifically binds human CD45, comprising a first antigen binding domain and a second antigen binding domain, wherein: (i) the first antigen binding domain comprises a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a LCDR1 comprising the sequence of SEQ ID NO: 3, a LCDR2 comprising the sequence of SEQ ID NO: 4, and a LCDR3 comprising the sequence of SEQ ID NO: 5, and wherein the heavy chain variable domain comprises a HCDR1 comprising the sequence of SEQ ID NO: 6, a HCDR2 comprising the sequence of SEQ ID NO: 7, and a HCDR3 comprising the sequence of SEQ ID NO: 8; preferably wherein the light chain variable domain comprises a sequence of SEQ ID NO: 1, and wherein the heavy chain variable domain comprises a sequence of SEQ ID NO: 2; and (ii) the second antigen binding domain comprises a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a LCDR1 comprising the sequence of SEQ ID NO: 13, a LCDR2 comprising the sequence of SEQ ID NO: 14, and a LCDR3 comprising the sequence of SEQ ID NO: 15, and wherein the heavy chain variable domain comprises a HCDR1 comprising the sequence of SEQ ID NO: 16, a HCDR2 comprising the sequence of SEQ ID NO: 17, and a HCDR3 comprising the sequence of SEQ ID NO: 18; preferably wherein the light chain variable domain comprises a sequence of SEQ ID NO: 11, and wherein the heavy chain variable domain comprises a sequence of SEQ ID NO: 12; and wherein (L-D) is as described herein. The antibodies (which includes the biparatopic and bispecific antibodies described herein), antibody drug conjugates or pharmaceutical compositions described herein may be administered in combination with one or more other therapeutic agents. For example, the antibodies, antibody drug conjugates or pharmaceutical compositions of the invention may be administered in combination with other agents for myelosuppression, and/or other agents for immunosuppression. In some aspects, the antibodies, antibody drug conjugates or pharmaceutical compositions of the invention may be administered in combination with one or more immunosuppressive agents selected from Alemtuzumab, anti-thymocyte globulin (ATG), fludarabine, cyclophosphamide, and low dose (<5Gy) total body irradiation. Alternatively, the antibodies, antibody drug conjugates or pharmaceutical compositions of the invention may be administered with other agents for cytoreduction/myelosuppression, such as busulphan, treosulphan, thiotepa, melphalan, etoposide, total body irradiation. In some aspects, the antibodies, antibody drug conjugates or pharmaceutical compositions of the invention may be administered without said agents for cytoreduction/myelosuppression, and/or without said immunosuppressive agents. In some aspects, the antibodies, antibody drug conjugates or pharmaceutical compositions of the invention may be administered in combination with a therapeutically effective amount of one or more chemotherapeutic agents, such as daunorubicin, mitoxantrone, doxorubicin, cytarabine, cyclophosphamide, ifosfamide, steroids, vincristine, Asparaginase, nelarabine, cisplatin, bortezimib, lenalidomide. In some aspects, the antibodies, antibody drug conjugates or pharmaceutical compositions of the invention may be administered in combination with Rituximab or ibrutinib. In these aspects, the one or more further agents may be formulated within the same pharmaceutical composition as the antibodies and/or antibody drug conjugates; or preferably, the one or more further agents may be formulated in one or more separate pharmaceutical composition. The further agents may be administered concurrently with the antibodies, antibody drug conjugates or pharmaceutical compositions of the invention. The antibody, antibody drug conjugate or pharmaceutical composition of the invention may be administered before, after or concurrently with the one or more further agents. The antibody, antibody drug conjugate or pharmaceutical composition of the invention may be administered in combination with or sequentially to, for example, cytotoxic agents, anti-cancer agents, tumour targeting antibodies, target therapy, pathway inhibitors, immunosuppressive agent or myelosuppressive agents. Further the antibody, antibody drug conjugate or pharmaceutical composition of the invention may also be combined with local radiation. Medical uses and methods of treatment The primary therapeutic applications of the antibodies (which includes the biparatopic and bispecific antibodies described herein) and antibody drug conjugates of the invention include in the treatment of cancer, particularly haematological cancers, and in conditioning subjects for bone marrow or haematopoietic stem cell transplant and gene therapy. As used herein, the term “conditioning” may be understood to mean the process of preparing a subject for transplantation with a preparation containing haematopoietic stem cells, or for gene therapy, by selectively depleting (i.e., by cell killing) the subject’s autologous haematopoietic stem cells, haematopoietic progenitor cells, and/or leukocytes, to provide a niche for engraftment of the transplanted cells. The antibodies of the invention exert targeted cell killing activity, for example through ADCC or CDC mechanisms, of cells expressing CD45 (i.e., CD45-positive cells). Typically such cells are those of the haematopoietic system. The antibody drug conjugates of the invention include a drug unit (D) that has an anti-cancer, cytotoxic or cytostatic effect. Thus, the antibody drug conjugates of the invention can selectively deliver an effective dose of a cytotoxic agent to target CD45- positive cells. The antibody drug conjugates may exhibit enhanced cell killing activity as compared to the antibodies alone (i.e., more potent toxicity), which can advantageously allow a lower efficacious dose to be achieved using the antibody drug conjugates. Thus, the present invention provides the antibodies, antibody drug conjugates or pharmaceutical compositions of the invention for use in therapy. Haematological cancer treatment In some aspects, the present invention provides a method of treating haematological cancer, the method comprising administering an antibody of the invention (e.g., an antibody of the first antibody group, an antibody of the second antibody group, a biparatopic antibody, a bispecific antibody etc. as described herein), an antibody drug conjugate of the invention, or a pharmaceutical composition of the invention, to a subject in need thereof. In some aspects, the present invention provides an antibody of the invention, an antibody drug conjugate of the invention, or a pharmaceutical composition of the invention for use in a method of treating haematological cancer, the method comprising administering said antibody, antibody drug conjugate or pharmaceutical composition to a subject in need thereof. The present invention also provides a method of treating haematological cancer, the method comprising administering a first antibody of the invention, and a second, different antibody of the invention, to a subject in need thereof. The present invention also provides a method of treating haematological cancer, the method comprising administering a first antibody of the invention to a subject in need thereof, wherein the subject has been, is being, or will be administered a second, different antibody of the invention. The present invention further provides a first antibody of the invention and a second, different antibody of the invention, for use in a method of treating haematological cancer, wherein the method comprises administering the first antibody and the second antibody to a subject in need thereof. The present invention also provides a first antibody of the invention, for use in a method of treating haematological cancer, wherein the method comprises administering the first antibody, and a second, different antibody of the invention, to a subject in need thereof. In some aspects, the first antibody may be an antibody of the first antibody group, as described herein, and the second antibody may be an antibody of the second antibody group, as described herein. In some aspects, the first antibody may be an antibody of the second antibody group, as described herein, and the second antibody may be an antibody of the first antibody group, as described herein. In some aspects the first antibody and the second antibody are administered to the subject within the same pharmaceutical composition. In some other preferred aspects, the first antibody and the second antibody are administered to the subject as two separate pharmaceutical compositions. In some aspects the first antibody and the second antibody are administered to the subject concurrently. In some aspects the first antibody is administered to the subject before the second antibody is administered to the subject. In some aspects the first antibody is administered to the subject immediately before the second antibody is administered to the subject. In some aspects the first antibody is administered to the subject at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 24, 36, 48, or 72 hours before, preferably at least 2 hours before, most preferably at least 12 hours before, the second antibody is administered to the subject. In some aspects the first antibody is administered to the subject at least 1, 2, 3, 4, 5, 7, 10, 14, 21, 28, 35, 42, or 49 days before, preferably at least 1 day, most preferably at least 7 days, before the second antibody is administered to the subject. The present invention also provides a method of treating haematological cancer, the method comprising administering a first antibody drug conjugate of the invention, and a second, different antibody drug conjugate of the invention, to a subject in need thereof. The present invention also provides a method of treating haematological cancer, the method comprising administering a first antibody drug conjugate of the invention to a subject in need thereof, wherein the subject has been, is being, or will be administered a second, different antibody drug conjugate of the invention. The present invention further provides a first antibody drug conjugate of the invention and a second, different antibody drug conjugate of the invention, for use in a method of treating haematological cancer, wherein the method comprises administering the first antibody drug conjugate and the second antibody drug conjugate, to a subject in need thereof. The present invention also provides a first antibody drug conjugate of the invention, for use in a method of treating haematological cancer, wherein the method comprises administering the first antibody drug conjugate and a second, different antibody drug conjugate of the invention, to a subject in need thereof. In some aspects the antibody (Ab) of the first antibody drug conjugate is an antibody of the first antibody group described herein, and the antibody (Ab) of the second antibody drug conjugate is an antibody of the second antibody group described herein. In such aspects, the drug (D or (L-D)) of the first antibody drug conjugate may be different from, or the same as, the drug (D or (L-D)) of the second antibody drug conjugate. In some aspects the antibody (Ab) of the first antibody drug conjugate is an antibody of the second antibody group described herein, and the antibody (Ab) of the second antibody drug conjugate is an antibody of the first antibody group described herein. In such aspects, the drug (D or (L-D)) of the first antibody drug conjugate may be different from, or the same as, the drug (D or (L-D)) of the second antibody drug conjugate. In some aspects the antibody (Ab) of both the first antibody drug conjugate and the second antibody drug conjugate is an antibody of the first antibody group described herein, and the drug (D or (L-D)) of the first antibody drug conjugate is different from the drug (D or (L-D)) of the second antibody drug conjugate. In some aspects the antibody (Ab) of both the first antibody drug conjugate and the second antibody drug conjugate is an antibody of the second antibody group described herein, and the drug (D or (L-D)) of the first antibody drug conjugate is different from the drug (D or (L-D)) of the second antibody drug conjugate. In some aspects the first antibody drug conjugate and the second antibody drug conjugate are administered to the subject within the same pharmaceutical composition. In some other preferred aspects, the first antibody drug conjugate and the second antibody drug conjugate are administered to the subject as two separate pharmaceutical compositions. In some aspects the first antibody drug conjugate and the second antibody drug conjugate are administered to the subject concurrently. In some aspects the first antibody drug conjugate is administered to the subject before the second antibody drug conjugate is administered to the subject. In some aspects the first antibody drug conjugate is administered to the subject immediately before the second antibody drug conjugate is administered to the subject. In some aspects the first antibody drug conjugate is administered to the subject at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 24, 36, 48, or 72 hours before, preferably at least 2 hours before, most preferably at least 12 hours before, the second antibody drug conjugate is administered to the subject. In some aspects the first antibody drug conjugate is administered to the subject at least 1, 2, 3, 4, 5, 7, 10, 14, 21, 28, 35, 42, or 49 days before, preferably at least 1 day, most preferably at least 7 days, before the second antibody drug conjugate is administered to the subject. In some aspects the haematological cancer comprises CD45-expressing cells. In some aspects the haematological cancer may be CD45-positive. In some aspects, the cancer may be selected from the group consisting of acute myeloid leukaemia, acute lymphoblastic leukaemia, chronic lymphocytic leukaemia, chronic myeloid leukaemia, myelodysplasia, multiple myeloma, non- Hodgkin’s lymphoma and Hodgkin’s disease. The subject may be a mammal, preferably the subject is a human. Typically the subject is a human (e.g., a patient) in need of treatment for haematological cancer, i.e., a subject having, or suspected of having, haematological cancer. In some aspects, the subject has been diagnosed as having haematological cancer, and is therefore in need of treatment as described herein. In some aspects the methods may further comprise administering one or more other therapeutic agents. For example, the methods may further comprise administering one or more anti-cancer agents. In some aspects the methods further comprise administering to the subject radiation and/or chemotherapy. In some aspects, the methods further comprise administering to the subject one or more of enasidenib, gilteritinib, ivosidenib, midostaurin, fludarabine, cyclophosphamide, rituximab, bendamustine, chlorambucil, ibrutinib, idelalisib, obinutuzumab, ofatumumab, prednisolone, brentuximab vedotin, lenalidomide, pomalidomide, carfilzomib, daratumumab, thalidomide, panobinostat, bortezomib, all-trans retinoic acid, arsenic trioxide, idarubicin, daunorubicin, cytarabine, azacitidine, mitoxantrone, cytarabine, etoposide, gemtuzumab, 5- azacytidine, hydroxyurea, midostaurin , vincristine, steroids, doxorubicin, asparaginase, ifosfamide, methotrexate, nelarabine, melphalan, bendamustine, carmustine (bis-chloroethylnitrosourea, BCNU), cis platin, carboplatin, busulphan, treosulphan, thiotepa, or total body irradiation. In some preferred aspects, the methods further comprise administering to the subject one or more cancer treatment(s) selected from: daunorubicin, idarubicin, mitoxantrone, cytarabine, etoposide, fludarabine, gemtuzumab, 5-azacytidine, hydroxyurea, midostaurin, vincristine, steroids, doxorubicin, asparaginase, cyclophosphamide, ifosfamide, methotrexate, nelarabine, daratumumab, melphalan, thalidomide, lenolidamide, bortezimib, pomalidomide, carfolizimib, bendamustine, carmustine (bis-chloroethylnitrosourea, BCNU), cis platin, carboplatin, rituximab, ofatumumab, obinutuzumab, ibrutinib, idelasalib, and brentuximab. In some aspects, the methods further comprise administering to the subject one or more conditioning agent(s) selected from: