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The expression region of this recombinant Human PYGL covers amino acids 2-846. This PYGL protein is expected to have a theoretical molecular weight of 123.9 kDa. The PYGL protein was expressed in e.coli. The PYGL coding gene included the N-terminal GST tag, which simplifies the detection and purification processes of the recombinant PYGL protein in following stages of expression and purification.Glycogen phosphorylase, liver form (PYGL) is an enzyme crucial for glycogenolysis, the breakdown of glycogen into glucose-1-phosphate. The main function of PYGL is to mobilize glucose from glycogen stores, providing an essential energy source during periods of increased energy demand. In the liver, PYGL plays a key role in maintaining blood glucose levels by releasing glucose into the bloodstream. Research on PYGL involves understanding its regulation and involvement in metabolic processes. Dysregulation of PYGL has been associated with metabolic disorders such as glycogen storage diseases, where impaired glycogen breakdown leads to abnormal glycogen accumulation. Investigating PYGL function contributes to insights into metabolic homeostasis, glycogen metabolism, and the development of therapeutic strategies for related disorders.
The expression region of this recombinant Human PYGL covers amino acids 2-846. This PYGL protein is expected to have a theoretical molecular weight of 123.9 kDa. The PYGL protein was expressed in e.coli. The PYGL coding gene included the N-terminal GST tag, which simplifies the detection and purification processes of the recombinant PYGL protein in following stages of expression and purification.Glycogen phosphorylase, liver form (PYGL) is an enzyme crucial for glycogenolysis, the breakdown of glycogen into glucose-1-phosphate. The main function of PYGL is to mobilize glucose from glycogen stores, providing an essential energy source during periods of increased energy demand. In the liver, PYGL plays a key role in maintaining blood glucose levels by releasing glucose into the bloodstream. Research on PYGL involves understanding its regulation and involvement in metabolic processes. Dysregulation of PYGL has been associated with metabolic disorders such as glycogen storage diseases, where impaired glycogen breakdown leads to abnormal glycogen accumulation. Investigating PYGL function contributes to insights into metabolic homeostasis, glycogen metabolism, and the development of therapeutic strategies for related disorders.
| Cat.No | ACP04714 | Target Name | PYGL |
|---|---|---|---|
| Form | Liquid or Lyophilized powder | Expression System | E.coli |
| Expression Range | 2-846aa | Mol Weight | 123.9kDa |
| Protein Length | Partial | Purity | Greater than 90% as determined by SDS-PAGE. |
| Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | P06737 |
|---|
Uniprot Id
P06737
Target Species
Human
Target Name
PYGL
Target Full Name
Glycogen phosphorylase, liver form
Target 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.
Target Involvement
Glycogen storage disease 6 (GSD6)
Target Subcellular Location
Cytoplasm, cytosol.
Target Protein Families
Glycogen phosphorylase family
Target Research Area
Metabolism
Target Synonyms
Glycogen phosphorylase; Glycogen phosphorylase L; Glycogen phosphorylase liver; Glycogen phosphorylase liver form; GSD6; Hers disease; glycogen storage disease type VI; liver form; OTTHUMP00000233649; OTTHUMP00000233651; Phosphorylase glycogen liver; Pygl; PYGL_HUMAN
Target Background
This gene encodes a homodimeric protein that catalyses the cleavage of alpha-1, 4-glucosidic bonds to release glucose-1-phosphate from liver glycogen stores. This protein switches from inactive phosphorylase B to active phosphorylase A by phosphorylation of serine residue 15. Activity of this enzyme is further regulated by multiple allosteric effectors and hormonal controls. Humans have three glycogen phosphorylase genes that encode distinct isozymes that are primarily expressed in liver, brain and muscle, respectively. The liver isozyme serves the glycemic demands of the body in general while the brain and muscle isozymes supply just those tissues. In glycogen storage disease type VI, also known as Hers disease, mutations in liver glycogen phosphorylase inhibit the conversion of glycogen to glucose and results in moderate hypoglycemia, mild ketosis, growth retardation and hepatomegaly. Alternative splicing results in multiple transcript variants encoding different isoforms.
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