| Code | CSB-RA010078A641phHU |
| Size | US$210 |
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| Application | Recommended Dilution |
|---|---|
| WB | 1:500-1:5000 |
| IF | 1:20-1:200 |
Glycogen synthase 1 (GYS1) serves as the rate-limiting enzyme in muscle glycogen synthesis, making it a central regulatory node in cellular energy metabolism. Phosphorylation at serine 641 represents one of the key inhibitory modifications that controls GYS1 activity, with this site serving as a direct target of glycogen synthase kinase-3 (GSK-3) and a readout of upstream insulin and growth factor signaling cascades. Researchers investigating metabolic regulation, diabetes pathways, or energy homeostasis rely on precise detection of this phosphorylation event to understand how cells balance glycogen storage with glucose utilization.
This recombinant rabbit monoclonal antibody, clone 1D1, was developed against a synthetic phosphopeptide corresponding to the human GYS1 sequence surrounding serine 641. The recombinant production method ensures that every lot delivers identical binding characteristics, eliminating the variability that can complicate longitudinal studies or multi-site collaborations. Affinity purification further enhances specificity for the phosphorylated epitope.
Validation studies demonstrate reliable performance across multiple experimental platforms. In western blot applications, the antibody detects a band at the predicted 85 kDa molecular weight in HeLa whole cell lysates and in HepG2 cells treated with Calyculin A or EGF, confirming its utility for monitoring phosphatase inhibition and growth factor-induced signaling dynamics. Immunofluorescence staining in HepG2 cells reveals clear cytoplasmic localization consistent with the known distribution of this metabolic enzyme.
Whether you are mapping insulin signaling networks, characterizing metabolic reprogramming in disease models, or screening compounds that modulate glycogen metabolism, this phospho-specific antibody provides the consistency and validated performance needed for confident signal transduction research.
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