GSK-3 beta Protein, Mouse (Active, sf9, His)

GSK-3 beta protein, a constitutively active kinase, serves as a negative regulator in the hormonal control of glucose homeostasis, Wnt signaling, and the regulation of transcription factors and microtubules. It achieves this by phosphorylating and inactivating key substrates such as glycogen synthase (GYS1 or GYS2), EIF2B, CTNNB1/beta-catenin, APC, AXIN1, DPYSL2/CRMP2, JUN, NFATC1/NFATC, MAPT/TAU, and MACF1. Primed phosphorylation is a prerequisite for the majority of its substrates. In skeletal muscle, GSK-3 beta contributes to insulin regulation of glycogen synthesis by inhibiting GYS1 activity. It may also mediate insulin resistance by regulating activation of transcription factors. Additionally, GSK-3 beta plays a role in protein synthesis by controlling the activity of initiation factor 2B (EIF2BE/EIF2B5). In Wnt signaling, it forms a multimeric complex with APC, AXIN1, and CTNNB1/beta-catenin, phosphorylating CTNNB1 and targeting it for degradation via ubiquitin/proteasomes. GSK-3 beta is involved in various cellular processes, including regulating replication in pancreatic beta-cells, influencing apoptosis, participating in ERBB2-dependent stabilization of microtubules, and controlling cell polarity and axon outgrowth. It also plays a role in the circadian clock regulation, autophagy, and the negative regulation of the extrinsic apoptotic signaling pathway. Moreover, GSK-3 beta phosphorylates several proteins, including E2F1, FXR1, and interleukin-22 receptor subunit IL22RA1, affecting their stability and function.