| Code | CSB-RA935337A0HU |
| Size | US$210 |
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| Application | Recommended Dilution |
|---|---|
| WB | 1:500-1:5000 |
Phosphoglycerate mutase 1 (PGAM1) serves as a critical enzyme in glycolysis, catalyzing the interconversion of 3-phosphoglycerate and 2-phosphoglycerate. Beyond its metabolic function, PGAM1 has emerged as a significant player in cancer biology, where its upregulation supports the enhanced glycolytic activity characteristic of rapidly proliferating tumor cells. This metabolic reprogramming makes PGAM1 an attractive target for researchers investigating cancer metabolism, signal transduction pathways, and potential therapeutic interventions.
This recombinant monoclonal antibody, clone 9A5, offers the reproducibility and consistency that demanding experimental workflows require. Because it is produced from a defined sequence rather than traditional hybridoma methods, you can expect uniform performance across different lots, eliminating the variability that can complicate long-term studies or multi-site collaborations. The rabbit IgG format, raised against a synthetic peptide derived from human PGAM1, provides excellent specificity for your target.
Validation by western blot demonstrates robust detection across an impressive range of sample types, including human cell lines such as HeLa, 293, HepG2, A549, and MCF-7, as well as mouse NIH/3T3 cells and both mouse and rat brain tissue lysates. This cross-species reactivity spanning human, mouse, and rat samples provides flexibility for comparative studies or translational research models. The antibody detects a band at approximately 29 kDa, slightly above the predicted 28 kDa molecular weight, a minor shift likely attributable to post-translational modifications. Recommended working dilutions range from 1:500 to 1:5000, allowing optimization for your specific experimental conditions.
Whether you are exploring metabolic alterations in cancer models or investigating PGAM1's role in cellular signaling, this antibody delivers the reliable performance your research demands.
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