Clone REA407 recognizes the human focal adhesion kinase (FAK) antigen phosphorylated at serine 910 (pS910). FAK is a 125 kDa non-receptor and non-membrane cytoplasmic tyrosine kinase that plays critical roles in integrin-mediated signal transductions and also participates in signaling by other cell surface receptors. In integrin-mediated cell adhesion, FAK is activated via disruption of an auto-inhibitory intra-molecular interaction between its amino terminal FERM domain and the central kinase domain. The activated FAK forms a complex with Src family kinases, which initiates multiple downstream signaling pathways through phosphorylation of other proteins to regulate different cellular functions. Those signaling pathways are identified to mediate FAK regulation of migration of various normal and cancer cells. Serine 910 (pS910) is a prominent site differentially phosphorylated in response to neurotransmitters, bioactive lipids, tumor promoters, and growth factors in intestinal epithelial cells.
Additional information: Clone REA407 displays negligible binding to Fc receptors.
PTK2, FADK, FAK1, FRNK, PPP1R71, p125FAK, pp125FAK, FADK 1