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OPA1-03885 detects phospho-FAK (pSer732) from mouse and rat samples. This antibody is expected to cross-react with human, chicken, and frog phospho-FAK due to sequence homology.
OPA1-03885 has been successfully used in Western blot procedures. By Western blot, this antibody detects an ~125 kDa protein representing phospho-FAK (pSer732).
Store at 4°C for up to one week. For long-term storage, aliquot and store at -20°C. Centrifuge before opening.
The OPA1-03885 immunizing phosphopeptide is derived from the region of FAK that contains serine 732.
Focal Adhesion Kinase (FAK) is a 125 kDa non-receptor protein tyrosine kinase that acts as a substrate for Src and is a key element of integrin signaling. FAK plays an important role in cell spreading, differentiation, migration, cell death, and acceleration of the G1 to S phase transition of the cell cycle. FAK has a central catalytic domain and a C-terminal tail that localizes it to focal adhesions, which are sites where cells attach to the extracellular matrix via surface integrin receptors. Increased FAK tyrosine phosphorylation occurs upon integrin engagement with fibronectin. Adhesion of murine NIH3T3 fibroblasts to fibronectin promotes association of the Grb2 adapter protein and c-Src PTK with FAK in vivo, and also results in activation of the ERK2 MAP kinase. In v-Src-transformed NIH3T3, the association of v-Src, Grb2, and Sos with FAK is independent of cell adhesion to fibronectin. In vitro the Grb2 SH2 domain binds directly to tyrosine-phosphorylated FAK, and the binding site has been identified as Tyr925 by site directed mutagenesis. Several transcript variants encoding different isoforms have been found for the FAK gene, but the full-length natures of only three of them have been determined.
仅用于科研。不用于诊断过程。未经明确授权不得转售。