Isocitrate dehydrogenase (IDH1) Mouse Monoclonal Antibody [Clone ID: LBI2H9]

mAbs-V

Stable for 1 year at -20°C from date of shipment. For maximum recovery of product, centrifuge the original vial after thawing and opening the cap. Aliquot will be stable at 4°C short term. For long-term storage, aliquot and store at -20°C or below. Stable for 12 months at -20°C. Avoid repeated freeze-thaw cycles.

Carrier-free (BSA/glycerol-free) IDH1 mouse monoclonal antibody, clone LBI2H9

Homo sapiens isocitrate dehydrogenase (NADP(+)) 1 (IDH1), transcript variant 1, mRNA.

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.

Lyophilized powder (original buffer 1X PBS, pH 7.3, 8% trehalose)

Purified from mouse ascites fluids or tissue culture supernatant by affinity chromatography (protein A/G)