Src Antibody Sampler Kit #9935
Product Information
Kit Usage Information
Protocols
Product Description
Specificity / Sensitivity
Each antibody in the kit detects endogenous levels of Src only when in the indicated phosphorylation state at the indicated residue. The antibodies may cross-react with other Src family members when in equivalent phosphorylation states.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with synthetic phospho- or non-phosphopeptides corresponding to residues surrounding Tyr527 of human Src protein. The mouse monoclonal antibody is produced by immunizing animals with a synthetic non-phosphopeptide corresponding to residues surrounding Tyr416 of human Src protein. The rabbit monoclonal antibody for P-Src Y416 is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr416 of human Src protein. The Src (32G6) rabbit monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the amino-terminus of human Src. Polyclonal antibodies are purified by protein A and peptide affinity chromatography.
Background
The Src family of protein tyrosine kinases, which includes Src, Lyn, Fyn, Yes, Lck, Blk, and Hck, are important in the regulation of growth and differentiation of eukaryotic cells (1). Src activity is regulated by tyrosine phosphorylation at two sites, but with opposing effects. While phosphorylation at Tyr416 in the activation loop of the kinase domain upregulates enzyme activity, phosphorylation at Tyr527 in the carboxy-terminal tail by Csk renders the enzyme less active (2).
Lyn is a member of the Src family that is predominantly expressed in hematopoietic cells (3). Lyn participates in signaling from multiple cell surface receptors such as the B cell Ag receptor (BCR) and CD40 (4).
Lck is essential for T-lymphocyte activation and differentiation (5,6). The activity of Lck is regulated by protein kinases and phosphatases. Phosphorylation of the C-terminal tyrosine 505 serves to downregulate Lck catalytic activity, while phosphorylation at tyrosine 394 leads to an increase in Lck activity (7).
- Thomas, S.M. and Brugge, J.S. (1997) Annu Rev Cell Dev Biol 13, 513-609.
- Hunter, T. (1987) Cell 49, 1-4.
- Yamanashi, Y. et al. (1989) Proc Natl Acad Sci U S A 86, 6538-42.
- Yamanashi, Y. et al. (1991) Science 251, 192-4.
- Molina, T.J. et al. (1992) Nature 357, 161-4.
- Straus, D.B. and Weiss, A. (1992) Cell 70, 585-93.
- Chow, L.M. et al. (1993) Nature 365, 156-60.
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