Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a classic glycolytic enzyme, is a multi-functional protein. It is mainly present in the cytoplasm. GAPDH is ubiquitously expressed. The GAPDH gene is located on human chromosome 12.
The product of this gene catalyzes an important energy-yielding step in carbohydrate metabolism, the reversible oxidative phosphorylation of glyceraldehyde-3-phosphate in the presence of inorganic phosphate and nicotinamide adenine dinucleotide (NAD). The enzyme exists as a tetramer of identical chains. Many pseudogenes similar to this locus are present in the human genome. (provided by RefSeq)
Immunogen
GAPDH (NP_002037, 226 a.a. ~ 335 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.
Monoclonal Anti-GAPDH antibody produced in mouse has been used in western blot, (1:5000)[1][2], and (1:2,000).[3]
Biochem/physiol Actions
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) participates in energy metabolism. It might have extra glycolytic roles in DNA repair. GAPDH plays a key role in glycolysis and several non-glycolytic actions. GAPDH binds to microtubules and regulates microtubule bundling and aids in membrane fusion. GAPDH participates in gene transcription, DNA replication, and nuclear RNA export. GAPDH acts as a uracil DNA glycosylase (UDG) that plays a role in DNA repair. It also acts as a mediator for cell death. GAPDH may play a role in Alzheimer′s disease (AD). It can be a potential therapeutic target in chemotherapy. Overexpression of the GAPDH gene in the T cell lineage is associated with angioimmunoblastic T cell lymphoma.
Physical form
Solution in phosphate buffered saline, pH 7.4
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FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 34(8), 10443-10461 (2020-06-17)
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a key enzyme involved in energy metabolism. Recently, GAPDH has been suggested to have extraglycolytic functions in DNA repair, but the underlying mechanism for the GAPDH response to DNA damage remains unclear. Here, we demonstrate that
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Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a classic glycolytic enzyme, and accumulating evidence has suggested that GAPDH is a multi-functional protein. In particular, its role as a mediator for cell death has been highlighted. For the last decade, many groups reported that
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