Recombinant Human PYGL protein
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Recombinant Human PYGL protein is a Human Full Length protein, in the 1 to 847 aa range, expressed in Escherichia coli, with >80%, suitable for SDS-PAGE.
View Alternative Names
PYGL
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human PYGL protein (AB202149)
15% SDS-PAGE analysis of ab202149 (3 μg).
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
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
The enzyme plays a major role in maintaining energy homeostasis by mobilizing glucose from glycogen stores during fasting states. It does not function as part of a larger complex operating instead as a homodimer when activated. PYGL is critical for the liver's ability to supply glucose to other organs when dietary glucose is not available. Proper functioning of PYGL helps maintain a balance between glucose storage and release contributing to overall metabolic equilibrium.
Pathways
PYGL has a notable role in glycogenolysis a process that liberates stored glycogen as glucose-1-phosphate. This enzyme also connects with gluconeogenesis where it impacts the production of glucose from non-carbohydrate sources. In these pathways its activity often intersects with other enzymes namely phosphoglucomutase and glucose-6-phosphatase which further process the products of PYGL’s activity.
Specifications
Form
Liquid
Additional notes
ab202149 was purified using conventional chromatography techniques.
General info
Function
Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis.
Sequence similarities
Belongs to the glycogen phosphorylase family.
Post-translational modifications
Acetylation, which is up-regulated by glucose and insulin and down-regulated by glucagon, inhibits the glycogen phosphorylase activity by promoting PPP1R3B-mediated recruitment of phosphatase PP1 and Ser-15 dephosphorylation.. Phosphorylation at Ser-15 converts inactive phosphorylase b into active phosphorylase a (PubMed:10949035). Dephosphorylation of Ser-15 by phosphatase PP1 inactivates the enzyme (PubMed:22225877).
Target data
Complementary Products
Product promise
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