Host: E. coli • AA: 1-335 • Tag: N-terminal His • MW: 38 kDa
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GAPDH (human, recombinant)

Item No. 31819

Technical Information
Synonyms
  • GAPD Protein
  • G3PD Protein
  • HEL-S-162eP
  • Peptidyl-cysteine S-nitrosylase
Purity
≥90% estimated by SDS-PAGE
Source
Recombinant human N-terminal His-tagged GAPDH expressed in E. coli
Amino Acids
1-335 (full length)
MW
38 kDa
Lyophilized from sterile 50 mM Tris, pH 7.5, with 30% glycerol
UniProt Accession №
P04406
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    Product Description

    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 (human, recombinant) protein consists of 346 amino acids and has a calculated molecular weight of 38 kDa.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Tristan, C., Shahani, N., Sedlak, T.W., et alThe 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 alCritical 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).