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Proteins and Peptides

Human IDH1 protein, His tag (active)

Product Sizes
100 ug
£335.00
GTX67054-PRO-100UG
About this Product
SKU:
GTX67054-PRO
Additional Names:
isocitrate dehydrogenase (NADP(+)) 1, cytosolic , HEL-216 , HEL-S-26 , IDCD , IDH , IDP , IDPC , PICD
Application:
Cell-based/Functional Assay
Buffer:
20mM Tris-HCl, 100mM NaCl, 20% Glycerol, 1mM DTT, 0.1mM PMSF, no preservatives.
Concentration:
1 mg/ml
Extra Details:
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. Alternatively spliced transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Sep 2013]
Immunogen:
isocitrate dehydrogenase (NADP(+)) 1, cytosolic
Physical State:
Liquid
Shipping Conditions:
Dry Ice
Storage Conditions:
-20[o]C Aliquot. Avoid freeze/thaw cycles. Store undiluted., 2-8[o]C Aliquot. Avoid freeze/thaw cycles. Store undiluted., -20[o]C/-70[o]C Aliquot. Avoid freeze/thaw cycles. Store undiluted.
Supplier:
GeneTex
Type:
Proteins, Peptides, Small Molecules & Other Biomolecules: Enzymes