Monoclonal Anti-GAPDH antibody produced in mouse

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)

GAPDH (NP_002037, 226 a.a. ~ 335 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.

Sequence
GKLTGMAFRVPTANVSVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGYSNRVVDLMAHMASKE

Monoclonal Anti-GAPDH antibody produced in mouse has been used in western blot, (1:5000), and (1:2,000).

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.

Solution in phosphate buffered saline, pH 7.4

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