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     Western blot analysis of Glycogen synthase expression in HeLa cell lysate.    

  
  

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     All lanes use the Antibody at 1:5K dilution for 1 hour at room temperature.    

  
  

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     All lanes use the Antibody at 1:5K dilution for 1 hour at room temperature.    

  
  

Glycogen synthase (GS) antibodies are essential tools in studying the regulation of glycogen metabolism, a critical process in energy homeostasis. GS is the rate-limiting enzyme responsible for glycogen synthesis, catalyzing the transfer of glucose monomers from UDP-glucose to glycogen chains. Its activity is tightly regulated by phosphorylation-dephosphorylation mechanisms, primarily through insulin and glucagon signaling. Antibodies targeting GS enable researchers to detect and quantify its expression, post-translational modifications (e.g., phosphorylation at Ser641. Ser645), and subcellular localization in tissues like liver, muscle, and adipose.

These antibodies are widely used in metabolic research, particularly in diabetes, obesity, and glycogen storage diseases. Phospho-specific GS antibodies help assess its inactive (phosphorylated) vs. active (dephosphorylated) states, reflecting cellular energy status. Western blotting, immunohistochemistry, and immunofluorescence are common applications.

Commercial GS antibodies are typically raised in rabbits or mice against peptide sequences from human or rodent GS isoforms (GS1 in liver, GS2 in muscle). Validation includes knockout controls and activity correlation. Dysregulation of GS is linked to insulin resistance, making these antibodies valuable in exploring therapeutic targets for metabolic disorders.