Anti-CSK Purified Monoclonal Antibody

C-terminal Src kinase (Csk) is a non-receptor protein tyrosine kinase which resembles Src-family kinases, but unlike them it lacks the conserved autophosphorylation site, the regulatory C-terminal tyrosine as well as myristylation and palmitylation. Csk negatively regulates Src-family kinases by phosphorylation of their C-terminal regulatory tyrosine. Disruption of the csk gene causes constitutive activation of Src-family kinases, and overexpression of Csk usually counteracts their signaling. The Csk-mediated regulation of those Src-family kinases, that are localized in lipid rafts, is enabled by a ubiquitously expressed transmembrane adaptor PAG (also known as Cbp, Csk-binding protein), which recruits Csk.

Bacterially expressed recombinant fragment of human Csk corresponding to aa 330-450. The mouse monoclonal antibody CSK-04 reacts with Csk (C-terminal Src kinase), a 50 kDa intracellular non-receptor protein tyrosine kinase.

Non-receptor tyrosine-protein kinase that plays an important role in the regulation of cell growth, differentiation, migration and immune response. Phosphorylates tyrosine residues located in the C-terminal tails of Src-family kinases (SFKs) including LCK, SRC, HCK, FYN, LYN, CSK or YES1. Upon tail phosphorylation, Src-family members engage in intramolecular interactions between the phosphotyrosine tail and the SH2 domain that result in an inactive conformation. To inhibit SFKs, CSK is recruited to the plasma membrane via binding to transmembrane proteins or adapter proteins located near the plasma membrane. Suppresses signaling by various surface receptors, including T- cell receptor (TCR) and B-cell receptor (BCR) by phosphorylating and maintaining inactive several positive effectors such as FYN or LCK.