busulphan, treosulphan, thiotepa, and total body irradiation. In such aspects, the further therapeutic agents may be formulated within the same pharmaceutical composition as the antibodies or antibody drug conjugates of the invention; or preferably, the further therapeutic agents may be administered in a separate formulation. The further therapeutic agents may be administered concurrently with the antibodies, antibody drug conjugates or pharmaceutical compositions of the invention. The antibody or antibody drug conjugate may be administered before, after or concurrently with the one or more further agents. Preparing a subject for transplantation of haematopoietic stem cells In some aspects, the present invention provides a method of preparing a subject for transplantation of haematopoietic stem cells, the method comprising administering an antibody of the invention (which includes the biparatopic and bispecific antibodies described herein), an antibody drug conjugate of the invention, or a pharmaceutical composition of the invention, to a subject in need thereof. In some aspects, the present invention provides an antibody of the invention, an antibody drug conjugate of the invention, or a pharmaceutical composition of the invention for use in a method of preparing a subject for transplantation of haematopoietic stem cells, the method comprising administering said antibody, antibody drug conjugate or pharmaceutical composition to a subject in need thereof. Preparing a subject for transplantation of haematopoietic stem cells may comprise, or consist essentially of, conditioning the subject for engraftment of haematopoietic stem cells. The antibody, antibody drug conjugate or pharmaceutical composition of the invention typically result in cell killing of CD45-positive cells. It is usually advantageous, before transplantation with a preparation containing haematopoietic stem cells or gene therapy, to reduce as far as possible the number of immunological effector cells in the subject's body, preferably to eliminate them entirely. Thus, the antibody, antibody drug conjugate or pharmaceutical composition of the invention provide broad spectrum cell killing of CD45-positive cells, including T-cells, NK cells, lymphocytes and monocytes. This may minimise graft rejection or graft versus host disease following transplantation. As discussed above, in some aspects, preparing a subject for transplantation with haematopoietic stem cells may comprise conditioning the subject for engraftment of haematopoietic stem cells. Thus, it may mean the process of selectively depleting (i.e., by cell killing) the subject’s autologous haematopoietic stem cells and/or leukocytes, to provide a niche for engraftment of transplanted haematopoietic stem cells. In some aspects the methods of the invention may be myeloablative, non-myeloablative or reduced intensity, preferably the methods of the invention provide reduced toxicity myeloablative conditioning. Typically, the subject’s autologous haematopoietic stem cells comprise a defect or mutation, which results in a disorder or disease in the subject. Thus, depleting or substantially eliminating the subject’s autologous haematopoietic stem cells and replacing them with corrected or healthy haematopoietic stem cells provides a treatment for the disease. In some aspects, the haematopoietic stem cells for transplantation into the subject are allogeneic. The term “allogeneic” may be understood in the context of the invention to mean a donor’s haematopoietic stem cells, i.e., the haematopoietic stem cells are isolated or derived from a donor, typically a human donor. The haematopoietic stem cells are not the subject’s own haematopoietic stem cells, i.e., they are not derived from the subject. In some aspects, the allogeneic haematopoietic stem cells for transplantation into the subject are from a healthy donor, i.e., a donor not having the same disease as the subject, or preferably a donor not having any disease. In preferred aspects, the allogeneic haematopoietic stem cells for transplantation into the subject are from a healthy, HLA-matched donor. As used herein, the term “HLA-matched” is used to mean, that the human leukocyte antigen (HLA) types of the donor haematopoietic stem cells are a close match with the subject’s HLA types. In some aspects, the donor and subject have at least 6, preferably at least 8, and most preferably at least 10 matching HLA markers. In some aspects the donor may be haploidentical with the subject (i.e., exactly half of the HLA markers match). In some aspects, the donor may be a sibling, parent or child of the subject. In the methods of the invention, in some aspects, said transplantation of allogeneic haematopoietic stem cells may be for treating a malignant disease or disorder. In some such aspects, the transplantation of allogeneic haematopoietic stem cells may be for treating a disease or disorder selected from the group consisting of: acute myeloid leukaemia, acute lymphoblastic leukaemia, chronic myeloid leukaemia, chronic lymphocytic leukaemia, myelodysplasia, myeloproliferative diseases, non-Hodgkin’s lymphoma and Hodgkin’s disease. Alternatively, in some other aspects, said transplantation of allogeneic haematopoietic stem cells may be for treating a non-malignant disease or disorder. In some such aspects, the transplantation of allogeneic haematopoietic stem cells may be for treating a disease or disorder selected from the group consisting of: severe aplastic anaemia and other bone marrow failure disorders, a primary immunodeficiency, primary haemophagocytic lymphohistiocytosis, a haemoglobinopathy, and a genetic metabolic disease. In some aspects, the transplantation of allogeneic haematopoietic stem cells may be for treating (i) a bone marrow failure disorder such as idiopathic severe aplastic anaemia, Fanconi anaemia, dyskeratosis congenita, severe congenital neutropenia, Shwachman-Diamond Syndrome, or Diamond Blackfan anaemia; (ii) a primary immunodeficiency such as SCID (e.g., newborn SCID), chronic granulomatous disease, Wiskott-Aldrich syndrome, CD40 ligand deficiency, XLP, MHC Class II deficiency, or primary haemophagocytic lymphohistiocytosis; (iii) a haemoglobinopathy such as sickle cell disease, β- thalassaemia major; or (iv) a genetic metabolic disease such as Hurler syndrome, X-linked adrenoleukodystrophy, alpha mannosidosis, or osteopetrosis. In some aspects, the transplantation of allogeneic haematopoietic stem cells may be for treating a disease or disorder selected from the group consisting of: severe aplastic anaemia and other bone marrow failure disorders, a haemoglobinopathy, a primary immunodeficiency, primary haemophagocytic lymphohistiocytosis, a genetic metabolic disease, Fanconi anaemia, dyskeratosis congenita, severe congenital neutropenia, Shwachman-Diamond Syndrome, Diamond-Blackfan syndrome, SCID (e.g., newborn SCID), chronic granulomatous disease, Wiskott-Aldrich syndrome, CD40 ligand deficiency, XLP, MHC Class II deficiency, primary haemophagocytic lymphohistiocytosis, sickle cell disease, β- thalassaemia major, Hurler syndrome, alpha mannosidosis, X-linked adrenoleukodystrophy and osteopetrosis. In such aspects, the subject is a human (e.g., a patient) in need of treatment for one or more of said diseases or disorders, i.e., a subject having, or suspected of having, one or more of said diseases or disorders. In some aspects, the subject has been diagnosed as having one or more of said diseases or disorders, and is therefore in need of treatment as described herein. In some aspects, the allogeneic haematopoietic stem cells for transplantation into the subject are genetically-modified. In such aspects, the transplantation of genetically-modified allogeneic haematopoietic stem cells may be for gene therapy of the subject. Thus, the invention further provides a method of preparing a subject for transplantation of allogeneic genetically-modified haematopoietic stem cells for gene therapy, the method comprising administering an antibody of the invention, an antibody drug conjugate of the invention, or an pharmaceutical composition of the invention. Typically, the subject’s autologous haematopoietic stem cells comprise a deficiency, disease or mutation that results in a disease or disorder. The genetically-modified allogeneic haematopoietic stem cells for transplantation may have been isolated or derived from the donor and treated ex vivo, for example by gene therapy, e.g., by transduction with a viral vector carrying a gene for a desired expression product, or through gene/base editing using for example TALENS or CRISPR technology. Following conditioning with the antibodies, antibody drug conjugates or pharmaceutical compositions of the invention, genetically-modified allogeneic haematopoietic stem cells can be transplanted into the subject, which may be useful for gene therapy for treating a genetic haematological disease or disorder, a primary immunodeficiency or a genetic metabolic disorder. For example, following conditioning with the antibodies, antibody drug conjugates or pharmaceutical compositions of the invention, genetically-modified allogeneic haematopoietic stem cells can be transplanted into the subject for treating Fanconi anaemia, where autologous HSCs are difficult to harvest, or for treating metachromatic leukodystrophy (MLD), where overexpression may be beneficial, or for CAR T cell therapy. In some aspects, the haematopoietic stem cells for transplantation into the subject are autologous. The term “autologous” may be understood in the context of the invention to mean the subject’s own haematopoietic stem cells, i.e., haematopoietic stem cells isolated or derived from the subject. In some aspects, the haematopoietic stem cells for transplantation into the subject may be the subject’s own haematopoietic stem cells. In the methods of the invention, in some aspects, said transplantation of autologous haematopoietic stem cells may be for treating a malignant disease or disorder. In some such aspects, the transplantation of autologous haematopoietic stem cells may be for treating a disease or disorder selected from the group consisting of: multiple myeloma, non- Hodgkin’s lymphoma, and Hodgkin’s disease. In some other aspects, the transplantation of autologous haematopoietic stem cells may be for treating an autoimmune disease or disorder. In some such aspects, the transplantation of autologous haematopoietic stem cells may be for treating a disease or disorder selected from the group consisting of: multiple sclerosis, systemic sclerosis, juvenile inflammatory arthritis, and systemic lupus erythematosus. In some aspects, the transplantation of autologous haematopoietic stem cells may be for treating a disease or disorder selected from the group consisting of: multiple myeloma, non-Hodgkin’s lymphoma, Hodgkin’s disease, an autoimmune disease or disorder, multiple sclerosis, systemic sclerosis, juvenile inflammatory arthritis and systemic lupus erythematosus. In some aspects, the haematopoietic stem cells for transplantation into the subject are autologous and genetically-modified. In such aspects, the transplantation of genetically-modified autologous haematopoietic stem cells may be for gene therapy of the subject. Thus, the invention further provides a method of preparing a subject for transplantation of autologous genetically-modified haematopoietic stem cells for gene therapy, the method comprising administering an antibody of the invention, an antibody drug conjugate of the invention, or an pharmaceutical composition of the invention. Typically, the subject’s autologous haematopoietic stem cells comprise a deficiency, disease or mutation that results in a disease or disorder. The genetically-modified autologous haematopoietic stem cells for transplantation may have been isolated or derived from the subject and treated ex vivo, for example by gene therapy, to correct the deficiency, disease or mutation, so that the haematopoietic stem cells no longer result in the disease or disorder. In some aspects, the genetically-modified haematopoietic stem cells for transplantation comprise, or consist essentially of, autologous haematopoietic stem cells (i.e., haematopoietic stem cells isolated from the subject to be treated), which have been genetically modified, e.g., by transduction with a viral vector carrying a gene for a desired expression product, or through gene/base editing using for example TALENS or CRISPR technology. For example, one or more viral vector(s) comprising a gene encoding the adenosine deaminase (ADA) or β-globin genes can be used in a known manner to insert these genes into haematopoietic stem cells isolated from a subject having an ADA deficiency or a haemoglobinopathy, respectively. Similarly, gene/base editing using CRISPR technology may be used to silence the BCL11A repressor gene to enable expression of γ-globin in haematopoietic stem cells isolated from a subject having sickle cell disease and/or β-thalassaemia. Following conditioning with the antibodies, antibody drug conjugates or pharmaceutical compositions of the invention, transplantation of such gene-corrected (i.e., genetically modified) autologous haematopoietic stem cells can be curative for these disorders. Thus, in some aspects, the haematopoietic stem cells for transplantation into the subject may be genetically-modified autologous haematopoietic stem cells. In the methods of the invention, in some aspects, said transplantation of genetically-modified autologous haematopoietic stem cells may be for gene therapy. In some aspects, the transplantation of genetically-modified autologous haematopoietic stem cells may be for gene therapy for treating a genetic haematological disease or disorder, a primary immunodeficiency or a genetic metabolic disorder. In some aspects, the transplantation of genetically-modified autologous haematopoietic stem cells may be for gene therapy for treating (i) a genetic haematological disease or disorder selected from a haemoglobinopathy, a transfusion dependent haemoglobinopathy, such as sickle cell disease and β- thalassaemia major, and Fanconi anaemia; (ii) a primary immunodeficiency selected from SCID (e.g., newborn SCID), chronic granulomatous disease, Wiskott-Aldrich syndrome and primary HLH; or (iii) a genetic metabolic disorder selected from Hurler’s syndrome, Sanfilippo disease, X- adrenoleukodystrophy, and metachromatic leukodystrophy. In some aspects, the transplantation of genetically-modified autologous haematopoietic stem cells may be for treating a disease or disorder selected from the group consisting of: a genetic haematological disease or disorder, a primary immunodeficiency, a genetic metabolic disorder, sickle cell disease, β- thalassaemia major, Fanconi anaemia, primary HLH, SCID (e.g., newborn SCID), chronic granulomatous disease, Wiskott-Aldrich syndrome, Hurler’s syndrome, Sanfilippo disease, X-adrenoleukodystrophy, and metachromatic leukodystrophy. In some aspects, the haematopoietic stem cells are comprised within a composition. Thus, in some aspects, the methods or medical uses of the invention are for preparing a subject for transplantation of with a composition comprising or consisting essentially of haematopoietic stem cells. The composition may be a pharmaceutical composition and may comprise a pharmaceutically acceptable carrier, as described herein. In some aspects, the subject is, or is intended to be, subsequently administered haematopoietic stem cells, a population of haematopoietic stem cells, or a composition comprising haematopoietic stem cells, wherein the haematopoietic stem cells are allogeneic, autologous or genetically-modified autologous haematopoietic stem cells as described herein. In some aspects, the methods or medical uses of the invention further comprise administering to the subject haematopoietic stem cells, which may be allogeneic, autologous or genetically-modified autologous haematopoietic stem cells as described herein. In some aspects, the methods or medical uses of the invention further comprise administering to the subject a population of haematopoietic stem cells, which may be allogeneic, autologous or genetically- modified autologous haematopoietic stem cells as described herein. In