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Mouse Monoclonal Glycogen Synthase 1 antibody [3A7] (STJ98112)
Supplier: St John’s Laboratory Ltd.
Recommended applications: WB, FC, ELISA
Recommended dilution: WB 1:500-1:2000; FC 1:200-1:400; ELISA 1:10000
Recommended protocols: check protocols
Click or hover above images to see image description for Glycogen Synthase 1 Monoclonal Antibody.
Check alternative names for the antibodyExpand
GYS1 antibody, GYS antibody,|Glycogen [starch] synthase antibody|Glycogen synthase 1 (muscle) antibody|Glycogen synthase 1 antibody|GSY antibody|GYS antibody|Gys1 antibody|GYS1_HUMAN antibody|muscle antibody|Anti-Glycogen synthase 1 antibody [EP817Y] (ab40810)
SCBT cat No: sc-47188|
Glycogen Synthase 1 Monoclonal Antibody
|Catalogue No.|| |
Glycogen Synthase 1 Monoclonal Antibody detects endogenous levels of Glycogen Synthase 1 protein.
Purified recombinant fragment of human Glycogen Synthase 1 expressed in E Coli
WB, FC, ELISA
|Recommended dilution|| |
WB 1:500-1:2000; FC 1:200-1:400; ELISA 1:10000
Glycogen Synthase 1 Antibody was tube-contained. Ascitic fluid containing 0.03% sodium azide.
Glycogen Synthase 1 Antibody was purified using affinity purification.
-20 Celsius degree. Avoid repeated freeze/thaw cycles.
|Alternative antibody names|| |
Glycogen synthase, muscle antibody,
|Protein names|| |
Glycogen synthase, muscle ,
|Protein function|| |
Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan. / UDP-alpha-D-glucose + ((1->4)-alpha-D-glucosyl)(n) = UDP + ((1->4)-alpha-D-glucosyl)(n+1). / Allosteric activation by glucose-6-phosphate. Phosphorylation reduces the activity towards UDP-glucose. When in the non-phosphorylated state, glycogen synthase does not require glucose-6-phosphate as an allosteric activator; when phosphorylated it does (By similarity). /
|Involvement in disease|| |
Muscle glycogen storage disease 0 (GSD0b) [MIM:611556]: Metabolic disorder characterized by fasting hypoglycemia presenting in infancy or early childhood. The role of muscle glycogen is to provide critical energy during bursts of activity and sustained muscle work. . Note: The disease is caused by mutations affecting the gene represented in this entry.
|Protein sequence and domain|| |
Belongs to the glycosyltransferase 3 family.
|Protein post-translational modifications|| |
Phosphorylation at Ser-8 by AMPK inactivates the enzyme activity. Primed phosphorylation at Ser-657 (site 5) by CSNK2A1 and CSNK2A2 is required for inhibitory phosphorylation at Ser-641 (site 3a), Ser-645 (site 3b), Ser-649 (site 3c) and Ser-653 (site 4) by GSK3A an GSK3B (By similarity). Phosphorylated at Ser-641 by DYRK2, leading to inactivation (By similarity). Phosphorylated at Ser-641 by PASK, leading to inactivation; phosphorylation by PASK is inhibited by glycogen. Dephosphorylation at Ser-641 and Ser-645 by PP1 activates the enzyme.
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St John’s Laboratory Ltd.
|Product type|| |
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