The PTPRC Antibody from MyBioSource.com is a Rabbit Polyclonal antibody. This antibody recognizes Human, Mouse, and Rat antigen. The PTPRC Antibody has been validated for the following applications: ELISA, Immunocytochemistry, Immunofluorescence, Immunohistochemistry, and Western Blot.
Description
Description: The protein phosphatase (PTP) receptor CD45 is a type I transmembrane protein comprised of a pair of intracellular tyrosine phosphatase domains and a variable extracellular domain generated by alternative splicing (1). The catalytic activity of CD45 is a function of the first phosphatase domain (D1) while the second phosphatase domain (D2) may interact with and stabilize the first domain, or recruit/bind substrates (2, 3). CD45 interacts directly with antigen receptor complex proteins or activates Src family kinases involved in the regulation of T-and B-cell antigen receptor signaling (1). Specifically, CD45 dephosphorylates Src-family kinases Lck and Fyn at their conserved negative regulatory carboxy-terminal tyrosine residues and upregulates kinase activity. Conversely, studies indicate that CD45 can also inhibit Lck and Fyn by dephosphorylating their positive regulatory autophosphorylation site. CD45 appears to be both a positive and a negative regulator that conducts signals depending on specific stimuli and cell type (1). Human leukocytes including lymphocytes, eosinophils, monocytes, basophils and neutrophils express CD45, while erythrocytes and platelets are negative for CD45 expression (4).
Function: Protein tyrosine-protein phosphatase required for T-cell activation through the antigen receptor. 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).
Subunit Structure: Binds GANAB and PRKCSH (By similarity). Interacts with SKAP1. Interacts with DPP4; the interaction is enhanced in a interleukin-12-dependent manner in activated lymphocytes. Interacts with human cytomegalovirus protein UL11.
Post-translational Modifications: Heavily N-and O-glycosylated.
Similarity: The first PTPase domain interacts with SKAP1. Belongs to the protein-tyrosine phosphatase family. Receptor class 1/6 subfamily