Cell Signaling Technology

Product Pathways - Metabolism

Phospho-Glycogen Synthase (Ser641) Antibody #3891

Applications Reactivity Sensitivity MW (kDa) Source
W IP IHC-P H M R Endogenous 85 to 90 Rabbit

Applications Key:  W=Western Blotting  IP=Immunoprecipitation  IHC-P=Immunohistochemistry (Paraffin)
Reactivity Key:  H=Human  M=Mouse  R=Rat
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

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.

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.

Western Blotting

Western Blotting

Western blot analysis of extracts from NIH/3T3 cells treated with calf intestinal alkaline phosphatase (CIP), using Phospho-Glycogen Synthase (Ser641) Antibody (upper) or control glycogen synthase antibody (lower).

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human breast carcinoma, showing cytoplasmic localization, using Phospho-Glycogen Synthase (Ser641) Antibody.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded renal clear cell adenocarcinoma using Phospho-Glycogen Synthase (Ser641) Antibody.


Background

Glycogen synthase (GS) is a key enzyme in the regulation of glycogen synthesis. There are two main isoforms of mammalian GS: the muscle and the liver isoform (1-2). Muscle GS is expressed in several tissues, and liver GS appears to be tissue specific (3). GS is regulated by multi-site phosphorylation and by the binding of allosteric ligands. Phosphorylation leads to inactivation of GS, but activity is restored by the binding of the allosteric activator glucose-6-phosphate, which induces its dephosphorylation and activation (4).

Ser641 is one of the most important phosphorylation sites for the regulation of glycogen synthase (5).

  1. Browner, M.F. et al. (1989) Proc. Natl. Acad. Sci. USA 86, 1443-1447.
  2. Bai, G. et al. (1990) J. Biol. Chem. 265, 7843-7848.
  3. Roach, P.J. et al. (1998) J. Basic Clin. Physiol. Pharmacol. 9, 139-151.
  4. Villar-Palasi, C. and Guinovart, J.J. (1997) FASEB J. 11, 544-558.
  5. Skurat, A.V. and Roach, P.J. (1995) J. Biol. Chem. 270, 12491-12497.

Application References

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