ANTI-PYK2/CAK? CLONE 74 25 MIG

Protein-tyrosine kinase 2beta (UniProt: P70600; also known as EC:2.7.10.2, Calcium-dependent tyrosine kinase, CADTK, Calcium-regulated non-receptor proline-rich tyrosine kinase, Cell adhesion kinase beta, CAK-beta, CAKB, Focal adhesion kinase 2, FADK 2, Proline-rich tyrosine kinase 2, Pyk2) is encoded by the Ptk2b (also known as Pak2, Pyk2) gene (Gene ID: 50646) in rat. Pky2 is a non-receptor protein-tyrosine kinase that regulates reorganization of the actin cytoskeleton, cell polarization, cell migration, adhesion, spreading, and bone remodeling. Its protein kinase domain is localized in amino acids 425-683. Pyk2 plays a role in the regulation of the humoral immune response and is required for normal levels of marginal B-cells in the spleen and normal migration of splenic B-cells. It is highly expressed in pulmonary vein endothelial cells, lung, and brain. It localizes to the cytoplasmic side of the membrane. Pyk2 is activated by phosphorylation of tyrosine residues in response to various stimuli that elevate intracellular calcium levels. Tyr402 is the major autophosphorylation site, but it can also be phosphorylated by other kinases. This phosphorylation promotes interaction with Src and Src family members, leading to phosphorylations at Tyr579, Tyr580, and Tyr881. Phosphorylation at Tyr402, Tyr579 and Tyr580 is required for its optimal kinase activity and phosphorylation at Tyr881 is essential for its interaction with Grb2.