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Mouse Anti-IDH1 Recombinant Antibody (CBYY-I2057) (CBMAB-I3227-YY)

This product is Mouse antibody that recognizes IDH1. The antibody CBYY-I2057 can be used for immunoassay techniques such as: WB, IHC
See all IDH1 antibodies
Published Data

Summary

Host Animal
Mouse
Specificity
Human, Dog, Rat, Mouse
Clone
CBYY-I2057
Antibody Isotype
IgG1
Application
WB, IHC

Basic Information

Immunogen
Synthetic peptide around the R132H mutation region of the human IDH conjugated to KLH
Specificity
Human, Dog, Rat, Mouse
Antibody Isotype
IgG1
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, PH 7.3, 1% BSA, 50% glycerol
Preservative
0.02% sodium azide
Concentration
1 mg/ml
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Isocitrate Dehydrogenase (NADP(+)) 1, Cytosolic
Introduction
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.
Entrez Gene ID
Human3417
Mouse15926
Rat24479
Dog478889
UniProt ID
HumanO75874
MouseO88844
RatP41562
DogF1PZA1
Alternative Names
Isocitrate Dehydrogenase (NADP(+)) 1, Cytosolic
Biological Process
2-oxoglutarate metabolic process Source: UniProtKB
Female gonad development Source: Ensembl
Glutathione metabolic process Source: Ensembl
Glyoxylate cycle Source: UniProtKB-KW
Isocitrate metabolic process Source: UniProtKB
NADP metabolic process Source: GO_Central
Regulation of phospholipid biosynthetic process Source: Ensembl
Regulation of phospholipid catabolic process Source: Ensembl
Response to oxidative stress Source: Ensembl
Response to steroid hormone Source: Ensembl
Tricarboxylic acid cycle Source: UniProtKB-KW
Cellular Location
Peroxisome; Cytosol
Involvement in disease
Glioma (GLM):
The gene represented in this entry is involved in disease pathogenesis. Mutations affecting Arg-132 are tissue-specific, and suggest that this residue plays a unique role in the development of high-grade gliomas. Mutations of Arg-132 to Cys, His, Leu or Ser abolish magnesium binding and abolish the conversion of isocitrate to alpha-ketoglutarate. Instead, alpha-ketoglutarate is converted to R(-)-2-hydroxyglutarate. Elevated levels of R(-)-2-hydroxyglutarate are correlated with an elevated risk of malignant brain tumors. Gliomas are benign or malignant central nervous system neoplasms derived from glial cells. They comprise astrocytomas and glioblastoma multiforme that are derived from astrocytes, oligodendrogliomas derived from oligodendrocytes and ependymomas derived from ependymocytes. Genetic variations are associated with cartilaginous tumors such as enchondroma or chondrosarcoma. Mutations of Arg-132 to Cys, Gly or His abolish the conversion of isocitrate to alpha-ketoglutarate. Instead, alpha-ketoglutarate is converted to R(-)-2-hydroxyglutarate.
PTM
Acetylation at Lys-374 dramatically reduces catalytic activity.

Sabo, K. A., Albekioni, E., Caliger, D., Coleman, N. J., Thornberg, E., Avellaneda Matteo, D., ... & Sohl, C. D. (2023). Capturing the Dynamic Conformational Changes of Human Isocitrate Dehydrogenase 1 (IDH1) upon Ligand and Metal Binding Using Hydrogen–Deuterium Exchange Mass Spectrometry. Biochemistry, 62(6), 1145-1159.

Reinbold, R., Hvinden, I. C., Rabe, P., Herold, R. A., Finch, A., Wood, J., ... & Schofield, C. J. (2022). Resistance to the isocitrate dehydrogenase 1 mutant inhibitor ivosidenib can be overcome by alternative dimer-interface binding inhibitors. Nature Communications, 13(1), 4785.

Herold, R. A., Reinbold, R., Megarity, C. F., Abboud, M. I., Schofield, C. J., & Armstrong, F. A. (2021). Exploiting electrode nanoconfinement to investigate the catalytic properties of isocitrate dehydrogenase (IDH1) and a cancer-associated variant. The Journal of Physical Chemistry Letters, 12(26), 6095-6101.

Liu, S., Abboud, M. I., John, T., Mikhailov, V., Hvinden, I., Walsby-Tickle, J., ... & Schofield, C. J. (2021). Roles of metal ions in the selective inhibition of oncogenic variants of isocitrate dehydrogenase 1. Communications Biology, 4(1), 1243.

Bruce-Brand, C., & Govender, D. (2020). Gene of the month: IDH1. Journal of Clinical Pathology, 73(10), 611-615.

Bhavya, B., Anand, C. R., Madhusoodanan, U. K., Rajalakshmi, P., Krishnakumar, K., Easwer, H. V., ... & Gopala, S. (2020). To be wild or mutant: role of isocitrate dehydrogenase 1 (IDH1) and 2-hydroxy glutarate (2-HG) in gliomagenesis and treatment outcome in glioma. Cellular and molecular neurobiology, 40, 53-63.

Luna, L. A., Lesecq, Z., White, K. A., Hoang, A., Scott, D. A., Zagnitko, O., ... & Sohl, C. D. (2020). An acidic residue buried in the dimer interface of isocitrate dehydrogenase 1 (IDH1) helps regulate catalysis and pH sensitivity. Biochemical journal, 477(16), 2999-3018.

Verdura, S., Cuyàs, E., Lozano-Sánchez, J., Bastidas-Velez, C., Llorach-Parés, L., Fernández-Arroyo, S., ... & Menendez, J. A. (2019). An olive oil phenolic is a new chemotype of mutant isocitrate dehydrogenase 1 (IDH1) inhibitors. Carcinogenesis, 40(1), 27-40.

Jakob, C. G., Upadhyay, A. K., Donner, P. L., Nicholl, E., Addo, S. N., Qiu, W., ... & Hutti, J. E. (2018). Novel modes of inhibition of wild-type isocitrate dehydrogenase 1 (IDH1): direct covalent modification of His315. Journal of Medicinal Chemistry, 61(15), 6647-6657.

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For research use only. Not intended for any clinical use.

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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