Render Target: STATIC
Render Timestamp: 2024-11-27T11:07:31.898Z
Commit: d79925545b26f8827f92d145dadc6f0527debdb1
XML generation date: 2024-08-01 15:23:28.708
Product last modified at: 2024-11-14T21:00:10.584Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

Phospho-Glycogen Synthase (Ser641) Antibody #3891

Filter:
  • WB
  • IP

    Supporting Data

    REACTIVITY H M R
    SENSITIVITY Endogenous
    MW (kDa) 85 to 90
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:100

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    Phospho-Glycogen Synthase (Ser641) Antibody detects endogenous levels of both muscle and liver isoforms of glycogen synthase only when phosphorylated at serine 640 or 641 of the muscle and liver isoforms, respectively.

    Species Reactivity:

    Human, Mouse, Rat

    The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.

    Species predicted to react based on 100% sequence homology:

    Horse

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser641 of human liver glycogen synthase. Antibodies are purified by protein A and peptide affinity chromatography.

    Background

    Glycogen is a polysaccharide of glucose and serves as an energy storage in mammalian muscle and liver (1). Glycogen synthase catalyzes the rate-limiting step of glycogen biosynthesis and has two major isoforms in mammals: muscle isoform (glycogen synthase 1, GYS1) and liver isoform (glycogen synthase 2, GYS2), respectively (1). Glycogen synthase kinase-3α (GSK-3α) and glycogen synthase kinase-3β (GSK-3β) phosphorylate glycogen synthase at multiple sites in its C-terminus (Ser641, Ser645, Ser649, and Ser653), inhibiting its activity (2,3). Hypoxia alters glycogen metabolism including temporal changes of GYS1 expression and phosphorylation in cancer cells, suggesting the role of metabolic reprogramming of glycogen metabolism in cancer growth (1).
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