Stressgen, BioMol, Alexis Corporation, Assay Designs, Alexis

抗体

[pSer9]GSK-3β单克隆抗体(3A8)

ADI-905-761-100

100微克

单克隆

小鼠

未共轭

磷酸化

3A8

人类, 小鼠, 大鼠, 犬

免疫印迹, 酶联免疫吸附测定

ADI-905-761-100

[pSer9]GSK-3β单克隆抗体(3A8)

小鼠

单克隆

磷酸化

抗体

100微克

3A8

IgG1

人类, 小鼠, 大鼠, 狗

Glycogen Synthase Kinase 3β (GSK-3β) is a unique serine/threonine kinase that is inactivated by phosphorylation. In response to insulin binding, PKB/AKT phosphorylates GSK-3β on serine 9, which prevents GSK-3β from phosphorylating glycogen synthase. Unphosphorylated glycogen synthase is active and able to synthesize glycogen. GSK-3β is also unique in that it requires a substrate that has been phosphorylated by a distinct kinase before it can phosphorylate the substrate. This phosphate priming mechanism explains why phosphorylation of serine 9 inactivates GSK-3β. The phosphorylated serine binds to the GSK-3β priming phosphate position and prevents binding of alternative substrates. In addition to insulin signaling, GSK-3β participates in the Wnt signaling pathway, where it forms a complex with axin, beta-catenin and adenomatous polyposis coli (APC) protein. In the presence of Wnts, GSK-3β is unable to phosphorylate beta-catenin, which leads to stabilization of beta-catenin. The Wnt pathway inactivates GSK-3β via the proteins, Dishevelled and FRAT, which disrupt the interaction of GSK-3β with axin, beta-catenin, and APC. Clinically, there is considerable interest in GSK-3β inhibitors because they may mimic the effect of insulin or reduce the hyperphosphorylation of Tau that is observed in Alzheimer's Disease.

糖原合酶激酶3β

Synthetic peptide corresponding to a portion of GSK-3β phosphorylated at Ser9.

Lyophilized from 1ml of 2x PBS containing 0.09% sodium azide, PEG, and sucrose.

酶联免疫吸附测定, 免疫印迹

-20°C