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Isocitrate dehydrogenases catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. Additionally we are shipping IDH1 Kits (15) and IDH1 Proteins (15) and many more products for this protein.
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Human Polyclonal IDH1 Primary Antibody for FACS, IF - ABIN391659
Geisbrecht, Gould: The human PICD gene encodes a cytoplasmic and peroxisomal NADP(+)-dependent isocitrate dehydrogenase. in The Journal of biological chemistry 1999
Show all 2 references for ABIN391659
Cow (Bovine) Polyclonal IDH1 Primary Antibody for IHC, WB - ABIN2785883
Kullberg, Nilsson, Arnason, Harley, Janke: Housekeeping genes for phylogenetic analysis of eutherian relationships. in Molecular biology and evolution 2006
Show all 2 references for ABIN2785883
Human Polyclonal IDH1 Primary Antibody for FACS, IF - ABIN391660
Xu, Zhao, Xu, Peng, Huang, Arnold, Ding: Structures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activity. in The Journal of biological chemistry 2004
Show all 2 references for ABIN391660
Human Monoclonal IDH1 Primary Antibody for IF, IHC - ABIN2452633
Elhammali, Ippolito, Collins, Crowley, Marasa, Piwnica-Worms: A high-throughput fluorimetric assay for 2-hydroxyglutarate identifies Zaprinast as a glutaminase inhibitor. in Cancer discovery 2014
IDH1 Mutations are associated with Glioma.
the article summarizes recent progress in understanding of the role of mutations in the genes encoding IDH1 and IDH2 (show IDH2 Antibodies) in tumorigenesis (Review)
formylcytosine (5fC) and 5-carboxylcytosine (5caC) levels did not change significantly in these tissues. We further examined the expression levels of IDH1 and IDH2 (show IDH2 Antibodies) in gastric cancer tissues and observed that IDH2 (show IDH2 Antibodies) levels were significantly lower in gastric cancer tissues than in the adjacent normal tissues
Report a simple, non-germline murine intrahepatic cholangiocarcinoma model with activated Notch (show NOTCH1 Antibodies), loss of p53 (show TP53 Antibodies) and IDH1R132C mutation, supporting the oncogenic potential of IDH1R132C.
In patients with glioblastoma multiforme, less than a quarter of our patients' long-term survivorship was associated with favorable IDH1 status.
Identification of DNMT3A and IDH1/IDH2 mutations is instrumental for early detection of acute myeloid leukemia relapse after allogeneic hematopoietic stem cell transplantation.
mechanistic studies of IDH1 mutations in gliomas (review)
IDH1 (R132H) mutation may not preclude distant, trans-tentorial spread in gliomas.
preclinical studies assessing small molecule inhibitors of mutant IDH1/2 enzymes have provided proof of concept that this approach decreases intracellular 2-HG levels, reverses epigenetic dysregulation and induces cellular differentiation
IDH1 mutation is associated with higher risk of malignant transformation in low-grade glioma.
data suggest that mutant IDH1 contributes to malignancy in the T-cell lineage and may alter the metabolic profile of malignant T cells
The results suggest that Idh1 has a physiological function in protecting cells from oxidative stress by regulating the intracellular NADP(+)/NADPH (show FDXR Antibodies) ratio.
These results support the translational potential of immunotherapeutic targeting of gliomas carrying IDH1 mutations R132H.
MiR (show MLXIP Antibodies)-181a regulates lipid metabolism via IDH1
revealed a role for IDH1 in the synthesis/turnover of phospholipids in developing astrocytes and highlight the lipid alterations resulting from the loss of wild-type IDH1 activity.
these data show that mutant IDH or d-2HG causes persistence of chondrocytes, giving rise to rests of growth-plate cells that persist in the bone as enchondromas.
WA might exert its chemopreventive activity via inhibiting not only oncogenic activation, but also IDH1 inactivation.
Brain-specific (show CALY Antibodies) Idh1-KI mice show brain hemorrhage accompanied by high D2HG levels but decreased ROS (show ROS1 Antibodies)
Suggest that decreased IDPc expression renders melanocytes more vulnerable to oxidative stress, and IDPc plays an important antioxidant function in melanocytes.
Absence of IDH1 mutations in low-grade gliomas (LGGs) identifies a novel entity of LGGs with distinctive location, infiltrative behavior, specific molecular alterations, and dismal outcome.
Data suggest that the expression of cytosolic NADP+-dependent isocitrate dehydrogenase in bovine mammary epithelium is modulated by regulators of differentiation including extracellular matrix and lactogenic hormones as well as metabolic effectors.
Tyr140 and Lys212 are required for the catalytic activity of porcine NADP-dependent isocitrate dehydrogenase (show IDH3B Antibodies)
analysis of the coenzyme binding site in the porcine mitochondrial NADP-dependent isocitrate dehydrogenase (show IDH3B Antibodies)
These results suggest that IDPm (show IDH2 Antibodies) plays an important protective role in cadmium-induced apoptosis by maintaining cellular redox status and by protection of Grx (show GRX1 Antibodies) activity.
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.
isocitrate dehydrogenase 1 (NADP+), soluble
, isocitrate dehydrogenase [NADP] cytoplasmic-like
, NADP(+)-specific ICDH
, NADP-dependent isocitrate dehydrogenase, cytosolic
, NADP-dependent isocitrate dehydrogenase, peroxisomal
, isocitrate dehydrogenase [NADP] cytoplasmic
, oxalosuccinate decarboxylase
, cytosolic NADP-isocitrate dehydrogenase
, isocitrate dehydrogenase 1
, Isocitrate dehydrogenase 1, soluble
, NADPH-specific isocitrate dehydrogenase
, isocitrate dehydrogenase [NADP], mitochondrial