some aspects, the methods or medical uses of the invention further comprise administering to the subject a composition comprising haematopoietic stem cells and optionally a pharmaceutically acceptable carrier, wherein the haematopoietic stem cells are allogeneic, autologous or genetically-modified autologous haematopoietic stem cells as described herein. In seem aspects, the administered haematopoietic stem cells engraft in a target tissue of the subject. Preferably, said target tissue is bone marrow. In some aspects, the present invention provides a method of engrafting stem cells in a subject, the method comprising (a) administering an effective amount of an antibody of the invention, an antibody drug conjugate of the invention, or a pharmaceutical composition of the invention, to the subject; and (b) administering a stem cell population to the subject (preferably to a target tissue of the subject), wherein the administered stem cell population engrafts in a target tissue of the subject. In some aspects, the present invention provides a method of engrafting stem cells in a subject, the method comprising administering an effective amount of an antibody of the invention, an antibody drug conjugate of the invention, or a pharmaceutical composition of the invention, to the subject; wherein the subject is (or is intended to be) subsequently administered a stem cell population (preferably to a target tissue of the subject), wherein the administered stem cell population will engraft in a target tissue of the subject. In some aspects, the present invention provides an antibody of the invention, an antibody drug conjugate of the invention, or a pharmaceutical composition of the invention for use in a method of engrafting stem cells in a subject, the method comprising (a) administering an effective amount of the antibody, antibody drug conjugate, or pharmaceutical composition of the invention, to the subject; and (b) administering a stem cell population to the subject (preferably to a target tissue of the subject), wherein the administered stem cell population engrafts in a target tissue of the subject. Preferably, the stem cells are haematopoietic stem cells, which may be allogeneic, autologous or genetically-modified autologous haematopoietic stem cells as described herein. Preferably, the target tissue is bone marrow. A method of engrafting stem cells in a subject may describe the process of depleting or substantially eliminating (e.g., by cell killing) a subject’s autologous stem cells, which may comprise a mutation or defect that is causing a disease or disorder in the subject, to make space in the bone marrow stem cell niche for replacement of the subject’s autologous stem cells with healthy stem cells. Said healthy stem cells may be from a healthy donor or may be produced from stem cells that have been isolated from the subject and treated by gene therapy to correct the defect or mutation that is causing the disease or disorder in the subject, as described above. The stem cells are typically haematopoietic stem cells. The stem cell population may comprise or consist essentially of haematopoietic stem cells. In some aspects, the stem cell population comprises exogenous stem cells, e.g., isolated from a healthy donor. In some aspects, the stem cell population comprises the subject’s autologous stem cells, e.g., that have been genetically modified to correct a disease or genetic defect. The stem cell population typically comprises healthy or corrected stem cells, preferably healthy or corrected haematopoietic stem cells. The healthy stem cells, preferably healthy haematopoietic stem cells are typically from a healthy donor, as described above. The corrected stem cells, preferably corrected haematopoietic stem cells are typically from the subject (i.e., are autologous) and treated ex vivo with gene therapy to correct the defect or mutation that is causing the disease or disorder in the subject, as described above. The healthy or corrected stem cells are typically transplanted into the subject and engraft in the target tissue of the subject. The target tissue may be any tissue to which the stem cell population may be targeted. The target tissue is preferably bone marrow. Thus, the healthy or corrected stem cells are typically haematopoietic stem cells and once transplanted, integrate into the subject’s haematopoietic system, in the bone marrow. As used herein the term “stem cells” refers to undifferentiated or partially differentiated cells that can differentiate into various types of cells and proliferate indefinitely to produce more of the same stem cell. Typically, stem cells are the earliest type of cell in a cell lineage and are defined by their ability to form multiple cell types (multi potency) and their ability to self-renew. As used herein, “haematopoietic stem cells” refers to stem cells that can differentiate into the hematopoietic lineage and give rise to all blood cell types such as white blood cells and red blood cells, including myeloid (e.g., monocytes and macrophages, neutrophils, basophils, eosinophils, erythrocytes, megakaryocytes/platelets, dendritic cells), and lymphoid lineages (e.g., T-cells, B-cells, NK-cells). Human hematopoietic stem cells can be identified, for example by cell surface markers such as CD34+, CD90+, CD49f+, CD38- and CD45RA-. As used herein the term “effective amount” may be understood to mean and amount of the antibody, antibody drug conjugate or pharmaceutical composition of the invention that is sufficient to have the desired effect. Typically it is an amount sufficient to deplete or substantially eliminate the subject’s autologous haematopoietic stem cell population. The skilled practitioner is readily capable of determining an effective amount. In some aspects, the stem cell population is administered to the target tissue of the subject after the antibody, antibody drug conjugate or pharmaceutical composition has cleared or dissipated from the subject's target tissue. This prevent or reduces a cytotoxic effect on the administered stem cell population. Accordingly, in some aspects, the stem cell population is administered to the subject after the concentration of the antibody, antibody drug conjugate or pharmaceutical composition in the subject’s target tissue has been reduced to an undetectable concentration. The period of time necessary to clear the antibody, antibody drug conjugate or pharmaceutical composition from the subject’s target tissue may be determined using routine means available to one of skill in the art, for example, by detecting the concentration of the antibody, antibody drug conjugate or pharmaceutical composition in the subject’s target tissue. In some aspects, the stem cell population is administered to the target tissue of the subject after the antibody, antibody drug conjugate or pharmaceutical composition has substantially cleared from the subject’s target tissue. In some aspects “substantially cleared” means that the level of antibody, antibody drug conjugate or pharmaceutical composition of the invention remaining in the target tissue of the subject does not induce significant cell death in the transplanted stem cell population. For example, the stem cell population may be administered to the target tissue of the subject at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 18, 21 or more days, preferably at least 1 day, most preferably at least 2 days, after the administration of the antibody, antibody drug conjugate or pharmaceutical composition of the invention. Too long a period between administration of antibody, antibody drug conjugate or pharmaceutical composition of the invention and administration of the new stem cell population would undesirably expose the subject to prolonged duration of neutropenia. In some aspects, the stem cell population may be administered to the subject, e.g., to the target tissue of the subject, from 6 to 72 hours, from 1 to 5 days, from 1 to 7 days, or from 1 to 10 days; preferably from about 1 to about 7 days, after the administration of the antibody, antibody drug conjugate or pharmaceutical composition of the invention. In some aspects, the methods or medical uses of the invention result in conditioning of a subject’s target tissues and engraftment of stem cells and achieve at least about 5-100% donor chimerism, preferably at least about 50-100%, most preferably at least about 80-100% donor chimerism (i.e., percentage of the cells derived from the donor) in the subject’s target tissue (e.g., bone marrow) four months post-administration of the stem cell population to the subject. Preferably, the donor chimerism is complete, i.e., at least 95% donor chimerism. In some aspects, the donor chimerism is stable high-level mixed chimerism, i.e., at least 50% donor chimerism, which is typically sufficient for cure. Most preferably, the donor chimerism is in both myeloid and lymphoid lineages. The level of engraftment needed may depend on the clinical scenario. For haematological malignancies at least about 50-100%, preferably at least about 80-100%, and most preferably complete donor chimerism, is the aim. For non-malignant disorders, whilst complete donor chimerism is still preferable, mixed chimerism (e.g., 30-70%, preferably 50-70% donor chimerism) is often curative. The level of donor chimerism needed to be curative may depend on the disease. For example, for haemoglobinopathies stable, 30% donor chimerism in myeloid lineage may be curative; for primary immunodeficiencies even 10-20% donor chimerism may be sufficient. In some aspects, the methods or medical uses of the invention that comprise transplantation of genetically-modified autologous haematopoietic stem cells to the subject, for example for gene therapy, may result in a viral copy number of 0.1-10 copies/cell, preferably 0.5-4 copies/cell and most preferably 1-2 copies/cell, in the relevant cell lineage (e.g., myeloid and/or lymphoid) in the blood. In some aspects, the methods of the invention result in conditioning of a subject’s target tissues and engraftment of stem cells and achieve an engraftment rate of at least 50%, preferably at least 60%, most preferably at least 80%, of subjects treated according to the methods of the invention. The methods and compositions described herein may provide an enhanced or improved engraftment efficiency, i.e., the efficiency with which an administered stem cell population (e.g., HSCs) engrafts in the conditioned target tissue of the subject (e.g., bone marrow). The subject may be a mammal, most preferably a human. The subject may have, may have been diagnosed with, or may be suspected of having, a disease or disorder that can be treated by haematopoietic stem cell transplant. In some aspects, the subject may have, may have been diagnosed with, or may be suspected of having, a disease or disorder that can be treated by gene therapy, optionally with haematopoietic stem cell transplant. In some aspects, the subject has, has been diagnosed with, or is suspected of having, cancer, preferably a haematological cancer. In some aspects, the subject has, has been diagnosed with, or is suspected of having, acute myeloid leukaemia, acute lymphoblastic leukaemia, chronic lymphocytic leukaemia, chronic myeloid leukaemia, myelodysplasia, multiple myeloma, non-Hodgkin’s lymphoma and Hodgkin’s disease. In some aspects, the subject has, has been diagnosed with, or is suspected of having, a non- malignant disease, disorder or condition. In some aspects, the subject has, has been diagnosed with, or is suspected of having a disorder or disease selected from the group consisting of: severe aplastic anaemia or other bone marrow failure disorder (such as Fanconi anaemia, dyskeratosis congenita, Shwachman-Diamond Syndrome, severe congenital neutropenia, Diamond-Blackfan anaemia), a primary immunodeficiency (such as SCID (e.g., newborn SCID), chronic granulomatous disease, Wiskott-Aldrich syndrome, CD40 ligand deficiency, XLP, MHC Class II deficiency, primary haemophagocytic lymphohistiocytosis), a haemoglobinopathy, preferably a transfusion dependent haemoglobinopathy (such as sickle cell disease, β- thalassaemia major), a genetic metabolic disease (such as Hurler’s syndrome, X-linked adrenoleukodystrophy, alpha mannosidosis, osteopetrosis, metachromatic leukodystrophy, Sanfilippo disease), or an autoimmune disorder (such as multiple sclerosis, systemic sclerosis, juvenile inflammatory arthritis, systemic lupus erythematosus). In the methods or medical uses of the invention, in some aspects, the subject is chemorefractory (i.e., cannot be treated with chemotherapy, the subject has a cancer that is not responsive to chemotherapy, such as traditional chemotherapies). In some aspects, the subject is contraindicated for chemotherapy and/or radiotherapy. In some aspects, the subject has an immunodeficiency, optionally a congenital immunodeficiency or an acquired immunodeficiency. In some aspects, the subject has pre-existing organ toxicity (i.e. is too ill for conventional conditioning regimes), or has a DNA or telomere repair disorder precluding conventional chemo/radiotherapy conditioning.. In some aspects, the subject is a human adult. In some aspects, the subject is over 12 years of age, preferably over 15 years of age, or most preferably over 20 years of age. In some aspects, the subject is immunocompetent, i.e., not immunodeficient. The methods described herein of preparing a subject for transplantation of haematopoietic stem cells, and the methods of engrafting stem cells in a subject, may be useful in the treatment of malignant diseases or disorders. In some aspects the malignant disease or disorder is caused by CD45-expressing cells. In some aspects, the malignant disease or disorder is cancer. In preferred aspects, the malignant disease or disorder is a haematological cancer. In some aspects, the malignant disease or disorder is selected from the group consisting of acute myeloid leukaemia, acute lymphoblastic leukaemia, chronic lymphocytic leukaemia, chronic myeloid leukaemia, myelodysplasia, myeloproliferative disease, multiple myeloma, non-Hodgkin’s lymphoma and Hodgkin’s disease. The methods described herein of preparing a subject for transplantation of haematopoietic stem cells, and the methods of engrafting stem cells in a subject, may be useful in the treatment of non- malignant diseases, disorders or conditions. In some aspects the non-malignant disease, disorder or condition is caused by CD45-expressing cells. In some aspects, the non-malignant disease, disorder or condition may be selected from the group consisting of: severe aplastic anaemia or other bone marrow failure disorder (such as Fanconi anaemia, dyskeratosis congenita, Shwachman- Diamond Syndrome, severe congenital neutropenia, Diamond-Blackfan anaemia), a primary immunodeficiency (such as SCID, newborn SCID, chronic granulomatous disease, Wiskott-Aldrich syndrome, CD40 ligand deficiency, XLP, MHC Class II deficiency, primary haemophagocytic lymphohistiocytosis), a transfusion dependent haemoglobinopathy (such as sickle cell disease, β- thalassaemia major), a genetic metabolic disease (such as Hurler’s syndrome, X-linked adrenoleukodystrophy, alpha mannosidosis, osteopetrosis, metachromatic leukodystrophy, Sanfilippo disease) or an autoimmune disorder (such as multiple sclerosis, systemic sclerosis, juvenile inflammatory arthritis, systemic lupus erythematosus). In some preferred aspects, the methods described herein of preparing a subject for transplantation of haematopoietic stem cells, and the methods of engrafting stem cells in a subject, may be useful in the treatment of a Fanconi anaemia, chronic granulomatous disease and/or Hurler’s syndrome. In some most preferred aspects, the methods described herein of preparing a subject for transplantation of haematopoietic stem cells, and the methods of engrafting stem cells in a subject, may be useful in the treatment of sickle cell anaemia, β-thalassemia, and/or newborn SCID. In the methods of treatment and medical uses described herein the antibodies, antibody drug conjugates or pharmaceutical compositions of the invention are preferably administered by parenteral administration. Preferred routes of administration for the