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Literature summary for 2.4.1.186 extracted from

  • Skurat, A.V.; Dietrich, A.D.; Roach, P.J.
    Interaction between glycogenin and glycogen synthase (2006), Arch. Biochem. Biophys., 456, 93-97.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.4.1.186

Application

Application Comment Organism
synthesis the COOH-terminal fragment of glycogenin can be used as a effective high affinity reagent for the purification of glycogen synthase from skeletal muscle and liver
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Protein Variants

Protein Variants Comment Organism
additional information deletion construct pGEX-GN (263-333). The fragment of glycogenin is fused with glutathione-S-transferase (GST). The fusion protein is able to precipitate glycogen synthase in the presence of glutathione-agarose.
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additional information deletion construct pGEX-GN (297-333). The fragment of glycogenin is fused with glutathione-S-transferase (GST). The fusion protein is able to precipitate glycogen synthase in the presence of glutathione-agarose.
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additional information deletion construct pGEX-GN (301-333). The fragment of glycogenin is fused with glutathione-S-transferase (GST). The fusion protein is able to precipitate glycogen synthase in the presence of glutathione-agarose.
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Organism

Organism UniProt Comment Textmining
Homo sapiens
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 the amino acid residues 301-333 in glycogenin are engaged in interaction with glycogen synthase. Glycogenin contains at least one additional interacting site for glycogen synthase beside the COOH-terminus.
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Source Tissue

Source Tissue Comment Organism Textmining
muscle skeletal muscle library
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Synonyms

Synonyms Comment Organism
glycogenin
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