Glyceraldehyde-3-phosphate dehydrogenase human

Human glyceraldehyde-3-phosphate dehydrogenase has been used as a positive control for hydrogen sulfide treatment to detect sulfhydration of protein targets.

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) catalyzes the reversible oxidative phosphorylation of glyceraldehyde-phosphate, which is a critical energy-yielding step in carbohydrate metabolism. It binds to several proteins including actin, tubulin, amyloid precursor, polyglutamine peptides, DRPLA (dentatorubral-pallidoluysian atrophy) and huntingtin. Phosphorylated GAPDH associates with cytoskeletal elements and controls microtubule dynamics in the early secretory pathway. GAPDH is also a component of the functional GAIT (interferon-?-activated inhibitor of translation) mRNP (messenger ribonucleoprotein). GAPDH expression is dysregulated during melanoma progression.

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) localizes to the cytoplasm but can be translocated to the nucleus depending on cellular conditions. It is a tetramer containing identical chains. The gene encoding GAPDH is localized on human chromosome 12p13.

Alternative number: CAS Number 9001-50-7

One unit will reduce 1.0 μmole of 3-phosphoglycerate to D-glyceraldehyde 3-phosphate per minute in a coupled system with 3-phosphoglyceric phosphokinase (3-PGK) at pH 7.6 at 25 °C

This product is recombinant, human GAPDH expressed in E. coli with an N-terminal histidine tag and has a predicted molecular mass of 37,984 Da. The product is lyophilized from a buffered solution with stabilizers.