KGA Antibody (IJ-2): sc-100533

KGA Antibody (IJ-2) is a mouse monoclonal IgG2a kappa light chain antibody that detects KGA protein of human origin by western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), and enzyme-linked immunosorbent assay (ELISA). Anti-KGA antibody (IJ-2) is available as the non-conjugated form. KGA protein plays a crucial role in cellular metabolism, particularly in glutamine catabolism, which is vital for various physiological processes, including nitrogen transport and energy production. Located primarily in mitochondria, KGA protein is essential for converting glutamine to glutamate, a key neurotransmitter, and is involved in acid-base balance regulation in kidney, especially during metabolic acidosis. KGA protein expression increases in response to low pH conditions, highlighting its importance in maintaining metabolic homeostasis. Human KGA gene, mapped to chromosome 2, produces three isoforms—KGA, GAC, and GAM—through alternative splicing, with KGA isoform being predominantly expressed in brain and kidney, while GAC isoform is mainly found in cardiac muscle and pancreas. Understanding KGA protein function and regulation is critical for elucidating its role in metabolic disorders and potential therapeutic targets.

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KGA Antibody (IJ-2) References:

1. Identification of two human glutaminase loci and tissue-specific expression of the two related genes.  |  Aledo, JC., et al. 2000. Mamm Genome. 11: 1107-10. PMID: 11130979
2. Structural basis for the allosteric inhibitory mechanism of human kidney-type glutaminase (KGA) and its regulation by Raf-Mek-Erk signaling in cancer cell metabolism.  |  Thangavelu, K., et al. 2012. Proc Natl Acad Sci U S A. 109: 7705-10. PMID: 22538822
3. Structural basis for the active site inhibition mechanism of human kidney-type glutaminase (KGA).  |  Thangavelu, K., et al. 2014. Sci Rep. 4: 3827. PMID: 24451979
4. Physapubescin, a natural withanolide as a kidney-type glutaminase (KGA) inhibitor.  |  Cheng, L., et al. 2017. Bioorg Med Chem Lett. 27: 1243-1246. PMID: 28174105
5. Design and synthesis of novel tellurodibenzoic acid compounds as kidney-type glutaminase (KGA) inhibitors.  |  Hou, W., et al. 2019. Bioorg Med Chem Lett. 29: 1673-1676. PMID: 31076348
6. Upregulation of GLS1 Isoforms KGA and GAC Facilitates Mitochondrial Metabolism and Cell Proliferation in Epstein-Barr Virus Infected Cells.  |  Krishna, G., et al. 2020. Viruses. 12: PMID: 32727118