p-Shc Antibody (15E11): sc-81518

p-Shc Antibody (15E11) is a mouse monoclonal IgG1 antibody that detects p-Shc in mouse, rat, human, and canine samples through applications such as western blotting (WB), immunoprecipitation (IP), and immunofluorescence (IF). p-Shc is a critical adaptor protein involved in various signaling pathways, particularly those activated by growth factor receptors with tyrosine kinase activity. p-Shc facilitates signal transmission from these receptors to downstream effectors, such as the Ras/MAPK pathway, which is essential for regulating cell proliferation, differentiation, and survival. Phosphorylation of specific tyrosine residues on p-Shc, particularly Tyr 239 and Tyr 317, is crucial for interaction with the Grb2-Sos complex, thereby promoting Ras activation. This interaction mediates cellular responses to growth factors like insulin and epidermal growth factor (EGF), highlighting p-Shc′s importance in processes such as insulin-induced mitogenesis. The human Shc gene is located on chromosome 1q21.3, and widespread expression underscores significance in various physiological and pathological contexts. Anti-p-Shc antibody (15E11) provides valuable insights into signaling pathway dynamics for researchers studying cellular responses to growth factors and their implications in health and disease.

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p-Shc Antibody (15E11) References:

1. The p66shc adaptor protein controls oxidative stress response and life span in mammals.  |  Migliaccio, E., et al. 1999. Nature. 402: 309-13. PMID: 10580504
2. The shc adaptor protein forms interdependent phosphotyrosine-mediated protein complexes in mast cells stimulated with interleukin 3.  |  Velazquez, L., et al. 2000. Blood. 96: 132-8. PMID: 10891441
3. The functional significance of Shc in insulin signaling as a substrate of the insulin receptor.  |  Sasaoka, T. and Kobayashi, M. 2000. Endocr J. 47: 373-81. PMID: 11075717
4. Shc proteins are phosphorylated and regulated by the v-Src and v-Fps protein-tyrosine kinases.  |  McGlade, J., et al. 1992. Proc Natl Acad Sci U S A. 89: 8869-73. PMID: 1409579
5. A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction.  |  Pelicci, G., et al. 1992. Cell. 70: 93-104. PMID: 1623525
6. Phospho-Tyrosine(s) vs. Phosphatidylinositol Binding in Shc Mediated Integrin Signaling.  |  Lin, X. and Vinogradova, O. 2015. Am J Mol Biol. 5: 17-31. PMID: 25893141
7. The Shc adaptor protein is highly phosphorylated at conserved, twin tyrosine residues (Y239/240) that mediate protein-protein interactions.  |  van der Geer, P., et al. 1996. Curr Biol. 6: 1435-44. PMID: 8939605
8. Tyrosine phosphorylation sites at amino acids 239 and 240 of Shc are involved in epidermal growth factor-induced mitogenic signaling that is distinct from Ras/mitogen-activated protein kinase activation.  |  Gotoh, N., et al. 1997. Mol Cell Biol. 17: 1824-31. PMID: 9121430
9. Relative involvement of Shc tyrosine 239/240 and tyrosine 317 on insulin induced mitogenic signaling in rat1 fibroblasts expressing insulin receptors.  |  Ishihara, H., et al. 1998. Biochem Biophys Res Commun. 252: 139-44. PMID: 9813159
10. Gads is a novel SH2 and SH3 domain-containing adaptor protein that binds to tyrosine-phosphorylated Shc.  |  Liu, SK. and McGlade, CJ. 1998. Oncogene. 17: 3073-82. PMID: 9872323

The preferred Shc antibody is Shc Antibody (PG-797): sc-967.