phosphorylase, Glycogen, Liver (PYGL) (Middle Region) Peptide
PYGL
Reactivity: Human
Host: Synthetic
WB
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- Target See all PYGL products
- PYGL (phosphorylase, Glycogen, Liver (PYGL))
- Protein Region
- Middle Region
- Origin
- Human
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Source
- Synthetic
- Application
- Western Blotting (WB)
- Sequence
- SMATLGLAAY GYGIRYEYGI FNQKIRDGWQ VEEADDWLRY GNPWEKSRPE
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- Restrictions
- For Research Use only
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- Format
- Lyophilized
- Reconstitution
- Add 100 μL of sterile PBS. Final peptide concentration is 1 mg/mL in PBS.
- Storage
- -20 °C
- Storage Comment
- For longer periods of storage, store at -20°C. Avoid repeat freeze-thaw cycles.
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- Target
- PYGL (phosphorylase, Glycogen, Liver (PYGL))
- Synonyms
- zgc:66314 Peptide, GSD6 Peptide, glycogen phosphorylase L Peptide, phosphorylase, glycogen, liver Peptide, phosphorylase, glycogen, liver S homeolog Peptide, liver glycogen phosphorylase Peptide, PYGL Peptide, pygl Peptide, pygl.S Peptide, Pygl Peptide
- Background
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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.
Alias Symbols: GSD6
Protein Size: 167 - Gene ID
- 5836
- NCBI Accession
- NM_001163940, NP_001157412
- UniProt
- P06737
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