Recombinant Mouse Glycogenin 1 + GYS1 protein (Tagged)
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Recombinant Mouse Glycogenin 1 + GYS1 protein (Tagged) is a Mouse Full Length protein, in the 1 to 738 aa range, expressed in Baculovirus infected Sf9 cells, with >68%, suitable for SDS-PAGE.
View Alternative Names
Gyg, Gyg1, Glycogenin-1, GN-1, GN1
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Mouse Glycogenin 1 + GYS1 protein (Tagged) (AB271531)
SDS-PAGE analysis of 4 μg ab271531.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
GYS1 functions as the primary enzyme responsible for glycogen synthesis within cells. This enzyme operates in a complex with glycogenin which serves as the primer necessary for glycogen biosynthesis initiation. The association ensures the formation of a glycogen molecule by elongating the glucose chain. Through this mechanism GYS1 enables the formation of substantial glycogen reserves essential for energy demand particularly in cells with high energy needs like muscle cells.
Pathways
The function of GYS1 integrates into the glycogenesis pathway allowing cells to effectively store glucose as glycogen. As part of this pathway GYS1 works alongside glycogen phosphorylase which breaks down glycogen during times of energy need. GYS1 activity is regulated by insulin signaling highlighting its connection to the the insulin signaling pathway which controls glucose metabolism. This regulation allows the cell to maintain energy homeostasis linking GYS1 to broader metabolic pathways.
Specifications
Form
Liquid
Additional notes
Affinity purified.
General info
Function
Glycogenin participates in the glycogen biosynthetic process along with glycogen synthase and glycogen branching enzyme. It catalyzes the formation of a short alpha (1,4)-glucosyl chain covalently attached via a glucose 1-O-tyrosyl linkage to internal tyrosine residues and these chains act as primers for the elongation reaction catalyzed by glycogen synthase.
Sequence similarities
Belongs to the glycosyltransferase 8 family. Glycogenin subfamily.
Post-translational modifications
Self-glycosylated by the transfer of glucose residues from UDP-glucose to itself, forming an alpha-1,4-glycan of around 10 residues attached to Tyr-195.. Phosphorylated.
Target data
Additional targets
Product promise
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