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Focal adhesion kinase (FAK) is a non receptor protein tyrosine kinase discovered as a substrate for Src and a key element in integrin signaling. FAK plays a central role in cell spreading, differentiation, migration, cell death and acceleration of the G1 to S phase transition of the cell cycle. FAK regulation includes phosphorylation at multiple tyrosine and serine residues. Phosphorylation of tyrosine is generally associated with positive regulation and growth promotion; however, dephosphorylation at these sites occurs as cells enter mitosis (M-Phase). In contrast, serine phosphorylation either remains high or is increased as cells enter mitosis and may play a role in focal adhesion disassembly. FAK and its phosphorylation states have been implicated in cancer metastasis, tumor cell survival, and adhesion-independent growth. Recent evidence indicates that elevation of FAK activity in human carcinoma cells is associated with increased invasive potential. A central role in tumor formation and progression suggests that FAK is an attractive target for therapeutic intervention. Activation of FAK by integrin clustering leads to autophosphorylation at Tyr397.,官网链接:https://www.sigmaaldrich.cn/product/mm/abt135
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