GAPDH (C-Term) Rabbit Monoclonal Antibody (RM114)

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is an enzyme that catalyzes the conversion of glyceraldehyde-3-phosphate (Item No. 17865) to 1,3-bisphosphoglycerate during glycolysis and is involved in numerous additional cellular processes, including intracellular trafficking, receptor-mediated signaling, apoptosis, DNA repair, and the oxidative stress response.^1,2 It exists as a tetramer and is composed of an N-terminal domain, which contains binding sites for NAD⁺, phosphatidylserine, RNA, and glutathione, and a C-terminal catalytic domain.³ GAPDH is widely expressed and primarily localizes to the cytosol, where it has roles in glycolysis and intracellular trafficking.^1,4 It also localizes to the nucleus, mediating DNA integrity, gene transcription, and apoptosis, as well as to cellular membranes, where it has roles in membrane fusion and iron transport.⁴ GAPDH expression is increased by insulin, hypoxia-inducible factor-1 (HIF-1), p53, and nitric oxide (NO) and decreased by acetylated histones.^1,5 Aberrant mRNA and protein levels of GAPDH have been found in tumor biopsies from patients with a variety of cancers, including lung, renal cell, colorectal, or breast cancer.⁶ Cayman's GAPDH (C-Term) Rabbit Monoclonal Antibody (RM114) can be used for immunocytochemistry (ICC), immunoprecipitation (IP), chromatin immunoprecipitation (ChIP), and Western blot (WB) applications. The antibody recognizes the C-terminal region of GAPDH at approximately 36 kDa.

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1. Tristan, C., Shahani, N., Sedlak, T.W., et al. The diverse functions of GAPDH: Views from different subcellular compartments. Cell. Signal. 23(2), 317-323 (2011).

2. Sirover, M.A. On the functional diversity of glyceraldehyde-3-phosphate dehydrogenase: Biochemical mechanisms and regulatory control. Biochim. Biophys. Acta 1810(8), 741-751 (2011).

3. Sirover, M.A. Structural analysis of glyceraldehyde-3-phosphate dehydrogenase functional diversity. Int. J. Biochem. Cell Biol. 57, 20-26 (2014).

4. Sirover, M.A. Pleiotropic effects of moonlighting glyceraldehyde-3-phosphate dehydrogenase (GAPDH) in cancer progression, invasiveness, and metastases. Cancer Metastasis Rev. 37(4), 665-676 (2018).

5. Zhang, J.-Y., Zhang, F., Hong, C.-Q., et al. Critical protein GAPDH and its regulatory mechanisms in cancer cells. Cancer Biol. Med. 12(1), 10-22 (2015).

6. Guo, C., Liu, S., and Sun, M.-Z. Novel insight into the role of GAPDH playing in tumor. Clin. Transl. Oncol. 15(3), 167-172 (2013).