Mouse monoclonal antibody raised against partial recombinant human IDH1.
Recombinant protein corresponding to 119 residues around amino acids 280-420 of human IDH1.
Theoretical MW (kDa):
Protein A/G purification
Flow Cytometry (0.5-1 ug/106 cells in 0.1 mL) Immunofluorescence (0.5-1 ug/mL) Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) (0.5-1 ug/mL) Western Blot (0.5-1 ug/mL) The optimal working dilution should be determined by the end user.
In 1 mM PBS.
Store at -20 to -80°C. Aliquot to avoid repeated freezing and thawing.
Isocitrate dehydrogenases catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. These enzymes belong to two distinct subclasses, one of which utilizes NAD(+) as the electron acceptor and the other NADP(+). Five isocitrate dehydrogenases have been reported: three NAD(+)-dependent isocitrate dehydrogenases, which localize to the mitochondrial matrix, and two NADP(+)-dependent isocitrate dehydrogenases, one of which is mitochondrial and the other predominantly cytosolic. Each NADP(+)-dependent isozyme is a homodimer. The protein encoded by this gene is the NADP(+)-dependent isocitrate dehydrogenase found in the cytoplasm and peroxisomes. It contains the PTS-1 peroxisomal targeting signal sequence. The presence of this enzyme in peroxisomes suggests roles in the regeneration of NADPH for intraperoxisomal reductions, such as the conversion of 2, 4-dienoyl-CoAs to 3-enoyl-CoAs, as well as in peroxisomal reactions that consume 2-oxoglutarate, namely the alpha-hydroxylation of phytanic acid. The cytoplasmic enzyme serves a significant role in cytoplasmic NADPH production. [provided by RefSeq