CD45.2 (104) Mouse mAb (violetFluor^™ 500 Conjugate) #95440

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).
Murine CD45 glycoproteins have three alleles (Ly5a, Ly5b, and Ly5c) that have been categorized in inbred mice. Ly6a and Ly6b, also referred to as CD45.1 and CD45.2, respectively, can be distinguished based on reactivity with specific monoclonal antibodies. Common mouse strains including BALB/c, C57BL, CBA/J, and NZB/BLNJ express CD45.2 where SJL/J mice express CD45.1 (5).