Anti-phospho Gab2 (p-Ser 210) Antibody

Grb2-associated binder (Gab) proteins serve as docking proteins, recruiting SH2 domain-containing effectors and relaying signals to downstream signalling pathways from receptor tyrosine kinases (RTKs) such as growth factor, cytokine and antigen receptors. There are three mammalian Gab proteins, Gab1-3. These all contain Grb2 SH3 domain-binding sites and multiple tyrosine phosphorylation sites. Following tyrosine phosphorylation, Gab proteins recruit the tyrosine phosphatase SHP2 and the p85 subunit of pI3K, resulting in potentiation of the Ras/Erk and PI3K/Akt pathways.

Gab proteins are also subject to negative regulation. It has recently been demonstrated that growth factor-induced phosphorylation of Gab2 on Ser210 and Thr391 leads to the recruitment of 14-3-3 proteins which promotes dissociation of Gab2 from Grb2. Gab2 is thus uncoupled from the receptor complex, resulting in termination of Gab2 signalling (1). This regulatory mechanism is unique to Gab2.