Src Family, Negative Regulatory Tyrosine Phosphorylation Site

The Src family of non-receptor tyrosine kinases is involved in the modulation of a wide variety of normal and pathogenic cellular processes including growth, development, differentiation and carcinogenesis. These proteins contain a consensus structure comprised of one or more N-terminal SH2 and/or SH3 domains involved in protein-protein interactions, a central catalytic tyrosine kinase domain and a short C-terminal domain. This C-terminal domain contains a tyrosine residue that, when phosphorylated by Csk tyrosine kinase, functions as a negative regulatory site (tyrosines 530, 531, 522, 505 and 508 in Src, Fyn, Hck, Lck and Lyn, respectively) by providing a binding site for the N-terminal SH2 domain. The association of these two domains blocks access to a\ncritical tyrosine residue in the activation loop, the phosphorylation of which is required for enzyme activation. When the C-terminal domain tyrosine residue is dephosphorylated, the catalytic domain tyrosine can be maximally phosphorylated leading to full kinase activation.\n\nApplications: \nSuitable for use in Western Blot. Other applications not tested.\n\nRecommended Dilution:\nOptimal dilutions to be determined by the researcher.\n\nPositive Control: \nPC12 cells +/- sorbitol, Chick Embryofibronectin and recombinant activated Fyn, Lck and Lyn proteins\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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SPECIFICATIONS

Catalog Number

S6504-27

Size

10 Blots

Applications

WB

Hosts

Rabbit

Reactivities

Hum

Form

Supplied as a liquid in PBS (without Mg2+ and Ca2+), 1mg/ml BSA (IgG, protease free), pH 7.2, 0.05% sodium azide.

P Type

Pab

Purity

Purified by immunoaffinity chromatography.

References

1. Yasuda, K., et al. (2002) Fyn is essential for tyrosine phosphorylation of Csk-binding\nprotein/phosphoprotein associated with glycolipid-enriched microdomains in lipid rafts in resting T\ncells. J. Immunol. 169(6):2813-2817. 2. Young, M.A., et al. (2001) Dynamic coupling between the SH2 and SH3 domains of c-Src and Hck underlies their inactivation by C-terminal tyrosine phosphorylation. Cell 105(1):115-126. 3. Hubbard, S.R., and J.H. Till (2000) Protein tyrosine kinase structure and function. Ann. Rev. Biochem. 69:373-398. 4. Egan, C., et al. (1999) Activation of Src in human breast tumor cell lines: elevated levels of phosphotyrosine phosphatase activity that preferentially recognizes the Src carboxy terminal negative regulatory tyrosine 530. Oncogene 18(5):1227-1237. 5. Thomas, S.M. and J.S. Brugge (1997) Cellular functions regulated by Src family kinases. Ann. Rev. Cell Devel. Biol. 13:513-609.

Additional Info

Recognizes human Src kinase family members (Src, Fyn, Lck, Lyn, and Hck). Species sequence homology: mouse and rat, and also among other members of the Src protein family.\n