Phospho-Lck (Tyr505) AntibodyProduct information
Product Pathways - Lymphocyte Signaling
Phospho-Lck (Tyr505) Antibody #2751
|2751S||100 µl (10 western blots)||---||In Stock||---|
|2751T||20 µl (2 western blots)||---||In Stock||---|
|2751||carrier free and custom formulation / quantity||email request|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IP=Immunoprecipitation
Specificity / Sensitivity
Phospho-Lck (Tyr505) Antibody detects endogenous levels of Lck only when phosphorylated at Tyr505. This antibody may cross-react with certain phosphorylated Src family members due to high sequence homology.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr505 of human Lck. Antibodies are purified by protein A and peptide affinity chromatography.
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).
Lck is essential for T-lymphocyte activation and differentiation (3,4). Phosphorylation of Tyr505 in the carboxy-terminal tail of Lck downregulates its catalytic activity, while phosphorylation of Tyr394 leads to an increase in Lck activity (5).
- Thomas, S.M. and Brugge, J.S. (1997) Annu Rev Cell Dev Biol 13, 513-609.
- Hunter, T. (1987) Cell 49, 1-4.
- Molina, T. J. et al. (1992) Nature 357, 161-164.
- Straus, D. B. et al. (1992) Cell 70, 585-593.
- Chow, L. M. et al. (1993) Nature 365, 156-160.
- Harr, M.W. et al. (2010) Cell Death Differ 17, 1381-91. Applications: Western Blotting.
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This product is intended for research purposes only. The product is not intended to be used for therapeutic or diagnostic purposes in humans or animals.
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