epitope corresponding to phosphorylated Tyr 627 of Gab 1 of human origin
recommended for detection of Tyr 627 phosphorylated Gab 1 of human and rat origin and correspondingly phosphorylated Tyr 628 of mouse origin by WB and IP
p-Gab 1 Background Information The insulin receptor substrate (IRS) family of proteins mediate a variety of intracellular signaling pathways by serving as signaling platforms downstream of several receptor tyrosine kinases, including the insulin and insulin-like growth factor (IGF-1) receptors. Gab 1 (Grb2-associated binder, one such member of the IRS family, plays an important role in cellular growth response, transformation and apoptosis . Gab 1 is a multi-substrate docking protein that functions downstream in the signaling pathways of different receptor kinases, including EGFR. Gab1 is tyrosine phosphorylated normally in response to insulin and consequently, enhances phosphatidylinositol 3-kinase (PI3K) binding. In response to osmotic shock, tyrosine-phosphorylated Gab 1 (p-Gab 1) also binds and activates phosphatidylinositol 3-kinase (PI3K), suggesting that Gab 1 is the major site for PI3K recruitment following osmotic shock stimulation. In the Flt3 ligand-responsive cells, Gab 1 is also rapidly tyrosine phosphorylated after receptor tyrosine kinase Flt3 ligand simulation and interacts with tyrosine-phosphorylated Shp-2, p85, Grb2 and Shc proteins.
p-Gab 1 (Tyr 627)
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p-Gab 1 (Tyr 627): sc-101685. Western blot analysis of phosphorylated Gab 1 expression in untreated (A) and EGF-treated (B) HUVEC whole cell lysates.