Recombinant Human Glycerol-3-Phosphate Dehydrogenase 2

GPD2 (Mitochondrial glycerol-3-phosphate dehydrogenase) is a Ca2+-sensitive, FAD-binding protein, which is located on the outer surface of the inner mitochondrial membrane. Two isoforms have been identified for mGPD: Isoform 1 is comprised of 727 a.a. residues, while isoform 2 lacks 126 a.a. residues of the N-terminus. GPD2 catalyses the oxidation of glycerol-3-phosphate to DHAP (dihydroxyacetone phosphate) with associated reduction of the enzyme-bound FAD. GPD2 is a testis-specific promoter of mitochondrial GPDH. GPD2 along with a cytosolic NAD-linked GPD forms the glycerol phosphate shuttle that uses the interconversion of G-3-P and DHAP to transfer reducing equivalents into mitochondria, which results in the reoxidation of NADH produced during glycolysis.
GPD2 deficiency contributes to the impairment of glucose-stimulated insulin discharge in a number of animal models of non-insulin dependent diabetes mellitus. GPD2 up-regulation as a result of a highly glycolytic environment contributes to the general increase in ROS generation and may lead to the progression of prostate cancer.

Escherichia Coli.

GPD2 protein is supplied in 1x PBS and 50% glycerol.

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