epitope corresponding to amino acids 171-257 mapping within an internal region of Lsk of human origin
recommended for detection of Lsk of human origin and Ctk of mouse and rat origin by WB, IP, IF and ELISA; also reactive with additional species, including equine, canine, bovine and porcine
Lsk Background Information All members of the Src gene family of tyrosine kinases are characterized by a carboxy terminal domain tyrosine, Y527 in the case of Src p60, which is highly phosphorylated in the inactive form of the enzyme, while phosphorylated to a much lesser extent when the enzyme is active. For instance, a mutant 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 the carboxy terminal regulatory sequences. Csk phosphorylates Src on Y527 and also down regulates Lyn, Fyn and Lck by tyrosine phosphorylation of carboxy terminal regulatory sites. A Csk-like protein-tyrosine kinase of mouse origin (Ctk), also designated Ntk, and its human homolog, Lsk, have also been described.