antibodies, conjugates or compositions in the methods and medial uses of the invention include intravenous, intramuscular, intradermal, intraperitoneal, subcutaneous, spinal or other parenteral routes of administration, for example by injection or infusion. The appropriate dosage of an antibody or antibody drug conjugate of the invention in the methods of treatment and medical uses described herein will depend for example on the disease to be treated, the subject group and individual subject requirements, but a skilled person would be readily capable of determining a suitable dosage regime. The antibody or antibody drug conjugate may be administered to the subject in a single dose in one continuous administration, or as multiple doses over a series of separate administrations. The antibody or antibody drug conjugate may be administered to the subject once in a single day. A suitable initial dose may be about 1 µg/kg to 15 mg/kg. A suitable daily dosage may range from about 1 µg/kg to 100 mg/kg of subject weight. An exemplary dosage of antibody or antibody drug conjugate to be administered to a subject may be in the range of about 0.1 mg/kg to about 10 mg/kg of subject weight. In some aspects where multiple doses are administered, these may be administered as separate administrations over a period of 1 week, 2 weeks, 3 weeks, 4 weeks, 2 months, 4 months, 8 months, 12 months, 18 months, 2 years, 3 year, 5 years or more; preferably where the antibodies or antibody drug conjugates are administered in multiple doses, they are administered over a period of 2-4 weeks. An exemplary dosing regimen comprises a course of administering an initial loading dose of about 4 mg/kg, followed by additional doses every week, two weeks, or three weeks of an antibody or antibody drug conjugate of the invention. Other dosage regimens may be useful. Combination therapies The antibodies (including the biparatopic and bispecific antibodies described herein) and antibody drug conjugates of the invention may be used in combination in the methods and medical uses of the invention, i.e., the methods of preparing a subject for transplantation of haematopoietic stem cells, and the methods of engrafting stem cells in a subject, which are described herein. The above disclosure of the further features of the methods or medical uses of the invention applies equally to the methods or medical uses of the invention that use a combination of antibodies or antibody drug conjugates, as described below. The present invention also provides a method of preparing a subject for transplantation of haematopoietic stem cells, the method comprising administering a first antibody of the invention, and a second, different antibody of the invention, to a subject in need thereof. The present invention also provides a method of preparing a subject for transplantation of haematopoietic stem cells, the method comprising administering a first antibody of the invention to a subject in need thereof, wherein the subject has been, is being, or will be administered a second, different antibody of the invention. The present invention further provides a first antibody of the invention and a second, different antibody of the invention, for use in a method of preparing a subject for transplantation of haematopoietic stem cells, wherein the method comprises administering the first antibody and the second antibody to a subject in need thereof. The present invention also provides a first antibody of the invention, for use in a method of preparing a subject for transplantation of haematopoietic stem cells, wherein the method comprises administering the first antibody, and a second, different antibody of the invention, to a subject in need thereof. In some aspects, the first antibody may be an antibody of the first antibody group, as described herein, and the second antibody may be an antibody of the second antibody group, as described herein. In some aspects, the first antibody may be an antibody of the second antibody group, as described herein, and the second antibody may be an antibody of the first antibody group, as described herein. In some aspects the first antibody and the second antibody are administered to the subject within the same pharmaceutical composition. In some other preferred aspects, the first antibody and the second antibody are administered to the subject as two separate pharmaceutical compositions. In some aspects the first antibody and the second antibody are administered to the subject concurrently. In some aspects the first antibody is administered to the subject before the second antibody is administered to the subject. In some aspects the first antibody is administered to the subject immediately before the second antibody is administered to the subject. In some aspects the first antibody is administered to the subject at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 24, 36, 48, or 72 hours before, preferably at least 1 hour before, the second antibody is administered to the subject. In some aspects the first antibody is administered to the subject at least 1, 2, 3, 4, 5, 7, 10, 14, 21, 28, 35, 42, or 49 days before, preferably at least 1 day, before the second antibody is administered to the subject. In some preferred aspects the first antibody and the second antibody are administered to the subject sequentially on the same day. The present invention also provides a method of preparing a subject for transplantation of haematopoietic stem cells, the method comprising administering a first antibody drug conjugate of the invention, and a second, different antibody drug conjugate of the invention, to a subject in need thereof. The present invention also provides a method of preparing a subject for transplantation of haematopoietic stem cells, the method comprising administering a first antibody drug conjugate of the invention to a subject in need thereof, wherein the subject has been, is being, or will be administered a second, different antibody drug conjugate of the invention. The present invention further provides a first antibody drug conjugate of the invention and a second, different antibody drug conjugate of the invention, for use in a method of preparing a subject for transplantation of haematopoietic stem cells, wherein the method comprises administering the first antibody drug conjugate and the second antibody drug conjugate, to a subject in need thereof. The present invention also provides a first antibody drug conjugate of the invention, for use in a method of preparing a subject for transplantation of haematopoietic stem cells, wherein the method comprises administering the first antibody drug conjugate and a second, different antibody drug conjugate of the invention, to a subject in need thereof. In some aspects the antibody (Ab) of the first antibody drug conjugate is an antibody of the first antibody group described herein, and the antibody (Ab) of the second antibody drug conjugate is an antibody of the second antibody group described herein. In such aspects, the drug (D or (L-D)) of the first antibody drug conjugate may be different from, or the same as, the drug (D or (L-D)) of the second antibody drug conjugate. In some aspects the antibody (Ab) of the first antibody drug conjugate is an antibody of the second antibody group described herein, and the antibody (Ab) of the second antibody drug conjugate is an antibody of the first antibody group described herein. In such aspects, the drug (D or (L-D)) of the first antibody drug conjugate may be different from, or the same as, the drug (D or (L-D)) of the second antibody drug conjugate. In some aspects the antibody (Ab) of both the first antibody drug conjugate and the second antibody drug conjugate is an antibody of the first antibody group described herein, and the drug (D or (L-D)) of the first antibody drug conjugate is different from the drug (D or (L-D)) of the second antibody drug conjugate. In some aspects the antibody (Ab) of both the first antibody drug conjugate and the second antibody drug conjugate is an antibody of the second antibody group described herein, and the drug (D or (L-D)) of the first antibody drug conjugate is different from the drug (D or (L-D)) of the second antibody drug conjugate. In some aspects the first antibody drug conjugate and the second antibody drug conjugate are administered to the subject within the same pharmaceutical composition. In some other preferred aspects, the first antibody drug conjugate and the second antibody drug conjugate are administered to the subject as two separate pharmaceutical compositions. In some aspects the first antibody drug conjugate and the second antibody drug conjugate are administered to the subject concurrently. In some aspects the first antibody drug conjugate is administered to the subject before the second antibody drug conjugate is administered to the subject. In some aspects the first antibody drug conjugate is administered to the subject immediately before the second antibody drug conjugate is administered to the subject. In some aspects the first antibody drug conjugate is administered to the subject at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 24, 36, 48, or 72 hours before, preferably at least 1 hour before, the second antibody drug conjugate is administered to the subject. In some aspects the first antibody drug conjugate is administered to the subject at least 1, 2, 3, 4, 5, 7, 10, 14, 21, 28, 35, 42, or 49 days before, preferably at least 1 day, before the second antibody drug conjugate is administered to the subject. In some aspects the first antibody drug conjugate and the second antibody drug conjugate are administered to the subject sequentially on the same day. Although co-administration of antibody drug conjugates of the invention is described herein, in some aspects administration of only a single antibody drug conjugate of the invention is advantageously sufficient to have the desired effect, e.g., effective conditioning or a therapeutic effect. The present invention also provides a method of engrafting stem cells in a subject, the method comprising (a) administering an effective amount of a first antibody of the invention, and a second, different antibody of the invention, to the subject; and (b) administering a stem cell population to the subject, preferably a target tissue of the subject, wherein the administered stem cell population engrafts in the target tissue of the subject. The present invention also provides a method of engrafting stem cells in a subject, the method comprising (a) administering an effective amount of a first antibody of the invention to the subject, wherein the subject has been, is being, or will be administered an effective amount of a second, different antibody of the invention; and (b) administering a stem cell population to the subject, preferably a target tissue of the subject, wherein the administered stem cell population engrafts in the target tissue of the subject. The present invention also provides a method of engrafting stem cells in a subject, the method comprising (a) administering an effective amount of a first antibody of the invention to the subject, wherein (i) the subject has been, is being, or will be administered an effective amount of a second, different antibody of the invention; and (ii) the subject will be administered a stem cell population, preferably to a target tissue of the subject, wherein the administered stem cell population engrafts in the target tissue of the subject. The present invention further provides a first antibody of the invention and a second, different antibody of the invention, for use in a method of engrafting stem cells in a subject, wherein the method comprises (a) administering an effective amount of the first antibody and the second antibody to the subject; and (b) administering a stem cell population to the subject, preferably a target tissue of the subject, wherein the administered stem cell population engrafts in the target tissue of the subject. The present invention also provides a first antibody of the invention, for use in a method of engrafting stem cells in a subject, wherein the method comprises (a) administering an effective amount of the first antibody, and an effective amount of a second, different antibody of the invention, to the subject ; and (b) administering a stem cell population to the subject, preferably a target tissue of the subject, wherein the administered stem cell population engrafts in the target tissue of the subject. In some aspects, the first antibody may be an antibody of the first antibody group, as described herein, and the second antibody may be an antibody of the second antibody group, as described herein. In some aspects, the first antibody may be an antibody of the second antibody group, as described herein, and the second antibody may be an antibody of the first antibody group, as described herein. In some aspects the first antibody and the second antibody are administered to the subject within the same pharmaceutical composition. In some other preferred aspects, the first antibody and the second antibody are administered to the subject as two separate pharmaceutical compositions. In some aspects the first antibody and the second antibody are administered to the subject concurrently. In some aspects the first antibody is administered to the subject before the second antibody is administered to the subject. In some aspects the first antibody is administered to the subject immediately before the second antibody is administered to the subject. In some aspects the first antibody is administered to the subject at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 24, 36, 48, or 72 hours before, preferably at least 1 hour before, the second antibody is administered to the subject. In some aspects the first antibody is administered to the subject at least 1, 2, 3, 4, 5, 7, 10, 14, 21, 28, 35, 42, or 49 days before, preferably at least 1 day, before the second antibody is administered to the subject. In some aspects the first antibody and the second antibody are administered to the subject sequentially on the same day. In some aspects, the stem cell population is administered to the subject at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 18, 21 or more days, preferably at least 1 day, most preferably at least 2 days, after the administration of the first antibody and/or the second antibody. In some aspects, the stem cell population is administered to the subject from 6 to 72 hours, from 1 to 5 days, from 1 to 7 days, or from 1 to 10 days; preferably from 1 to 7 days, after the administration of the first antibody and/or the second antibody. The present invention also provides a method of engrafting stem cells in a subject, the method comprising (a) administering an effective amount of a first antibody drug conjugate of the invention, and a second, different antibody drug conjugate of the invention, to the subject; and (b) administering a stem cell population to the subject, preferably a target tissue of the subject, wherein the administered stem cell population engrafts in the target tissue of the subject. The present invention also provides a method of engrafting stem cells in a subject, the method comprising (a) administering an effective amount of a first antibody drug conjugate of the invention to the subject, wherein the subject has been, is being, or will be administered an effective amount of a second, different antibody drug conjugate of the invention; and (b) administering a stem cell population to the subject, preferably a target tissue of the subject, wherein the administered stem cell population engrafts in the target tissue of the subject. The present invention also provides a method of engrafting stem cells in a subject, the method comprising (a) administering an effective amount of a first antibody drug conjugate of the invention to the subject, wherein (i) the subject has been, is being, or will be administered an effective amount of a second, different antibody drug conjugate of the invention; and (ii) the subject will be administered a stem cell population, preferably to a target tissue of the subject, wherein the administered stem cell population engrafts in the target tissue