Anti-phospho-PI 3 Kinase p85 alpha (Tyr607)

This affinity purified antibody is directed against the phosphorylated form of human PIK3R1 protein at the pY607 residue.  This product was affinity purified from monospecific antiserum by immunoaffinity purification.  The product was affinity purified from monospecific antiserum by immunoaffinity purification. Antiserum was first purified against the phosphorylated form of the immunizing peptide. The resultant affinity purified antibody was then cross adsorbed against the non-phosphorylated form of the immunizing peptide. Reactivity with non-phosphorylated human PIK3R1 Y607 is minimal by ELISA and dot blot. Reactivity against homologues from other sources is not known. A BLAST analysis was used to suggest reactivity with the antigen based on 100% homology with the immunizing sequence to human, mouse, and rat. Protein function: Binds to activated (phosphorylated) protein-Tyr kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Necessary for the insulin-stimulated increase in glucose uptake and glycogen synthesis in insulin-sensitive tissues. Plays an important role in signaling in response to FGFR1, FGFR2, FGFR3, FGFR4, KITLG/SCF, KIT, PDGFRA and PDGFRB. Likewise, plays a role in ITGB2 signaling (PubMed:17626883, PubMed:19805105, PubMed:7518429). Modulates the cellular response to ER stress by promoting nuclear translocation of XBP1 isoform 2 in a ER stress- and/or insulin-dependent manner during metabolic overloading in the liver and hence plays a role in glucose tolerance improvement (PubMed:20348923). [The UniProt Consortium]