Cd45 Mouse, Unlabeled, Clone: 69, Bd, Mouse Monoclonal Antibody, Each

Details:

Cd45 (also known as leukocyte common antigen, gp180, or t200) is found on all hematopoietic cells except those of red cell origin. The n-terminal domain is a large glycosylated extracellular region of variable length (390-542 amino acids) derived by the alternative splicing of at least three exons (4, 5, or 6). This variation accounts for the different isoforms of cd45 (180-220 kda). The remainder of the molecule includes a short transmembrane region followed by a large highly conserved cytoplasmic domain of 702 residues. The cd45 cytoplasmic domain possesses an intrinsic protein tyrosine phosphatase (ptpase) activity. This region contains two ptpase domains (domains i and ii) which share 40% homology. Both domains are required for optimal ptpase activity and show significant homology with other receptor-like and cytoplasmic ptpases. Cd45 plays a critical role in antigen receptor-induced responses of t and b cells. In b cells, cd45 can exist as part of a larger multisubunit complex composed of several tyrosine phosphorylated proteins, including the src-family ptk, lyn, or it can exist as the membrane immunoglobulin-associated mb-1/b29 heterodimer. In t cells, cd45 associates with and dephosphorylates both lck and fyn. In addition, cd45 can associate with membrane proteins involved in t cell activation, such as cd2, thy-1, tcr, and cd26.