IDH1 Monoclonal / Janelia Fluor 549 / IDH1/1152
Product Details
| Description | It recognizes a 45kDa protein, which is identified as isocitrate dehydrogenase (IDH1). It belongs to the isocitrate and isopropylmalate dehydrogenases family. IDH1 catalyzes the third step of the citric acid cycle, which involves the oxidative decarboxylation of isocitrate, forming ketoglutarate and CO2 in a two-step reaction. The first step involves the oxidation of isocitrate to the intermediate oxalosuccinate, while the second step involves the production of ketoglutarate. During this process, either NADH or NADPH is produced along with CO2. Recently, an inactivating mutation of IDH1 has been implicated in glioblastoma. IDH1 appears to function as a tumor suppressor that, when mutationally inactivated, contributes to tumorigenesis in part through induction of the HIF-1 pathway. | |
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| Conjugate | Janelia Fluor 549 | |
| Clone | IDH1/1152 | |
| Target Species | Human | |
| Applications | FC, IF, IHC-P, IHC | |
| Supplier | Novus Biologicals | |
| Catalog # | Sign in to view product details, citations, and spectra | |
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About IDH1
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]
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]
About Janelia Fluor 549
Janelia Fluor® 549 was developed at the Janelia Campus of the Howard Hughes Medical Institute but is commercialized by other vendors. The Janelia Fluor®s family is unique in that the fluorophores are cell-permeable and are available in photoactivatable forms. These fluorophores were developed for super-resolution microscopy (STED, PALM and STORM) and live-cell microscopy in the HaloTag and SNAP-tag versions. Janelia Fluor® 549 has an excitation peak at 549 nm and an emission peak at 571 nm.
Janelia Fluor® 549 was developed at the Janelia Campus of the Howard Hughes Medical Institute but is commercialized by other vendors. The Janelia Fluor®s family is unique in that the fluorophores are cell-permeable and are available in photoactivatable forms. These fluorophores were developed for super-resolution microscopy (STED, PALM and STORM) and live-cell microscopy in the HaloTag and SNAP-tag versions. Janelia Fluor® 549 has an excitation peak at 549 nm and an emission peak at 571 nm.
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