epitope corresponding to amino acids 1-75 mapping at the N-terminus of Csk p50 of human origin
recommended for detection of Csk p50 of mouse, rat and human origin by WB, IP, IF and ELISA; also reactive with additional species, including canine, bovine, porcine and avian
Csk Background Information All members of the Src gene family of tyrosine kinases are characterized by a carboxy terminal domain tyrosine which is highly phosphorylated in the inactive form of the enzyme and phosphorylated to a much lesser extent when the enzyme is active. In the case of Src p60, Y527 is this tyrosine; however, a mutant form of c-Src in which Y527 is replaced by phenylalanine is transforming and displays 5- to 10-fold elevated kinase activity compared to its normal counterpart. Csk has been identified as a Src-related tyrosine kinase having both SH2 and SH3 domains and a catalytic domain but lacking sequences amino terminal to the SH3 domain as well as carboxy terminal regulatory sequences. Csk phosphorylates Src on Y527 and also downregulates Lyn, Fyn and Lck by tyrosine phosphorylation of carboxy terminal regulatory sites.
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Csk (H-75)
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Csk (H-75): sc-13074. Western blot analysis of Csk expression in non-transfected 293T: sc-117752 (A), human Csk transfected 293T: sc-111742 (B) and Jurkat (C) whole cell lysates.
Csk (H-75): sc-13074. Western blot analysis of Csk expression in non-transfected 293T: sc-117752 (A), mouse Csk transfected 293T: sc-119481 (B) and Jurkat (C) whole cell lysates.