of the subject. The present invention further provides a first antibody drug conjugate of the invention and a second, different antibody drug conjugate of the invention, for use in a method of engrafting stem cells in a subject, wherein the method comprises (a) administering an effective amount of the first antibody drug conjugate and the second antibody drug conjugate to the subject; and (b) administering a stem cell population to the subject, preferably a target tissue of the subject, wherein the administered stem cell population engrafts in the target tissue of the subject. The present invention also provides a first antibody drug conjugate of the invention, for use in a method of engrafting stem cells in a subject, wherein the method comprises (a) administering an effective amount of the first antibody drug conjugate, and an effective amount of a second, different antibody drug conjugate of the invention, to the subject; and (b) administering a stem cell population to the subject, preferably a target tissue of the subject, wherein the administered stem cell population engrafts in the target tissue of the subject. In some aspects the antibody (Ab) of the first antibody drug conjugate is an antibody of the first antibody group described herein, and the antibody (Ab) of the second antibody drug conjugate is an antibody of the second antibody group described herein. In such aspects, the drug (D or (L-D)) of the first antibody drug conjugate may be different from, or the same as, the drug (D or (L-D)) of the second antibody drug conjugate. In some aspects the antibody (Ab) of the first antibody drug conjugate is an antibody of the second antibody group described herein, and the antibody (Ab) of the second antibody drug conjugate is an antibody of the first antibody group described herein. In such aspects, the drug (D or (L-D)) of the first antibody drug conjugate may be different from, or the same as, the drug (D or (L-D)) of the second antibody drug conjugate. In some aspects the antibody (Ab) of both the first antibody drug conjugate and the second antibody drug conjugate is an antibody of the first antibody group described herein, and the drug (D or (L-D)) of the first antibody drug conjugate is different from the drug (D or (L-D)) of the second antibody drug conjugate. In some aspects the antibody (Ab) of both the first antibody drug conjugate and the second antibody drug conjugate is an antibody of the second antibody group described herein, and the drug (D or (L-D)) of the first antibody drug conjugate is different from the drug (D or (L-D)) of the second antibody drug conjugate. In some aspects the first antibody drug conjugate and the second antibody drug conjugate are administered to the subject within the same pharmaceutical composition. In some other preferred aspects, the first antibody drug conjugate and the second antibody drug conjugate are administered to the subject as two separate pharmaceutical compositions. In some aspects the first antibody drug conjugate and the second antibody drug conjugate are administered to the subject concurrently. In some aspects the first antibody drug conjugate is administered to the subject before the second antibody drug conjugate is administered to the subject. In some aspects the first antibody drug conjugate is administered to the subject immediately before the second antibody drug conjugate is administered to the subject. In some aspects the first antibody drug conjugate is administered to the subject at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 24, 36, 48, or 72 hours before, preferably at least 2 hours before, most preferably at least 12 hours before, the second antibody drug conjugate is administered to the subject. In some aspects the first antibody drug conjugate is administered to the subject at least 1, 2, 3, 4, 5, 7, 10, 14, 21, 28, 35, 42, or 49 days before, preferably at least 1 day, most preferably at least 7 days, before the second antibody drug conjugate is administered to the subject. In some aspects, the stem cell population is administered to the subject at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 18, 21 or more days, preferably at least 1 day, most preferably at least 2 days, after the administration of the first antibody drug conjugate and/or the second antibody drug conjugate. In some aspects, the stem cell population is administered to the subject from 6 to 72 hours, from 1 to 5 days, from 1 to 7 days, or from 1 to 10 days; preferably from about 1 to 7 days, after the administration of the first antibody drug conjugate and/or the second antibody drug conjugate. The methods and medical uses of the invention, i.e., those methods of treatment using a single antibody, antibody drug conjugate or pharmaceutical composition of the invention, or those methods using a combination of two species of the antibodies or antibody drug conjugates of the invention, may further comprise administering one or more other therapeutic agents. For example, the methods may further comprise administering to the subject one or more agents for myelosuppression, and/or agents for immunosuppression. In some aspects, the methods may further comprise administering to the subject one or more of Alemtuzumab, ATG, fludarabine, and/or cyclophosphamide. In some aspects, the methods may further comprise administering to the subject one or more of busulphan, treosulphan, thiotepa, total body irradiation. Alternatively, in some aspects the methods of the invention do not comprise administering further agents for myelosuppression, and/or agents for immunosuppression. In some aspects, the methods may further comprise administration of a therapeutically effective amount of one or more chemotherapeutic agents. For example, in some aspects, the methods may further comprise administering to the subject one or more of daunorubicin, idarubicin, mitoxantrone, cytarabine, etoposide, fludarabine, gemtuzumab, 5-azacytidine, hydroxyurea, midostaurin, vincristine, steroids, doxorubicin, asparaginase, cyclophosphamide, ifosfamide, methotrexate, nelarabine, daratumumab, melphalan, thalidomide, lenolidamide, bortezimib, pomalidomide, carfolizimib, bendamustine, carmustine (bis-chloroethylnitrosourea, BCNU), cis platin, carboplatin, rituximab, ofatumumab, obinutuzumab, ibrutinib, idelasalib or brentuximab. In such aspects, the further agents may be administered concurrently with the antibodies, antibody drug conjugates or pharmaceutical compositions, as described herein. In some aspects, the one or more antibodies, the one or more antibody drug conjugates or the pharmaceutical compositions of the invention may be administered before, after or concurrently with the one or more further agents. The one or more antibodies, the one or more antibody drug conjugates or the pharmaceutical compositions of the invention may be administered in combination with or sequentially to, for example, cytotoxic agents, anti-cancer agents, tumour targeting antibodies, target therapy, pathway inhibitors, immunosuppressive agent or myelosuppressive agents. In some aspects, the methods of the invention may further comprise administering to the subject local radiation and/or chemotherapy. In some aspects, the methods do not comprise administering to the subject Alemtuzumab (an anti- CD52 antibody) or ATG (anti-thymocyte globulin). In some aspects, the methods do not comprise administering to the subject fludarabine. In some aspects, the methods do not comprise administering to the subject a low dose cyclophosphamide for immunosuppression. In some aspects, the methods do not comprise administering to the subject Alemtuzumab, ATG, fludarabine and a low dose cyclophosphamide for immunosuppression. In some aspects where the antibodies, antibody drug conjugates or pharmaceutical compositions are used in a method of engrafting stem cells in a subject, or for preparing a subject for gene therapy, or for transplantation with a preparation containing haematopoietic stem cells, the one or more antibodies or antibody drug conjugates may be administered in combination with radiotherapy, chemotherapy (such as busulphan, treosulphan, melphalan and others), immunosuppressive agents (such as fludarabine, cyclophosphamide, Alemtuzumab, ATG or others), anti-microbial agents (e.g., anti-viral, anti- fungal or anti-bacterial agents), GvHD prophylaxis (such as methotrexate, cyclosporine, tacrolimus and/or others) or GvHD treatment (such as glucocorticoids, ECP, Ruxolitinib, ibrutinib, Infliximab, sirolimus or others). In some aspects of the methods of treatment or medical uses described herein, such further agents are administered (i) before, (ii) concurrently with, and/or (iii) after, the one or more antibodies or antibody drug conjugates, preferably concurrently with and/or after, most preferably after. EXAMPLES Example 1 – anti-CD45 antibodies Previously, c-Kit had been considered as a potential target on haematopoietic stem cells (HSCs) for targeted conditioning agents. However, the present inventors have confirmed the superiority of CD45 as a HSC-specific target compared to c-Kit. Evidence for this is provided by a number of key experiments. Substantially greater CD45 expression was observed on key cell types, as compared to c-Kit expression. c-Kit was previously a candidate target for a non-toxic conditioning product because of its specificity for HSCs. However, HSC surface expression levels of CD45 were shown to be substantially higher than those for c-Kit (see Figure 1). Much higher levels of CD45 protein than c-Kit receptors were observed across a range of peripheral and umbilical cord stem cell types, which might explain the superiority of the anti-CD45 combination to approaches targeting c-Kit. Two rat IgG2b monoclonal antibodies that bind human CD45 were selected for testing (having heavy and light chain variable regions of SEQ ID NOs 1 and 2 (Ab1) or having heavy and light chain variable regions of SEQ ID NOs 11 and 12 (Ab2)). Using non-human antibodies meant that the antibodies clear much more quickly from the human body, which is advantageous for conditioning regimens that will be followed haematopoietic stem cell transplant, to avoid the newly transplanted cells being affected by the conditioning agents. The two antibodies Ab1 and Ab2 were selected for testing because they had been shown to function synergistically, with each antibody binding to a different part of the CD45 protein, and inducing CDC. The antibodies had also been shown to be rapidly cleared in humans. These two anti-CD45 monoclonal antibodies (rat IgG2b Ab1 and Ab2) were found to completely prevent colony formation via complement-dependent cytotoxicity (CDC). Evidence for targeting CD45 as a method of specifically killing HSCs via CDC was shown using a clonogenic in vitro assay (see Figure 2). The combination of rat IgG2b Ab1 and Ab2 as applied to HSCs, in the presence of complement protein in serum completely abrogated cell colony formation. Additionally, incubating human CD34+ cells with the combination of rat IgG2b Ab1 and Ab2 in the presence of complement was further shown to completely abrogate engraftment of the cells following transplantation into NSG (NOD scid gamma) immunodeficient mice (see Figure 3). This shows that, at least in vitro, CDC via CD45 targeting can be a powerful method for specifically killing HSCs. In contrast, ex vivo treatment of human CD34+ cells with anti-c-kit antibodies in the presence of complement only partially inhibited colony formation and did not prevent engraftment in NSG mice. Furthermore, it has been confirmed using live-imaging microscopy that rat IgG2b Ab1 and Ab2 are substantially internalised and processed via a lysosomal pathway (see Figure 4). The fact that the antibodies are readily internalised by the target cells supports the hypothesis that these antibodies are suited to an ADC-based approach. In particular, the lysosomal pathway can be important in providing an environment for cleavage of the antibody-drug linkers, hereby releasing the drug in the target cells for highly specific cell killing. The applicability of anti-CD45 antibodies in conditioning methods in patients has been further confirmed by the present inventors in a clinical trial (Straathof et al., Lancet (2009) 374(9693), pp. 912-920). Additionally, a recent patent application from Magenta Therapeutics, Inc. (WO 2020/146432) has highlighted that anti-human CD45 antibody drug conjugates are useful in human patients undergoing chimeric antigen receptor (CAR) immunotherapy in order to promote acceptance of CAR expressing immune cells. Enhanced cytotoxicity of anti-CD45 antibodies (rat IgG2b Ab1 and Ab2) in the presence of an immunotoxin has also been demonstrated by the present inventors, using the ribosome inactivating protein (RIP), saporin, indirectly attached to the anti- CD45 antibodies (Figure 8), which indicates that anti-CD45 immunotoxins may also be useful. Ab1, Ab2 and rat IgG2b isotype control (clone RTK4530, Biolegend) were conjugated to saporin, a ribosome-inactivating protein, using goat anti-rat IgG-saporin conjugate (Rat-ZAP, ATSBio) following manufacturer’s recommendations. Human CD45+ Jurkat cells were incubated, in triplicate, in 96-well plates with serially diluted antibody alone, immunotoxin or media alone (RPMI 1640 plus 10% FBS) for 72 hours. Cell viability was determined using PrestoBlue™ Cell Viability reagent (Invitrogen). Fluorescence intensity from each well was detected using a FLUOstar OPTIMA microplate reader (BMG Labtech) using excitation filter of 560-10 and 590-10 emission filter and gain at 1500. Cell viability assays showed that the anti-CD45-saporin immunotoxins were able to specifically kill CD45+ Jurkat cells with IC ₅₀ values between 55-164 nM (Figure 8, Table 1). There was little cell killing with the naked antibodies under these conditions, or with the Isotype-saporin control. Thus, anti-CD45 immunotoxins, using a protein toxin, can be generated which have specificity against CD45+ cell lines. Table 1. Comparison of the IC ₅₀ values (pM) for anti-CD45-saporin immunotoxins on Jurkat cells. The lower observed expression levels of the alternative target c-Kit, and the suboptimal clinical efficacy of prior art anti-CD45 antibody combinations, prompted consideration of further anti- CD45 antibody-based strategies for selective killing of HSCs. Example 2 – Materials and methods Generation of ADCs Ab1 and Ab2 (YTH24.5 and YTH54.12) and isotype control (MOPC21), were expressed as recombinant rat IgG2b, k (Evitria AG) with the following sequence at the C-terminus of the light chain (GGGGSLPETGGWSHPQFEK (SEQ ID NO: 39)), to enable sortase conjugation to the Gly3-PEG-N3 linker (ADC Biotechnology Ltd). Bulk azide reactive intermediate was generated, followed by a copper-free click reaction of a range of DBCO functionalised payloads with different mechanisms-of-action, which included MMAE, Maytansine derivative, Dxd, Duocarmycin and PNU with a target ‘drug:antibody ratio’ (DAR) of 2.0. For reference, the full names of the toxin linkers used are: DBCO Caproyl Valine Citrulline PAB DMEA (PEG2) Duocarmycin SA; DBCO PEG4 Valine Citrulline PAB DMEA PNU159682 (anthracycline / nemorubicin metabolite); DBCO PEG4 Ahx Maytansine; DBCO PEG4 Valine Citrulline PAB MMAE (auristatin derivative); and DBCO PEG4 GGFG DX8951 (Exatecan derivative). Cell viability assays with ADCs Human CD45+ OCIM1 and Jurkat cell lines and the human CD45- Nalm6 cell line were cultured in RPMI 1640 plus 10% foetal bovine serum (FBS) for 5 days in presence of different concentrations of Isotype-ADC, or anti-CD45 ADC, or media alone. Cell viability was determined using PrestoBlue™ Cell Viability reagent. Data was plotted using Prism 8.0 and sigmoid dose- response non-linear regression. EC ₅₀ values were determined as the concentration at which gave 50% cell viability. Data was expressed relative to the untreated cells ± s.d. Clonogenic assays Cryopreserved CD34+ cells from mobilised peripheral blood of a healthy donor were thawed, washed, and resuspended at a final cell density of 0.5×10 ⁵ /mL in RPMI 1640 medium plus 10% FBS in presence of Isotype ADC, or anti-CD45 ADC, or media alone or for 2 hours. Cells were mixed and 1000 cells were transferred to 