Recombinant Human Glycogenin 1 + Glycogen synthase 2 protein (Tagged)
Be the first to review this product! Submit a review
|
(0 Publication)
Recombinant Human Glycogenin 1 + Glycogen synthase 2 protein (Tagged) is a Human Full Length protein, in the 1 to 350 aa range, expressed in Baculovirus infected Sf9 cells, with >69%, suitable for SDS-PAGE.
View Alternative Names
Glycogen synthase 2, GYS2
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human Glycogenin 1 + Glycogen synthase 2 protein (Tagged) (AB271532)
SDS-PAGE analysis of 3.6 μg ab271532.
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
Glycogenin 1 and glycogen synthase 2 play significant roles in glycogen metabolism. Glycogenin 1 starts glycogen synthesis by adding glucose units to itself forming the core structure of glycogen granules. Meanwhile glycogen synthase 2 extends the alpha-14-glucosidic links further enlarging the glycogen molecules. Both are integral to glycogenesis the process of converting glucose into glycogen for storage. These proteins often function in a complex with other enzymes and regulatory proteins ensuring that glycogen synthesis occurs efficiently.
Pathways
Both glycogenin 1 and glycogen synthase 2 are central in glycogen biosynthesis and storage pathways. Glycogen metabolism tightly regulates glucose homeostasis in response to hormonal signals and energy needs. Glycogen phosphorylase an enzyme that breaks down glycogen is influenced by these pathways. Glycogen synthase and glycogenin interact with regulatory kinases and phosphatases which modify their activity in response to signals therefore fine-tuning glycogen levels in cells.
Specifications
Form
Liquid
Additional notes
Affinity purified.
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
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. Dephosphorylation at Ser-641 and Ser-645 by PP1 activates the enzyme (By similarity). Phosphorylation at Ser-8 is not required for interaction with GYG1 (By similarity). Interaction with GYG1 does not regulate the phosphorylation at Ser-8 and Ser-641 (By similarity).
Target data
Additional targets
Product promise
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
For licensing inquiries, please contact partnerships@abcam.com