PEPCK-M/PCK2 Antibody (62-W): sc-130388

PEPCK-M Antibody (62-W) is a mouse monoclonal IgG2a kappa light chain antibody that detects PEPCK-M protein of human origin by western blotting (WB) and immunoprecipitation (IP). Anti-PEPCK-M antibody (62-W) is available as a non-conjugated format, providing researchers with a reliable tool for studying this critical protein. Phosphoenolpyruvate carboxykinase (PEPCK) is essential for gluconeogenesis, a metabolic pathway that generates glucose from non-carbohydrate substrates, thereby playing a vital role in maintaining blood glucose homeostasis. PEPCK-M monoclonal antibody (62-W) helps researchers study regulation particularly important in type 2 diabetes, where impaired gluconeogenesis can lead to hyperglycemia. PEPCK-M, the mitochondrial isoform of PEPCK, is specifically involved in converting oxaloacetate to phosphoenolpyruvate, a key step in gluconeogenesis. Expression is upregulated by glucagon and glucocorticoids, while insulin suppresses levels, highlighting the intricate balance of hormonal signals that govern glucose metabolism. Understanding the dynamics of PEPCK-M expression and regulatory mechanisms offers potential therapeutic avenues for addressing insulin resistance and obesity, making PEPCK-M (62-W) antibody an invaluable asset for investigating metabolic disorders.

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PEPCK-M/PCK2 Antibody (62-W) References:

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2. Identification of a novel variant in the phosphoenolpyruvate carboxykinase gene promoter in Japanese patients with type 2 diabetes.  |  Horikawa, Y., et al. 2003. Horm Metab Res. 35: 308-12. PMID: 12916001
3. Novel concepts in insulin regulation of hepatic gluconeogenesis.  |  Barthel, A. and Schmoll, D. 2003. Am J Physiol Endocrinol Metab. 285: E685-92. PMID: 12959935
4. Sustained peripheral expression of transgene adiponectin offsets the development of diet-induced obesity in rats.  |  Shklyaev, S., et al. 2003. Proc Natl Acad Sci U S A. 100: 14217-22. PMID: 14617771
5. AMP-activated protein kinase regulates PEPCK gene expression by direct phosphorylation of a novel zinc finger transcription factor.  |  Inoue, E. and Yamauchi, J. 2006. Biochem Biophys Res Commun. 351: 793-9. PMID: 17097062
6. Insulin and other regulatory factors modulate the growth and the phosphoenolpyruvate carboxykinase (PEPCK) activity of primary rabbit kidney proximal tubule cells in serum free medium.  |  Wang, Y. and Taub, M. 1991. J Cell Physiol. 147: 374-82. PMID: 1710231
7. Structures of rat cytosolic PEPCK: insight into the mechanism of phosphorylation and decarboxylation of oxaloacetic acid.  |  Sullivan, SM. and Holyoak, T. 2007. Biochemistry. 46: 10078-88. PMID: 17685635
8. Identification of a sequence in the PEPCK gene that mediates a negative effect of insulin on transcription.  |  O'Brien, RM., et al. 1990. Science. 249: 533-7. PMID: 2166335
9. PEPCK-M expression in mouse liver potentiates, not replaces, PEPCK-C mediated gluconeogenesis.  |  Méndez-Lucas, A., et al. 2013. J Hepatol. 59: 105-13. PMID: 23466304
10. Insulin decreases H4IIE cell PEPCK mRNA by a mechanism that does not involve cAMP.  |  Beale, EG., et al. 1986. Diabetes. 35: 546-9. PMID: 3007246
11. PEPCK-M recoups tumor cell anabolic potential in a PKC-ζ-dependent manner.  |  Hyroššová, P., et al. 2021. Cancer Metab. 9: 1. PMID: 33413684
12. Glycosylation defects, offset by PEPCK-M, drive entosis in breast carcinoma cells.  |  Hyroššová, P., et al. 2022. Cell Death Dis. 13: 730. PMID: 36002449

The preferred PEPCK/PCK1/PCK2 antibody is PEPCK/PCK1/PCK2 Antibody (F-3): sc-271029.