| Code | CSB-RA018072MA1HU |
| Size | US$210 |
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| Application | Recommended Dilution |
|---|---|
| WB | 1:500-1:2000 |
| IHC | 1:50-1:200 |
| IF | 1:50-1:200 |
| FC | 1:50-1:200 |
Pyruvate kinase M (PKM) serves as a critical metabolic gatekeeper, catalyzing the final rate-limiting step of glycolysis by converting phosphoenolpyruvate to pyruvate. This enzyme has garnered substantial research attention due to its alternatively spliced isoforms, particularly PKM2, which plays a pivotal role in the Warburg effect observed in cancer cells. Beyond its glycolytic function, PKM interacts with thyroid hormone-binding proteins and participates in diverse cellular processes, making it an essential target for metabolic research, oncology studies, and investigations into cellular energy homeostasis.
This recombinant monoclonal antibody, generated against recombinant human PKM protein, offers the reproducibility and consistency that demanding experimental workflows require. As a sequence-defined reagent with defined clone identity (6C3C7), it eliminates the lot-to-lot variability that can compromise longitudinal studies and multi-site collaborations. The human IgG1 isotype and affinity-chromatography purification ensure reliable performance across applications.
Extensive validation demonstrates this antibody's versatility across multiple experimental platforms. Western blot analysis confirms detection of the expected 58 kDa band across human cell lines including HEK293, HeLa, A431, Jurkat, and U-251MG, with cross-species reactivity verified in mouse and rat skeletal muscle tissue lysates. Immunohistochemistry staining in human skeletal muscle tissue, immunofluorescence in HeLa cells, and flow cytometry analysis in HepG2 cells further establish its utility for diverse sample types and detection methods.
Whether investigating tumor metabolism, characterizing glycolytic pathway regulation, or exploring PKM's non-canonical functions in cellular signaling, this antibody provides researchers with a dependable tool for advancing their understanding of this metabolically significant enzyme.
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