2 ml of StemMACS HSC-CFU complete with Epo (Miltenyi Biotech) and mixed well. 0.5 ml was plated, in triplicate, into wells of a 24-well plate. Colonies were enumerated after 12 to 14 days. Data was plotted using Prism 8.0 and sigmoid dose- response non-linear regression. IC ₅₀ values were determined as the concentration at which gave 50% cell viability. Data was expressed relative to the untreated cells ± s.d. AML studies NSG mice were transplanted with 7.5x10 ⁶ luciferase expressing (fLuc+) OCIM1 cells. On the following day PBS or unconjugated antibody or ADCs were injected i.v. via a tail vein at a dose of 1 mg/kg. Mice were regularly monitored for signs of morbidity for the duration of the experiment. For imaging, mice were injected intraperitoneally with 200 µl of 15 mg/mL D-luciferin (Regis Technologies) in PBS. Mice were subsequently anesthetised with 4% isoflurane and maintained at 2% isoflurane. Ten minutes after injection of D-luciferin, mice were placed with anterior side up inside a IVIS Lumina III (PerkinElmer). A sub-saturating image was captured using the auto- exposure setting in the Living Image software (v4.5). Quantification and preparation of images was also carried out using the same software. Generation and testing of anti-CD45 biparatopic antibody. Biparatopic antibodies were generated by controlled Fab-arm exchange of the Ab1 and Ab2 rat IgG2b antibodies (Labrijn, et al., 2017) after introduction of specific point mutations in the heavy chains to facilitate pairing of the antibodies. The F405L mutation was introduced into the heavy chain of Ab2 rat IgG2b along with a HA tag sequence at the C-terminus to generate the Ab2- F405L.HA antibody. S370K and K409R mutations were introduced into the heavy chain of the Ab1 rat IgG2b antibody in addition to a C-terminal His tag sequence to generate Ab1-S370K- K409R.His. Antibody expression was carried out by Evitria AG and antibody purification from supernatant was carried out in-house using HiTrap® Protein L columns (Cytiva) and dialysed into PBS. Controlled Fab-arm exchange was carried out as described in Labrijn, et al., 2017, followed by dialysis in PBS. Flow cytometry experiments were carried out to determine whether biparatopic antibodies were generated. HEK293T cells were transiently transfected with plasmid DNA to enable co-expression of GFP and either the V5 epitope-tagged full length CD45 extracellular domain (V5-CD45 FL) (SEQ ID NO: 40), or the V5 epitope-tagged CD45Δ2 truncation mutant (V5-CD45Δ2) which lacked the distal fibronectin type 3 repeat, cysteine-rich region and variable N-terminal region (SEQ ID NO: 41). Both constructs expressed the transmembrane region and a signal peptide. Transfected HEK293T cells were stained with Ab1-S370K-K409R.His or Ab2-F405L.HA, or the biparatopic antibody, Ab1-S370K-K409R.His x Ab2-F405L.HA. Cells were subsequently stained with anti-V5-PE, anti-His-APC, anti-HA-PE-Cy7 and 7-AAD as a viability dye. Cells were analysed on a Beckman CytoFLEX analyser, followed by post-acquisition analysis using FlowJo 10 software. Example 3 - Assessment of ADC efficacy on leukaemic cell lines in vitro Results Cell viability assays showed that anti-CD45-PNU ADCs were the most potent ADCs, killing CD45+ OCIM1 and Jurkat cells with low/sub picomolar IC ₅₀ values (OCIM1 IC ₅₀ = 0.007 to 0.822 pM and Jurkat IC ₅₀ = 0.04 to 0.5pM) (Figure 9 and Table 2). There was a 3-4 log difference between the anti-CD45-PNUs compared to the control MOPC21-PNU (Table 2). Non-specific killing was observed with anti-CD45 ADCs on CD45- Nalm6 cells at the highest concentrations only, similar to the Isotype-ADCs. With the anti-CD45-Maytansine derivative ADCs, there was specific killing of Jurkat cells (IC ₅₀ = 4.9 to 9.5 pM), but not specific killing of OCIM1 cells (Figure 10, Table 2). As expected, Nalm6 cells were insensitive to both the anti-CD45-Maytansine derivative ADCs and Isotype-Maytansine derivative and non-specific cell killing was observed only at the highest concentrations. There was 7-9 fold difference in the IC ₅₀ values between Ab1-Dxd and MOPC21-Dxd on OCIM1 and Jurkat cells (Figure 11, Table 2). However, the IC ₅₀ values for Ab2-Dxd on OCIM1 and Jurkat cells were similar to those obtained with MOPC21-Dxd, indicating that Ab2-Dxd did not induce specific cell killing. The anti-CD45-Duocarmycin ADCs also showed specific killing of OCIM1 and Jurkat cells (OCIM1 IC ₅₀ = 8.0 to 292 pM and Jurkat IC ₅₀ = 414 to 4,808 pM), compared to MOPC21- Duocarmycin (IC ₅₀ = 12,257 to 20,591 pM) (Figure 12, Table 2). The Ab1-Duocarmycin ADCs appeared to have better activity compared to Ab2-Duocarmycin. No specific killing was observed with the Nalm6 cell line. Anti-CD45-MMAE ADCs were able to specifically kill Jurkat cells with IC ₅₀ values between 150-857 pM, but had only weak killing of OCIM1 cells (Figure 13, Table 2). No specific killing was observed with the Nalm6 cell line.

Table 2. Comparison of the IC ₅₀ values (pM) for different ADCs in vitro on cell lines. In a preliminary clonogenic assay, each ADC was used at 10µg/mL. PNU and Duocarmycin ADCs showed most effective inhibition of colonies (data not shown), therefore these ADCs were selected for further clonogenic assays to determine the IC ₅₀ values (Figure 14, Table 3). The anti-CD45 PNUs was the most potent, showing CD45-specific colony inhibition with IC ₅₀ values of ~2-4 nM compared to the MOPC21-PNU IC ₅₀ value of 24 nM. Similar results were also obtained for the anti-CD45-Duocarmycin ADCs. Table 3. Comparison of the IC ₅₀ values (pM) for different ADCs in vitro in clonogenic assays. Conclusions Anti-CD45 ADCs, using a range of payloads with different mechanisms-of-action, can induce specific killing of human CD45+ cell lines and primary human CD34+ blood stem and progenitor cells. Anti-CD45-PNU was the most potent on cell lines and in clonogenic assays, but promising results were obtained with all payloads tested. Of the other ADCs, there were differences in the activity between OCIM1 and Jurkat cells, e.g. anti-CD45-Maytansine derivative and anti-CD45- MMAE as well some difference between the two anti-CD45 clones. This may be due to a number of factors which include differences in sensitivity to the drug, differences in mitotic indices and intracellular trafficking as well as the final DAR achieved for each antibody. It is possible that for some payloads increased potency would be observed over longer culture times, for example to maximise toxicity of certain payloads such as those effecting cell killing through growth mechanisms. Using higher DARs, such as DARs of 4 or 8, might also increase the potency of some payloads. Example 4 - AML studies Results As the anti-CD45-PNU ADCs were very potent in cell viability assays, Ab1-PNU and MOPC21- PNU were assessed for their ability to delay onset of AML and prolong survival of mice. Ab1- PNU was able to slow AML progression in mice compared to MOPC21-PNU (Figure 15A) and was able to prolong survival of mice (Figure 15B). All control mice were culled by day 32, whereas 4/5 mice treated with Ab1-PNU were alive at the end of the experiment (day 48), with all remaining mice bearing tumour. Conclusions Ab1-PNU treatment was able to delay onset and progression of AML in mice, leading to prolonged survival compared to the Isotype-PNU treated mice. These data suggest that anti-CD45 ADCs can be used as anti-leukaemia agents. Example 5 - Generation of anti-CD45 biparatopic antibody Results Domain mapping analysis previously demonstrated complete loss of binding of Ab1 to the V5- CD45Δ2 truncation mutant, which consisted of the two membrane proximal fibronectin type III repeats, but lacked the distal fibronectin type III repeat, cysteine-rich region and N-terminal variable region, whilst Ab2 retained partial binding to V5-CD45Δ2 (Figure 16A and data not shown). Both antibodies bound to the full-length CD45 extracellular domain construct, V5-CD45 FL (Figure 16A and data not shown). As expected, Ab2-F405L.HA showed binding to the V5- CD45 FL and to V5-CD45Δ2 (Figure 16, left panels) whilst Ab1-S370K-K409R.His bound the full-length extracellular domain, but not the V5-CD45Δ2 truncation mutant (Figure 16, middle panels). However, Ab1-S370K-K409R.His was detected on the surface of cells expressing V5- CD45Δ2 truncation mutant only when part of the biparatopic antibody (Ab1-S370K-K409R.His x Ab2-F405L.HA), as well as on the surface of cells expressing the V5-CD45 FL protein but not to mock transfected cells (Figure 16, right panels). Conclusions These data indicated that an Ab1xAb2 biparatopic antibody (bpAb1-2) against CD45 could be generated and that flow cytometry using CD45 truncation mutants was able to distinguish biparatopic from monospecific binding. Forecast work plan 1 – anti-CD45 ADCs Additional anti-CD45 ADCs are generated using warheads that have different mechanisms of action to identify which ADC is the optimal clinical candidate. Using warheads with different mechanisms of action may allow for targeting quiescent as well as dividing cells, which could be more efficacious than using particular PBD warheads which only target dividing cells. A lower- potency payload will also be tested. Antibody drug conjugates comprising an antibody having heavy and light chain variable regions of SEQ ID NOs 1 and 2 (Ab1), or having heavy and light chain variable regions of SEQ ID NOs 11 and 12 (Ab2) are developed. High quantities of the anti-CD45 MAbs will be prepared for conjugation. The anti-CD45 antibodies are conjugated with a range of warheads to generate ADCs. The antibody having heavy and light chain variable regions of SEQ ID NOs 1 and 2 (Ab1) and the antibody having heavy and light chain variable regions of SEQ ID NOs 11 and 12 (Ab2) are each conjugated to different warheads including: MMAE (tubulin inhibition and bystander effect), anthracyclines (DNA alkylation and DNA cross-linking), amanitin (RNA polymerase II inhibitor), Duocarmycin (DNA alkylator), camptothecin (topoisomerase inhibition), calicheamycin (DNA damaging agent), Pseudomonas exotoxin A, or alpha sarcin, to generate a number of different ADCs. The yield, purity and drug/antibody ratio (DAR) of the ADCs is compared. The efficacy of the ADCs in vitro/ex vivo on human CD45+ cell lines and in clonogenic assays is evaluated. For example, in vitro cell viability assays are carried out using two CD45+ cell lines (OCIM and Jurkat) and a CD45- cell line (HEK 293T), in the presence of the two anti-CD45 antibodies being tested (Ab1 (having heavy and light chain variable regions of SEQ ID NOs 1 and 2) and Ab2 (having heavy and light chain variable regions of SEQ ID NOs 11 and 12)), either naked or in an ADC format using the selected drugs (MMAE, an anthracycline, amanitin, Duocarmycin, camptothecin, calicheamycin, Pseudomonas exotoxin A, or alpha sarcin), or a control antibody (rat IgGb2) again either naked or in an ADC format. Specific killing of CD45+ cells is observed at low concentrations, such as in the nanomolar concentration range with the ADCs with a wide therapeutic window. The antibodies and ADCs are also tested on CD34+ progenitor cells from a normal human donor and similar results are observed. Ex vivo treatment of human CD34+ cells with anti-CD45 ADC abrogates engraftment in NSG mice. Using a similar approach to that described above, human CD34+ cells are incubated either with the naked antibodies or in an ADC format, and then engrafted into immunodeficient (NSG) mice. At 1 nM concentrations, both naked antibodies and ADCs abrogate engraftment entirely; this effect persists for ADCs at at least a tenfold-lower concentration (0.1 nM or less). Based on these initial data one or more lead ADCs (e.g., the same antibody clone with two different payloads, or two different antibody clones with the same payloads) will be selected for scale-up production and testing prior to in vivo evaluation. In vitro cell assays and clonogenic assays will be performed to confirm efficacy of the ADCs. In vitro stability of the ADCs in mouse and human serum will be determined to monitor aggregate DAR loading over time. The antibodies comprising a mutant form of human IgG1 (AAA), which does not bind the human neonatal Fc receptor and therefore confers short in vivo half-life, have been compared with the rat IgG2b format antibodies (see e.g., Figure 6). Monitoring of plasma clearance at an equivalent dose of rat and human-mutant antibodies showed that the hIgG1-AAA anti-CD45 antibodies are cleared from immunodeficient (NSG) mice, or another suitable animal model, quicker than rat IgG2b antibodies. It is also crucial to assess the kinetics and stability of ADCs in vivo given the potential for off-target toxicity. The toxicity profiles of the lead ADCs are evaluated. One or more doses of the lead ADCs are injected into NSG immunodeficient mice, or another suitable animal model, and toxicity against non-haematological tissues is assessed using biochemical and/or histological analysis. In vivo testing in immunodeficient (NSG) mice, or another suitable animal model, shows that the antibodies in ADC format are well tolerated at 1 mg/kg. All mice or animals in this study are alive and well at least one month post-injection and show no weight loss. The PK data for the antibodies in ADC format indicate that very little de-conjugation of payload occurs in vivo, which suggests these therapeutics will translate to clinical phase with a low toxicity profile. The optimum dose for subsequent in vivo experiments can be determined using these studies. The efficacy of the lead ADCs in enabling successful transplantation of autologous GFP+ HSCs into humanised mice is evaluated. Anti-CD45 ADCs completely delete HSCs in humanised NSG mice in vivo. NSG mice are transplanted with human CD34+ progenitor cells, and several weeks later are shown to express human CD45+ cells in blood. They are then injected either with buffer (control), or the naked antibody combination (i.e., Ab1 + Ab2), or ADCs derived from each antibody (i.e., Ab1 ADC or Ab2 ADC). The ADCs demonstrate a dose-dependent and prolonged decrease in CD45+ cell level in blood that is significantly improved as compared to the transient decrease that is seen for the naked antibodies. The efficacy of the lead ADCs in enabling successful transplantation in a gene therapy model is evaluated. The efficacy of the lead ADCs in an AML leukaemia model is also evaluated. The efficacy of the ADCs (i) in vitro, (ii) in enabling successful transplantation of autologous GFP+ HSCs into humanised mice, and/or (iii) in inducing tumour regression in a xenogeneic cell line model of established AML, will be compared with the efficacy in the same assays of existing anti- CD45-PBD ADCs (SG3249/tesirine payload) that are disclaimed herein. EC50 values for the ADCs in leukaemic cell lines and cytotoxicity in clonogenic assays should be comparable to those achieved with anti-CD45-PBD ADCs as disclaimed herein, or in the expected range for the drug class. A lack of toxicity to non-haematopoietic tissues is observed for the ADCs. Greater than 20% stable multilineage engraftment of gene corrected human HSCs in the bone marrow of humanised mice treated with ADC followed by secondary transplantation is observed. Forecast work plan 2 – biparatopic antibody A biparatopic antibody having the heavy and light chain variable regions of SEQ ID NOs 1 and 2 (Ab1 variable domain) on one arm, and the heavy and light chain variable regions of SEQ ID NOs 11 and 12 (Ab2 variable domain) on the other arm is being developed (bpAb1-2). This antibody (bpAb1-2) is developed in different formats including, a rat IgG2b format, a human IgG1-AAA format, and a rat-mouse hybrid antibody format, as described herein. The combination of Ab1 and Ab2 has been shown to have high CDC activity both in vitro and in vivo. However, to be most clinically effective it would be advantageous to enhance this CDC activity. Ab1 and Ab2 bind at distinct non-overlapping sites on the extracellular domain of CD45. The variable domains of Ab1 and Ab2 are combined to form a biparatopic antibody (bpAb1-2). The bpAb1-2 has a particularly high and improved binding affinity (or at least equivalent binding) for the CD45 target as compared to the individual antibodies