IDH3A Mouse Monoclonal Antibody [Kloon ID: LBI5D2]

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. NAD (+) -dependent isocitrate dehydrogenases catalyze the allosterically regulated rate-limiting step of the tricarboxylic acid cycle. Each isozyme is a heterotetramer that is composed of two alpha subunits, one beta subunit, and one gamma subunit. The protein encoded by this gene is the alpha subunit of one isozyme of NAD (+) -dependent isocitrate dehydrogenase. [provided by RefSeq]

Carrier-free (BSA/glycerol-free) IDH3A mouse monoclonal antibody, clone LBI5D2

H-IDH alpha; isocitrate dehydrogenase (NAD+) alpha chain; isocitrate dehydrogenase 3 (NAD+) a; isocitrate dehydrogenase [NAD] subunit alpha; isocitric dehydrogenase; mitochondrial; NAD (H) -specific isocitrate dehydrogenase alpha subunit; NAD+-specific ICDH

Homo sapiens isocitrate dehydrogenase (NAD (+) ) 3 catalytic subunit alpha (IDH3A), mRNA; nuclear gene for mitochondrial product.

3419

P50213

Unconjugated

Citrate cycle (TCA cycle), Metabolic pathways

Citrate cycle (TCA cycle), Metabolic pathways

WB 1:500, IF 1:100

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

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

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.

IDH3A

https://www.ncbi.nlm.nih.gov/gene/?term=3419

https://www.uniprot.org/uniprot/P50213