Recombinant Human Glycogen synthase 1/GYS1 protein
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Recombinant Human Glycogen synthase 1/GYS1 protein is a Human Full Length protein, in the 1 to 737 aa range, expressed in Wheat germ, suitable for ELISA, WB.
View Alternative Names
GYS, GYS1, Glycogen synthase 1
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human Glycogen synthase 1/GYS1 protein (AB158615)
ab158615 on a 12.5% SDS-PAGE stained with Coomassie Blue.
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
This enzyme plays a critical role in the energy storage mechanism of muscle tissues. GYS1 functions as a part of the glycogen synthase complex interacting with various glycogen-associated proteins to modulate its activity. These interactions control the enzyme's affinity for its substrate and its susceptibility to regulatory signals like phosphorylation affecting glycogen synthesis efficiency. Through its activity GYS1 ensures a readily available reserve of glucose in muscle tissues for rapid energy production when required.
Pathways
Glycogen synthase 1 is a central component of the glycogen metabolism pathway. It acts alongside other enzymes such as glycogen phosphorylase which catalyzes glycogen breakdown. The balance between GYS1 and glycogen phosphorylase determines the rate of glycogen turnover within cells. GYS1 is further regulated by the insulin signaling pathway where insulin promotes glycogen synthesis by altering GYS1 activity alongside proteins like AKT influencing glucose homeostasis and energy management in tissues.
Specifications
Form
Liquid
General info
Function
Glycogen synthase participates in the glycogen biosynthetic process along with glycogenin and glycogen branching enzyme. Extends the primer composed of a few glucose units formed by glycogenin by adding new glucose units to it. In this context, glycogen synthase transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan.
Sequence similarities
Belongs to the glycosyltransferase 3 family.
Post-translational modifications
Phosphorylation at Ser-8 by AMPK inactivates the enzyme activity. Primed phosphorylation at Ser-657 (site 5) by CSNK2A1 and CSNK2A2 is required for inhibitory phosphorylation at Ser-641 (site 3a), Ser-645 (site 3b), Ser-649 (site 3c) and Ser-653 (site 4) by GSK3A an GSK3B (By similarity). Phosphorylated at Ser-641 by DYRK2, leading to inactivation (By similarity). Phosphorylated at Ser-641 by PASK, leading to inactivation; phosphorylation by PASK is inhibited by glycogen. Dephosphorylation at Ser-641 and Ser-645 by PP1 activates the enzyme (PubMed:35835870).
Target data
Product promise
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