Anti-CD45, monoclonal

CD45 is a family of single chain transmembraneous glycoproteins consisting of at least four isoforms which share a common large intracellular domain. Their extracellular domains are heavily glycosylated. The different isoforms are produced by alternative messenger RNA splicing of three exons of a single gene on chromosome 1. CD45 is expressed on cells of the human hematopoietic lineage (including hematopoietic stem cells) with the exception of mature red cells. It is not detected on differentiated cells of other tissues. It is likely that CD45 plays an important role in signal transduction, inhibition or upregulation of various immunological functions. Antibodies recognising a common epitope on all of the isoforms are termed CD45. Protein Function: Protein tyrosine-protein phosphatase required for T-cell activation through the antigen receptor (PubMed:35767951). Acts as a positive regulator of T-cell coactivation upon binding to DPP4. The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one. Upon T-cell activation, recruits and dephosphorylates SKAP1 and FYN. Dephosphorylates LYN, and thereby modulates LYN activity (By similarity). Interacts with CLEC10A at antigen presenting cell-T cell contact, CLEC10A on immature dendritic cells recognizes Tn antigen-carrying PTPRC/CD45 receptor on effector T cells and modulates T cell activation threshold to limit autoreactivity , (Microbial infection) Acts as a receptor for human cytomegalovirus protein UL11 and mediates binding of UL11 to T-cells, leading to reduced induction of tyrosine phosphorylation of multiple signaling proteins upon T-cell receptor stimulation and impaired T-cell proliferation [The Uniprot Consortium]