Ab1 or Ab2, as measured for example by Biacore at 25°C with the CD45 extracellular domain immobilised on the sensor chip. The bpAb1-2 also shows an enhanced or equivalent uptake by target cells, as measured for example by live-cell imaging. Antibody drug conjugates comprising bpAb1-2 are developed. High quantities of the anti-CD45 bpAb1-2 will be prepared for conjugation. The bpAb1-2 is conjugated with a range of warheads to generate ADCs. The bpAb1-2 is conjugated to different warheads including: MMAE (tubulin inhibition and bystander effect), anthracyclines (DNA alkylation and DNA cross-linking), amanitin (RNA polymerase II inhibitor), Duocarmycin (DNA alkylator), camptothecin (topoisomerase inhibition), calicheamycin, Pseudomonas exotoxin A, or alpha sarcin, to generate a number of different ADCs. The yield, purity and drug/antibody ratio (DAR) of the ADCs is compared. Lead bpAb1-2 ADCs are selected. The efficacy of bpAb1-2 in both antibody and ADC formats in vitro/ex vivo on human CD45+ cell lines and in clonogenic assays is evaluated. For example, in vitro cell viability assays are carried out using two CD45+ cell lines (OCIM1 and Jurkat) and a CD45- cell line (HEK 293T), in the presence of Ab1 and Ab2, or bpAb1-2, or a control antibody (rat IgGb2), in both antibody and ADC formats, in presence or absence of serum (as a source of complement). Cell killing is observed at lower concentrations, such as in the nanomolar concentration range, for bpAb1-2 as compared to Ab1 and Ab2, in both antibody and ADC formats. The antibodies and ADCs are also tested on CD34+ progenitor cells from a normal human donor and similar results are observed. Ex vivo treatment of human CD34+ cells with bpAb1-2 in presence of serum abrogates engraftment in NSG mice. Using a similar approach to that described above, human CD34+ cells are incubated either with Ab1 and Ab2, or bpAb1-2, in antibody or ADC formats, in presence of absence of serum, and then engrafted into immunodeficient (NSG) mice. At 1 nM concentrations, both Ab1 and Ab2, and bpAb1-2 (in both antibody or ADC formats) abrogate engraftment entirely; this effect persists for bpAb1-2 at e.g., a tenfold-lower concentration (0.1 nM or less). In vitro stability of bpAb1-2 in both antibody and ADC formats in mouse and human serum will be determined. The bpAb1-2 in hIgG1-AAA format, which does not bind the human neonatal Fc receptor and therefore confers short in vivo half-life, is compared with the rat IgG2b format bpAb1- 2, and the corresponding ADCs are also tested. Monitoring of plasma clearance at an equivalent dose of rat and human-mutant antibodies shows that the hIgG1-AAA bpAb1-2 is cleared from immunodeficient (NSG) mice, or another suitable animal model, quicker than rat IgG2b bpAb1-2, as is the case for the corresponding ADCs. The kinetics and stability of bpAb1-2 in vivo is evaluated. A dose of bpAb1-2 in either antibody or ADC format is injected into NSG immunodeficient mice, or another suitable animal model, and toxicity against non-haematological tissues is assessed using biochemical and/or histological analysis. In vivo testing in immunodeficient (NSG) mice, or another suitable animal model, shows that bpAb1-2, in either antibody or ADC format, is well tolerated at 1 mg/kg. All mice or animals in this study are alive and well at least one month post-injection and show no weight loss. The PK data for bpAb1-2 indicate that this therapeutic will translate to clinical phase with a low toxicity profile. The optimum dose for subsequent in vivo experiments can be determined using these studies. Lead bpAb1-2 ADCs are selected. The efficacy of bpAb1-2 in ADC format in enabling successful transplantation of autologous GFP+ HSCs into humanised mice is evaluated. bpAb1-2 ADC completely deletes HSCs in humanised NSG mice in vivo. NSG mice are transplanted with human CD34+ progenitor cells, and several weeks later are shown to express human CD45+ cells in blood. They are then injected either with buffer (control), the antibody combination (i.e., Ab1 + Ab2), Ab1 ADC, Ab2 ADC, or bpAb1-2 ADC. bpAb1-2 ADC demonstrates a dose-dependent and prolonged decrease in CD45+ cell level in blood that is significantly improved as compared to the transient decrease that is seen for Ab1 and Ab2. It would also be possible to test bpAb1-2 in antibody format using an NSG strain where complement activity has been restored (Verma, et al., (2017) Journal of Immunological Methods, 446: 47-53). The bpAb1-2 in either antibody or ADC format could also be tested in other suitable animal models for investigating HSC transplantation. The efficacy of bpAb1-2 ADC in enabling successful transplantation in a gene therapy model is evaluated. The efficacy of bpAb1-2 ADC in an AML leukaemia model is also evaluated. The efficacy of bpAb1-2 ADC (i) in vitro, (ii) in enabling successful transplantation of autologous GFP+ HSCs into humanised mice, and/or (iii) in inducing tumour regression in a xenogeneic cell line model of established AML, is compared with the efficacy in the same assays of the anti-CD45 ADCs of Forecast work plan 1. EC50 values for bpAb1-2 ADC in leukaemic cell lines and cytotoxicity in clonogenic assays should be comparable to those achieved with the ADCs of Forecast work plan 2, or in the expected range for the drug class. A lack of toxicity to non-haematopoietic tissues is observed for bpAb1-2 ADC. Greater than 20% stable multilineage engraftment of gene corrected human HSCs in the bone marrow of humanised mice treated with bpAb1-2 ADC followed by secondary transplantation is observed. References 1. WO 1995/013093 2. WO 2020/146432 3. Straathof, K. C., et al., Lancet 2009: 374: 912-20 4. “Monoclonal Antibodies; A manual of techniques”, H Zola, CRC Press, 1988 5. “Monoclonal Hybridoma Antibodies: Techniques and Application”, SGR Hurrell, CRC Press, 1982 6. Caceci et al. Byte 1984: 9: 340-362 7. Kabat et al., Sequences of Proteins of Immunological Interest, U.S. Department of Health and Human Services, 1991 8. Chothia, C., Lesk, A. M. J. Mol. Biol.1987: 196: 901–17 9. Giudicelli V, et al., Nucleic Acids Res.1997: 25: 206–11; 42 10. Lefranc, M. P. Immunol Today 1997: 18: 509 11. Karlin and Altschul (1990) Proc. Natl. Acad. Sci. USA 87:2264-68 12. Karlin and Altschul (1993) Proc. Natl. Acad. Sci. USA 90:5873-77 13. Altschul, et al. (1990) J. Mol. Biol.215:403-10 14. Altschul et al., (1997) Nucleic Acids Res.25(17):3389-3402 15. US 5,585,089 16. Dubowchik et al., Bioconjugate Chemistry, 2002, 13,855-869 17. Remington’s Pharmaceutical Sciences, by E. W. Martin, Mack Publishing Co., Easton, PA, 19th Edition, 1995 18. “Bioconjugate Techniques”, G.T. Hermanson, 3rd Ed., Elsevier Inc., 2013 19. Yang et al. Med Res Rev.2020; 1–32 20. Verma, et al., (2017) Journal of Immunological Methods, 446: 47-53 21. Thurston, et al., (1994) Chem. Rev.1994, 433-465 22. Antonow, D. and Thurston, D.E., (2011) Chem. Rev.111 (4), 2815-2864 23. Krance, R. A., et al. (2003), Biol Blood Marrow Transplant 9(4): 273-281.3 24. Labrijn, A.F., et al., (2017), Sci. Rep.7: 2476. LIST OF EMBODIMENTS 1. A monoclonal antibody or fragment thereof that specifically binds human CD45, comprising a light chain variable domain and a heavy chain variable domain, wherein: (a) the light chain variable domain comprises a light chain complementarity determining region (LCDR) 1, a LCDR2 and a LCDR3, and wherein the heavy chain variable domain comprises a heavy chain complementarity determining region (HCDR) 1, a HCDR2 and a HCDR3, wherein the antibody comprises the complementarity determining region (CDR) sequences of the light chain variable domain sequence SEQ ID NO: 1 and the heavy chain variable domain sequence SEQ ID NO: 2; (b) the light chain variable domain comprises a light chain complementarity determining region (LCDR) 1, a LCDR2 and a LCDR3, and wherein the heavy chain variable domain comprises a heavy chain complementarity determining region (HCDR) 1, a HCDR2 and a HCDR3, wherein LCDR1 comprises the sequence of SEQ ID NO: 3, LCDR2 comprises the sequence of SEQ ID NO: 4, and LCDR3 comprises the sequence of SEQ ID NO: 5, and HCDR1 comprises the sequence of SEQ ID NO: 6, HCDR2 comprises the sequence of SEQ ID NO: 7, and HCDR3 comprises the sequence of SEQ ID NO: 8; (c) the light chain variable domain comprises a sequence of SEQ ID NO: 1, and wherein the heavy chain variable domain comprises a sequence of SEQ ID NO: 2; or (d) the antibody comprises a light chain comprising a sequence of SEQ ID NO: 9 and a heavy chain comprising a sequence of SEQ ID NO: 10. 2. A monoclonal antibody or fragment thereof that specifically binds human CD45, comprising a light chain variable domain and a heavy chain variable domain, wherein: (a) the light chain variable domain comprises a light chain complementarity determining region (LCDR) 1, a LCDR2 and a LCDR3, and wherein the heavy chain variable domain comprises a heavy chain complementarity determining region (HCDR) 1, a HCDR2 and a HCDR3, wherein the antibody comprises the complementarity determining region (CDR) sequences of the light chain variable domain sequence SEQ ID NO: 11 and the heavy chain variable domain sequence SEQ ID NO: 12; (b) the light chain variable domain comprises a light chain complementarity determining region (LCDR) 1, a LCDR2 and a LCDR3, and wherein the heavy chain variable domain comprises a heavy chain complementarity determining region (HCDR) 1, a HCDR2 and a HCDR3, wherein LCDR1 comprises the sequence of SEQ ID NO: 13, LCDR2 comprises the sequence of SEQ ID NO: 14, and LCDR3 comprises the sequence of SEQ ID NO: 15, and HCDR1 comprises the sequence of SEQ ID NO: 16, HCDR2 comprises the sequence of SEQ ID NO: 17, and HCDR3 comprises the sequence of SEQ ID NO: 18; (c) the light chain variable domain comprises a sequence of SEQ ID NO: 11, and wherein the heavy chain variable domain comprises a sequence of SEQ ID NO: 12; or (d) the antibody comprises a light chain comprising a sequence of SEQ ID NO: 19 and a heavy chain comprising a sequence of SEQ ID NO: 20. 3. A biparatopic antibody or biparatopic fragment thereof, that specifically binds human CD45, comprising a first antigen binding domain and a second antigen binding domain, wherein: A. (i) the first antigen binding domain comprises a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a LCDR1 comprising the sequence of SEQ ID NO: 3, a LCDR2 comprising the sequence of SEQ ID NO: 4, and a LCDR3 comprising the sequence of SEQ ID NO: 5, and wherein the heavy chain variable domain comprises a HCDR1 comprising the sequence of SEQ ID NO: 6, a HCDR2 comprising the sequence of SEQ ID NO: 7, and a HCDR3 comprising the sequence of SEQ ID NO: 8; and (ii) the second antigen binding domain comprises a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a LCDR1 comprising the sequence of SEQ ID NO: 13, a LCDR2 comprising the sequence of SEQ ID NO: 14, and a LCDR3 comprising the sequence of SEQ ID NO: 15, and wherein the heavy chain variable domain comprises a HCDR1 comprising the sequence of SEQ ID NO: 16, a HCDR2 comprising the sequence of SEQ ID NO: 17, and a HCDR3 comprising the sequence of SEQ ID NO: 18; or B. (i) the first antigen binding domain comprises a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a sequence of SEQ ID NO: 1, and wherein the heavy chain variable domain comprises a sequence of SEQ ID NO: 2; and (ii) the second antigen binding domain comprises a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a sequence of SEQ ID NO: 11, and wherein the heavy chain variable domain comprises a sequence of SEQ ID NO: 12; or C. the first or second antigen binding domain comprises a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a LCDR1 comprising the sequence of SEQ ID NO: 3, a LCDR2 comprising the sequence of SEQ ID NO: 4, and a LCDR3 comprising the sequence of SEQ ID NO: 5, and wherein the heavy chain variable domain comprises a HCDR1 comprising the sequence of SEQ ID NO: 6, a HCDR2 comprising the sequence of SEQ ID NO: 7, and a HCDR3 comprising the sequence of SEQ ID NO: 8; or D. the first or second antigen binding domain comprises a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a LCDR1 comprising the sequence of SEQ ID NO: 13, a LCDR2 comprising the sequence of SEQ ID NO: 14, and a LCDR3 comprising the sequence of SEQ ID NO: 15, and wherein the heavy chain variable domain comprises a HCDR1 comprising the sequence of SEQ ID NO: 16, a HCDR2 comprising the sequence of SEQ ID NO: 17, and a HCDR3 comprising the sequence of SEQ ID NO: 18; or E. the first or second antigen binding domain comprises a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a sequence of SEQ ID NO: 1, and wherein the heavy chain variable domain comprises a sequence of SEQ ID NO: 2; or F. the first or second antigen binding domain comprises a light chain variable domain and a heavy chain variable domain, wherein the light chain variable domain comprises a sequence of SEQ ID NO: 11, and wherein the heavy chain variable domain comprises a sequence of SEQ ID NO: 12. 4. The antibody or fragment thereof of any one of embodiments 1-3, wherein the antibody is a rat antibody. 5. The antibody or fragment thereof of any one of embodiments 1-3, wherein the antibody is a chimeric or humanised antibody. 6. The antibody or fragment thereof of any one of embodiments 1- 5, which is a single domain fragment, a Fab fragment, a Fab' fragment, a F(ab)'2 fragment, a single chain Fab (scFab) fragment, a single chain Fv protein (scFv), a tandem scFv protein, a disulfide stabilized Fv protein (dsFv), or a scFv-Fc protein. 7. The antibody or fragment thereof of any one of the preceding embodiments, wherein the antibody is an IgG. 8. The antibody or fragment thereof of embodiment 5, wherein the antibody is a rat IgG2b antibody. 9. An antibody drug conjugate of formula (I): Ab – (L–D)p (I) wherein Ab is an antibody or fragment thereof according to any one of the preceding embodiments; wherein L is a linker connecting Ab to D; wherein D is an anti-cancer agent, a cytotoxic agent or a cytostatic agent; wherein p is from 1 to 8; and wherein D is not a pyrrolobenzodiazepine (PBD), such as a PBD dimer. 10. The antibody drug conjugate of embodiment 9, wherein each D is independently selected from the group consisting of a tubulin inhibitor, a DNA damaging agent, a topoisomerase I inhibitor, and an RNA polymerase II inhibitor; optionally wherein each D is independently selected from the group consisting of MMAE, Maytansine, Maytansine derivative, Dxd, Duocarmycin, PNU, an anthracycline, amanitin, Duocarmycin, calicheamycin, camptothecin, Pseudomonas exotoxin A, and alpha sarcin; optionally wherein each D is independently selected from the group consisting of Monomethyl auristatin E (MMAE), an anthracycline, amanitin, Duocarmycin, calicheamycin, camptothecin, Pseudomonas exotoxin A, and alpha sarcin; optionally wherein each D is independently selected from the group consisting of MMAE, Maytansine, Maytansine derivative, Dxd, Duocarmycin, and PNU. 11. The antibody drug conjugate of embodiment 9 or 10, wherein p is 1 to 4, 2 to 4, or 1 to 3, optionally wherein p is about 2. 12. The antibody drug conjugate of any one of embodiments 9-11, wherein each (L–D) is the same or wherein at least two different species of (L–D) are present. 13. The antibody drug conjugate of any one of embodiments 9-12, wherein L is a cleavable linker, optionally wherein L is selected from the group consisting of acid-cleavable linkers, protease-cleavable linkers, and disulfide linkers. 14. A pharmaceutical composition comprising the antibody of any one of embodiments 1-8 and optionally a pharmaceutically acceptable carrier. 15. The pharmaceutical composition of embodiment 14, comprising a first antibody according to embodiment 1 and a second antibody according to embodiment 2. 16. A pharmaceutical composition comprising an antibody drug conjugate according to any one of embodiments 9-13, and optionally a pharmaceutically acceptable carrier. 17. The pharmaceutical composition of embodiment 16, comprising a first antibody drug conjugate according to any one of embodiments 9-13, a second, different antibody drug conjugate according to any one of embodiments 9-13. 