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Glycogen synthase kinase 3 (GSK-3) inhibitors act on GSK-3α and GSK-3β, two constitutively active kinases. The serine/threonine kinase was separated in 1980 from rabbit skeletal muscle as a kinase that phosphorylates glycogen synthase. In 1995 insulin was shown to inhibit GSK-3 through protein kinase B (PKB), also known as Akt. GSK-3 also phosphorylates β-catenin and marks it for degradation, so its inhibition activates canonical Wnt signaling. In 2008 laduviglusib, also called CHIR-99021, was combined with a second kinase inhibitor to keep mouse embryonic stem cells in a ground state of self-renewal. SB 216763, TWS119, tideglusib and AR-A 014418 are further GSK-3 inhibitors for Wnt, neuronal and metabolic studies.
2B-(SP) is an eIF2B-based substrate specifically designed for glycogen synthase kinase-3 (GSK-3). It exhibits efficient phosphorylation by both GSK-3α and GSK-3β isoforms, making it a valuable tool for studying GSK-3-related signaling pathways and cellular processes. This compound is suitable for research applications involving protein phosphorylation and GSK-3 activity modulation.
Phospho-Glycogen Synthase Peptide-2 is a specific substrate for glycogen synthase kinase-3 (GSK-3). This peptide facilitates the study of GSK-3 activity and its role in various signaling pathways. It is also suitable for affinity purification of protein-serine kinases, enabling researchers to investigate kinase interactions and functions in cellular processes.
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