The serine/threonine kinase Akt family contains several members, including Akt1 (also designated PKBα or RacPK), Akt2 (also designated PKB-β or RacPK-β) and Akt3 (also designated PKB-γ or thyoma viral proto-oncogene 3). Akt1 and Akt2 are activated by PDGF stimulation. This activation is dependent on PDGFR-β tyrosine residues 740 and 751, which bind the 85 kDa subunit of the phosphatidylinositol 3-kinase (PI 3-kinase) complex. Activation of Akt1 by insulin or insulin-growth factor-1 (IGF-1) results in phosphorylation of both Thr 308 and Ser 473. Phosphorylation of both residues is important to generate a high level of Akt1 activity, and the phosphorylation of Thr 308 is not dependent on phosphorylation of Ser 473 in vivo. Thus, Akt proteins become phosphorylated and activated in insulin/IGF-1- stimulated cells by an upstream kinase(s). The activation of Akt1 and Akt2 is inhibited by the PI kinase inhibitor wortmannin. Taken together, this data strongly suggests that the protein signals downstream of the PI kinases.，官网链接：https://www.sigmaaldrich.cn/product/mm/04736 默克 科研、开发、生产。 作为生命科学行业的全球领先供应商，我们致力于为科研、生物技术开发和生产，以及制药药物疗法开发和生产提供各类解决方案和服务。

非质量问题不退不换