18. The pharmaceutical composition of embodiment 17, wherein: (a) Ab of both the first and second antibody drug conjugates is according to embodiment 1, and (L–D) of the first antibody drug conjugate is different from (L–D) of the second antibody drug conjugate; (b) Ab of both the first and second antibody drug conjugates is according to embodiment 2, and (L–D) of the first antibody drug conjugate is different from (L–D) of the second antibody drug conjugate; (c) Ab of the first antibody drug conjugate is according to embodiment 1, and Ab of the second antibody drug conjugate is according to embodiment 2; and (L–D) of the first antibody drug conjugate is the same as (L–D) of the second antibody drug conjugate; or (d) Ab of the first antibody drug conjugate is according to embodiment 1, and Ab of the second antibody drug conjugate is according to embodiment 2; and (L–D) of the first antibody drug conjugate is different from (L–D) of the second antibody drug conjugate. 19. A method of treating haematological cancer, the method comprising administering the antibody of any one of embodiments 1-8, the antibody drug conjugate of any one of embodiments 9-13, or the pharmaceutical composition of any one of embodiments 14-18, to a subject in need thereof. 18. The method of embodiment 17, wherein the haematological cancer is selected from the group consisting of: acute myeloid leukaemia, acute lymphoblastic leukaemia, chronic lymphocytic leukaemia, chronic myeloid leukaemia, myelodysplasia, myeloproliferative diseases, multiple myeloma, non-Hodgkin’s lymphoma and Hodgkin’s disease. 19. A method of preparing a subject for transplantation of haematopoietic stem cells, the method comprising administering the antibody of any one of embodiments 1-8, the antibody drug conjugate of any one of embodiments 9-13, or the pharmaceutical composition of any one of embodiments 14-18. 20. The method of embodiment 19, wherein said preparing for transplantation of haematopoietic stem cells comprises conditioning the subject for engraftment of haematopoietic stem cells. 21. The method of embodiment 19 or 20, wherein the haematopoietic stem cells are allogeneic. 22. The method of embodiment 21, wherein said transplantation of haematopoietic stem cells is for treating a malignant disease or disorder, optionally selected from the group consisting of: acute myeloid leukaemia, acute lymphoblastic leukaemia, chronic myeloid leukaemia, chronic lymphocytic leukaemia, myelodysplasia, myeloproliferative diseases, myeloma, non-Hodgkin’s lymphoma and Hodgkin’s disease. 23. The method of embodiment 21, wherein said transplantation of haematopoietic stem cells is for treating a non-malignant disease or disorder, optionally selected from the group consisting of: severe aplastic anaemia, a bone marrow failure disorder, a primary immunodeficiency, primary haemophagocytic lymphohistiocytosis, a haemoglobinopathy, and a genetic metabolic disease. 24. The method of embodiment 21 or 23, wherein said transplantation of haematopoietic stem cells is for treating (i) a bone marrow failure disorder selected from severe aplastic anaemia, Fanconi anaemia, dyskeratosis congenita, Shwachman-Diamond Syndrome, severe congenital neutropenia, Diamond-Blackfan anaemia; (ii) a primary immunodeficiency selected from SCID, chronic granulomatous disease, Wiskott-Aldrich syndrome, CD40 ligand deficiency, XLP, MHC Class II deficiency, and primary haemophagocytic lymphohistiocytosis; (iii) a haemoglobinopathy selected from sickle cell disease, β- thalassaemia major; or (iv) a genetic metabolic disease selected from Hurler syndrome, X-linked adrenoleukodystrophy, alpha mannosidosis and osteopetrosis. 25. The method of embodiment 19 or 20, wherein the haematopoietic stem cells are autologous. 26. The method of embodiment 25, wherein said transplantation of haematopoietic stem cells is for treating a malignant disease or disorder, optionally selected from the group consisting of: multiple myeloma, non-Hodgkin’s lymphoma, Hodgkin’s disease. 27. The method of embodiment 25, wherein said transplantation of haematopoietic stem cells is for treating an autoimmune disease or disorder, optionally selected from the group consisting of: multiple sclerosis, systemic sclerosis, juvenile inflammatory arthritis and systemic lupus erythematosus. 28. The method of embodiment 19 or 20, wherein the haematopoietic stem cells are genetically-modified autologous haematopoietic stem cells. 29. The method of embodiment 19, 20 or 28, wherein said transplantation of haematopoietic stem cells is for gene therapy. 30. The method of embodiment 29, wherein the gene therapy is for treating a genetic haematological disease or disorder, a primary immunodeficiency or a genetic metabolic disorder. 31. The method of embodiment 29 or 30, wherein the gene therapy is for treating (i) a genetic haematological disease or disorder selected from a transfusion dependent haemoglobinopathy, sickle cell disease, β-thalassaemia major, and Fanconi anaemia; (ii) a primary immunodeficiency selected from SCID, chronic granulomatous disease, Wiskott-Aldrich syndrome and primary haemophagocytic lymphohistiocytosis; or (iii) a genetic metabolic disorder selected from Hurler’s syndrome, Sanfilippo disease, X-adrenoleukodystrophy, and metachromatic leukodystrophy. 32. A method of engrafting stem cells in a subject, the method comprising: (a) administering to the subject an effective amount of the antibody of any one of embodiments 1- 8, the antibody drug conjugate of any one of embodiments 9-13, or the pharmaceutical composition of any one of embodiments 14-18; and (b) administering a stem cell population to the target tissue of the subject, wherein the administered stem cell population engrafts in the target tissue of the subject. 33. An antibody of any one of embodiments 1-8, the antibody drug conjugate of any one of embodiments 9-13, or the pharmaceutical composition of any one of embodiments 14-18, for use in a method of treating haematological cancer. 34. An antibody of any one of embodiments 1-8, the antibody drug conjugate of any one of embodiments 9-13, or the pharmaceutical composition of any one of embodiments 14-18, for use in a method of preparing a subject for transplantation of haematopoietic stem cells. 35. A first antibody according to any one of embodiments 1-8 and a second, different antibody according to any one of embodiments 1-8, for use in a method of treating haematological cancer, wherein the method comprises administering the first antibody and the second antibody to a subject in need thereof. 36. A first antibody drug conjugate according to any one of embodiments 9-13 and a second, different antibody drug conjugate according to any one of embodiments 9-13, for use in a method of treating haematological cancer, wherein the method comprises administering the first antibody drug conjugate and the second antibody drug conjugate, to a subject in need thereof. 37. A first antibody according to any one of embodiments 1-8 and a second, different antibody according to any one of embodiments 1-8, for use in a method of preparing a subject for transplantation of haematopoietic stem cells, wherein the method comprises administering the first antibody and the second antibody to a subject in need thereof. 38. A first antibody drug conjugate according to any one of embodiments 9-13 and a second, different antibody drug conjugate according to any one of embodiments 9-13, for use in a method of preparing a subject for transplantation of haematopoietic stem cells, wherein the method comprises administering the first antibody drug conjugate and the second antibody drug conjugate, to a subject in need thereof. 39. A first antibody according to any one of embodiments 1-8, for use in a method of treating haematological cancer, wherein the method comprises administering the first antibody, and a second, different antibody according to any one of embodiments 1-8, to a subject in need thereof. 40. A first antibody drug conjugate according to any one of embodiments 9-13, for use in a method of treating haematological cancer, wherein the method comprises administering the first antibody drug conjugate, and a second, different antibody drug conjugate according to any one of embodiments 9-13, to a subject in need thereof. 41. A first antibody according to any one of embodiments 1-8, for use in a method of preparing a subject for transplantation of haematopoietic stem cells, wherein the method comprises administering the first antibody, and a second, different antibody according to any one of embodiments 1-8, to a subject in need thereof. 42. A first antibody drug conjugate according to any one of embodiments 9-13, for use in a method of preparing a subject for transplantation of haematopoietic stem cells, wherein the method comprises administering the first antibody drug conjugate and a second, different antibody drug conjugate according to any one of embodiments 9-13, to a subject in need thereof.

SEQUENCE LISTING SEQ ID NO 1: light chain variable domain of YTH 24.5 (Ab1) DVVMTQTPVSLSVSLGGQVSISCRSSQSFVSSDGNTYLNWYLQKPGQSPQLLIYKVSNRL S GVPDRFSGSGSGTDFTLKISRVEHDDLGVYYCGQASKIPLTFGSGTKLEIK SEQ ID NO 2: heavy chain variable domain of YTH 24.5 (Ab1) QVNLLQSGAALVKPGASVKLSCKASSYTFTDYYIHWVKQSHGKTLEWIGYINPKSGFTNY NEKFRRKATLTVDKSTNTAYMDISRLTSEDSATYYCTRRTGVIPMDAWGQGASVTVSS SEQ ID NO 3: LCDR1 of YTH 24.5 (Ab1) (as defined by Kabat system) RSSQSFVSSDGNTYLN SEQ ID NO 4: LCDR2 of YTH 24.5 (Ab1) (as defined by Kabat system) KVSNRLS SEQ ID NO 5: LCDR3 of YTH 24.5 (Ab1) (as defined by Kabat system) GQASKIPLT SEQ ID NO 6: HCDR1 of YTH 24.5 (Ab1) (as defined by Kabat system) DYYIH SEQ ID NO 7: HCDR2 of YTH 24.5 (Ab1) (as defined by Kabat system) YINPKSGFTNYNEKFRR SEQ ID NO 8: HCDR3 of YTH 24.5 (Ab1) (as defined by Kabat system) RTGVIPMDA SEQ ID NO 9: light chain of rat IgG2b YTH 24.5 (rat IgG2b Ab1) DVVMTQTPVSLSVSLGGQVSISCRSSQSFVSSDGNTYLNWYLQKPGQSPQLLIYKVSNRL S GVPDRFSGSGSGTDFTLKISRVEHDDLGVYYCGQASKIPLTFGSGTKLEIKRADAAPTVS IF PPSMEQLTSGGATVVCFVNNFYPRDISVKWKIDGSEQRDGVLDSVTDQDSKDSTYSMSST LSLTKVEYERHNLYTCEVVHKTSSSPVVKSFNRNEC SEQ ID NO 10: heavy chain of rat IgG2b YTH 24.5 (rat IgG2b Ab1) QVNLLQSGAALVKPGASVKLSCKASSYTFTDYYIHWVKQSHGKTLEWIGYINPKSGFTNY NEKFRRKATLTVDKSTNTAYMDISRLTSEDSATYYCTRRTGVIPMDAWGQGASVTVSSAQ TTAPSVYPLAPGCGDTTSSTVTLGCLVKGYFPEPVTVTWNSGALSSDVHTFPAVLQSGLY T LTSSVTSSTWPSQTVTCNVAHPASSTKVDKKVERRNGGIGHKCPTCPTCHKCPVPELLGG P SVFIFPPKPKDILLISQNAKVTCVVVDVSEEEPDVQFSWFVNNVEVHTAQTQPREEQYNS TF RVVSALPIQHQDWMSGKEFKCKVNNKALPSPIEKTISKPKGLVRKPQVYVMGPPTEQLTE QTVSLTCLTSGFLPNDIGVEWTSNGHIEKNYKNTEPVMDSDGSFFMYSKLNVERSRWDSR APFVCSVVHEGLHNHHVEKSISRPPGK SEQ ID NO 11: light chain variable domain of YTH 54.12 (Ab2) DVQMTQSPSYLAASPGESVSISCKASKSISNYLAWYQQKPGEANKILIYSGSTLQSGTPS RF SGSGSGTDFSLTIRNLEPEDFAVYYCQQYDEKPLTFGSGTKLEIK SEQ ID NO 12: heavy chain variable domain of YTH 54.12 (Ab2) EVQLVESGGGLVQPGGSMKLSCAASGFTFSDYYMAWVRQAPKKGLEWVASMSFAGSST YYGDSVKGRFTISRDNAKTTLYLQMNSLRSEDTATYYCARMYTTDYYLYWYFDFWGPG TMVTVSS SEQ ID NO 13: LCDR1 of YTH 54.12 (Ab2)(as defined by Kabat system) KASKSISNYLA SEQ ID NO 14: LCDR2 of YTH 54.12 (Ab2) (as defined by Kabat system) SGSTLQS SEQ ID NO 15: LCDR3 of YTH 54.12 (Ab2) (as defined by Kabat system) QQYDEKPLT SEQ ID NO 16: HCDR1 of YTH 54.12 (Ab2) (as defined by Kabat system) DYYMA SEQ ID NO 17: HCDR2 of YTH 54.12 (Ab2) (as defined by Kabat system) SMSFAGSSTYYGDSVKG SEQ ID NO 18: HCDR3 of YTH 54.12 (Ab2) (as defined by Kabat system) MYTTDYYLYWYFDF SEQ ID NO 19: light chain of rat IgG2b YTH 54.12 (rat IgG2b Ab2) DVQMTQSPSYLAASPGESVSISCKASKSISNYLAWYQQKPGEANKILIYSGSTLQSGTPS RF SGSGSGTDFSLTIRNLEPEDFAVYYCQQYDEKPLTFGSGTKLEIKRADAAPTVSIFPPSM EQ LTSGGATVVCFVNNFYPRDISVKWKIDGSEQRDGVLDSVTDQDSKDSTYSMSSTLSLTKV EYERHNLYTCEVVHKTSSSPVVKSFNRNEC SEQ ID NO 20: heavy chain of rat IgG2b YTH 54.12 (rat IgG2b Ab2) EVQLVESGGGLVQPGGSMKLSCAASGFTFSDYYMAWVRQAPKKGLEWVASMSFAGSST YYGDSVKGRFTISRDNAKTTLYLQMNSLRSEDTATYYCARMYTTDYYLYWYFDFWGPG TMVTVSSAQTTAPSVYPLAPGCGDTTSSTVTLGCLVKGYFPEPVTVTWNSGALSSDVHTF P AVLQSGLYTLTSSVTSSTWPSQTVTCNVAHPASSTKVDKKVERRNGGIGHKCPTCPTCHK CPVPELLGGPSVFIFPPKPKDILLISQNAKVTCVVVDVSEEEPDVQFSWFVNNVEVHTAQ TQ PREEQYNSTFRVVSALPIQHQDWMSGKEFKCKVNNKALPSPIEKTISKPKGLVRKPQVYV MGPPTEQLTEQTVSLTCLTSGFLPNDIGVEWTSNGHIEKNYKNTEPVMDSDGSFFMYSKL N VERSRWDSRAPFVCSVVHEGLHNHHVEKSISRPPGK SEQ ID NO 21: LCFR1 of YTH 24.5 (Ab1) DVVMTQTPVSLSVSLGGQVSISC SEQ ID NO 22: LCFR2 of YTH 24.5 (Ab1) WYLQKPGQSPQLLIY SEQ ID NO 23: LCFR3 of YTH 24.5 (Ab1) GVPDRFSGSGSGTDFTLKISRVEHDDLGVYYC SEQ ID NO 24: LCFR4 of YTH 24.5 (Ab1) FGSGTKLEIK SEQ ID NO 25: HCFR1 of YTH 24.5 (Ab1) QVNLLQSGAALVKPGASVKLSCKASSYTFT SEQ ID NO 26: HCFR2 of YTH 24.5 (Ab1) WVKQSHGKTLEWIG SEQ ID NO 27: HCFR3 of YTH 24.5 (Ab1) KATLTVDKSTNTAYMDISRLTSEDSATYYCTR SEQ ID NO 28: HCFR4 of YTH 24.5 (Ab1) WGQGASVTVSS SEQ ID NO 29: LCFR1 of YTH 54.12 (Ab2) DVQMTQSPSYLAASPGESVSISC SEQ ID NO 30: LCFR2 of YTH 54.12 (Ab2) WYQQKPGEANKILIY SEQ ID NO 31: LCFR3 of YTH 54.12 (Ab2) GTPSRFSGSGSGTDFSLTIRNLEPEDFAVYYC SEQ ID NO 32: LCFR4 of YTH 54.12 (Ab2) FGSGTKLEIK SEQ ID NO 33: HCFR1 of YTH 54.12 (Ab2) EVQLVESGGGLVQPGGSMKLSCAASGFTFS SEQ ID NO 34: HCFR2 of YTH 54.12 (Ab2) WVRQAPKKGLEWVA SEQ ID NO 35: HCFR3 of YTH 54.12 (Ab2) RFTISRDNAKTTLYLQMNSLRSEDTATYYCAR SEQ ID NO 36: HCFR4 of YTH 54.12 (Ab2) WGPGTMVTVSS SEQ ID NO 37: human CD45 MTMYLWLKLLAFGFAFLDTEVFVTGQSPTPSPTGLTTAKMPSVPLSSDPLPTHTTAFSPA S TFERENDFSETTTSLSPDNTSTQVSPDSLDNASAFNTTGVSSVQTPHLPTHADSQTPSAG TD TQTFSGSAANAKLNPTPGSNAISDVPGERSTASTFPTDPVSPLTTTLSLAHHSSAALPAR TSN TTITANTSDAYLNASETTTLSPSGSAVISTTTIATTPSKPTCDEKYANITVDYLYNKETK LFT AKLNVNENVECGNNTCTNNEVHNLTECKNASVSISHNSCTAPDKTLILDVPPGVEKFQLH DCTQVEKADTTICLKWKNIETFTCDTQNITYRFQCGNMIFDNKEIKLENLEPEHEYKCDS EI LYNNHKFTNASKIIKTDFGSPGEPQIIFCRSEAAHQGVITWNPPQRSFHNFTLCYIKETE KDC LNLDKNLIKYDLQNLKPYTKYVLSLHAYIIAKVQRNGSAAMCHFTTKSAPPSQVWNMTVS MTSDNSMHVKCRPPRDRNGPHERYHLEVEAGNTLVRNESHKNCDFRVKDLQYSTDYTFK AYFHNGDYPGEPFILHHSTSYNSKALIAFLAFLIIVTSIALLVVLYKIYDLHKKRSCNLD EQQ ELVERDDEKQLMNVEPIHADILLETYKRKIADEGRLFLAEFQSIPRVFSKFPIKEARKPF NQ NKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWR MIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKL NIVNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGV G RTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVEYNQFGE TEVNLSELHPYLHNMKKRDPPSEPSPLEAEFQRLPSYRSWRTQHIGNQEENKSKNRNSNV I PYDYNRVPLKHELEMSKESEHDSDESSDDDSDSEEPSKYINASFIMSYWKPEVMIAAQGP L KETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQTYGDIEVDLKDTDKSSTY TLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQKNSSEGNKH HKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQ F LYDVIASTYPAQNGQVKKNNHQEDKIEFDNEVDKVKQDANCVNPLGAPEKLPEAKEQAE GSEPTSGTEGPEHSVNGPASPALNQGS SEQ ID NO 38: human CD45 extracellular domain QSPTPSPTGLTTAKMPSVPLSSDPLPTHTTAFSPASTFERENDFSETTTSLSPDNTSTQV SPDS LDNASAFNTTGVSSVQTPHLPTHADSQTPSAGTDTQTFSGSAANAKLNPTPGSNAISDVP G ERSTASTFPTDPVSPLTTTLSLAHHSSAALPARTSNTTITANTSDAYLNASETTTLSPSG SAVI STTTIATTPSKPTCDEKYANITVDYLYNKETKLFTAKLNVNENVECGNNTCTNNEVHNLT E CKNASVSISHNSCTAPDKTLILDVPPGVEKFQLHDCTQVEKADTTICLKWKNIETFTCDT Q NITYRFQCGNMIFDNKEIKLENLEPEHEYKCDSEILYNNHKFTNASKIIKTDFGSPGEPQ IIFC RSEAAHQGVITWNPPQRSFHNFTLCYIKETEKDCLNLDKNLIKYDLQNLKPYTKYVLSLH A YIIAKVQRNGSAAMCHFTTKSAPPSQVWNMTVSMTSDNSMHVKCRPPRDRNGPHERYHL EVEAGNTLVRNESHKNCDFRVKDLQYSTDYTFKAYFHNGDYPGEPFILHHSTSYNSK SEQ ID NO 39: C-terminus sequence for sortase conjugation GGGGSLPETGGWSHPQFEK SEQ ID NO 40: V5-CD45 FL with signal peptide MTMYLWLKLLAFGFAFLDTEVFVTGGKPIPNPLLGLDSTQSPTPSPTGLTTAKMPSVPLS S DPLPTHTTAFSPASTFERENDFSETTTSLSPDNTSTQVSPDSLDNASAFNTTGVSSVQTP HLP THADSQTPSAGTDTQTFSGSAANAKLNPTPGSNAISDVPGERSTASTFPTDPVSPLTTTL SL AHHSSAALPARTSNTTITANTSDAYLNASETTTLSPSGSAVISTTTIATTPSKPTCDEKY ANI TVDYLYNKETKLFTAKLNVNENVECGNNTCTNNEVHNLTECKNASVSISHNSCTAPDKTL ILDVPPGVEKFQLHDCTQVEKADTTICLKWKNIETFTCDTQNITYRFQCGNMIFDNKEIK LE NLEPEHEYKCDSEILYNNHKFTNASKIIKTDFGSPGEPQIIFCRSEAAHQGVITWNPPQR SFH NFTLCYIKETEKDCLNLDKNLIKYDLQNLKPYTKYVLSLHAYIIAKVQRNGSAAMCHFTT KSAPPSQVWNMTVSMTSDNSMHVKCRPPRDRNGPHERYHLEVEAGNTLVRNESHKNCD FRVKDLQYSTDYTFKAYFHNGDYPGEPFILHHSTSYNSKALIAFLAFLIIVTSIALLVVL YKI YDLHKKRSCNLDEQQE SEQ ID NO 41: V5-CD45Δ2 truncation mutant with signal peptide MTMYLWLKLLAFGFAFLDTEVFVTGGKPIPNPLLGLDSTSPGEPQIIFCRSEAAHQGVIT W NPPQRSFHNFTLCYIKETEKDCLNLDKNLIKYDLQNLKPYTKYVLSLHAYIIAKVQRNGS A AMCHFTTKSAPPSQVWNMTVSMTSDNSMHVKCRPPRDRNGPHERYHLEVEAGNTLVRN ESHKNCDFRVKDLQYSTDYTFKAYFHNGDYPGEPFILHHSTSYNSKALIAFLAFLIIVTS IAL LVVLYKIYDLHKKRSCNLDEQQE