Ugrás a tartalomra
Merck

SAB4200548

Sigma-Aldrich

Anti-IDH1 (R132H) antibody, Mouse monoclonal

clone HMab-1, purified from hybridoma cell culture

Szinonimák:

Idh1 R132H Antibody, Idh1 R132H Antibody - Anti-IDH1 (R132H) antibody, Mouse monoclonal, Anti-IDCD, Anti-IDH, Anti-IDP, Anti-IDPC, Anti-Isocitrate dehydrogenase 1 (NADP+), soluble, Anti-NADP(+)-specific ICDH, Anti-NADP-dependent isocitrate dehydrogenase, cytosolic, Anti-NADP-dependent isocitrate dehydrogenase, peroxisomal, Anti-Oxalosuccinate decarboxylase, Anti-PICD

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

UNSPSC kód:
12352203
NACRES:
NA.41

biológiai forrás

mouse

Minőségi szint

konjugátum

unconjugated

antitest forma

purified immunoglobulin

antitest terméktípus

primary antibodies

klón

HMab-1, monoclonal

form

buffered aqueous solution

molekulatömeg

antigen ~43 kDa

faj reaktivitás

human

koncentráció

~1.0 mg/mL

technika/technikák

western blot: 4.0-8.0 μg/mL using extract of HEK-293T cells overexpressing IDH1R132H.

UniProt elérési szám

alkalmazás(ok)

research pathology

kiszállítva

dry ice

tárolási hőmérséklet

−20°C

célzott transzláció utáni módosítás

unmodified

Géninformáció

human ... IDH1(3417)

Általános leírás

Anti-IDH1 (R132H) antibody, Mouse monoclonal (mouse IgG1 isotype) is derived from the hybridoma HMab1 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a peptide corresponding to mutation R132H of human IDH1. A member of isocitrate dehydrogenase (IDH) family, IDH1, is the human cytoplasmic NADP-specific enzyme. Its subcellular localization was shown to be in both peroxisomes and the cytoplasm.

Immunogen

peptide corresponding to mutation R132H of human IDH1.

Alkalmazás

Anti-IDH1 (R132H) antibody has been used:
  • in immunoblotting
  • in immunohistochemistry
  • in western blotting
  • in cell cycle analysis and apoptosis assays
  • in chromatin immunoprecipitation (ChIP) assay
  • in in vitro migration assay

Biokémiai/fiziológiai hatások

Isocitrate dehydrogenase 1 (IDH1) catalyzes the oxidative decarboxylation of isocitrate into α α -KG) using NADP as co-substrate. Mutations in IDH1 are specific to Arg132 (R132) and endow them with the function of generating 2-hydroxyglutarate (2HG) instead of α-KG. This product alters gene transcription through effects on DNA and histone methylation. Several IDH1 mutations exist, including R132H, R132C, R132S, R132G and R132L. Each may result in different tumor type with varied malignant progression. The most frequent known mutation (>90%) is the alteration of arginine to histidine (R132H). Hence, antibodies that recognize the IDH1R132H mutation can be useful for the diagnosis of mutation-bearing tumors like gliomas.

Fizikai forma

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Jogi nyilatkozat

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Tárolási osztály kódja

10 - Combustible liquids

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable


Analitikai tanúsítványok (COA)

Analitikai tanúsítványok (COA) keresése a termék sarzs-/tételszámának megadásával. A sarzs- és tételszámok a termék címkéjén találhatók, a „Lot” vagy „Batch” szavak után.

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Peroxisomal localization and function of NADP+-specific isocitrate dehydrogenases in yeast
Lu Q and McAlister-H L.
Archives of Biochemistry and Biophysics, 493(2), 125-134 (2010)
Expression of Idh1R132H in the murine subventricular zone stem cell niche recapitulates features of early gliomagenesis
Bardella C, et al.
Cancer Cell, 30(4), 578-594 (2016)
IDH1R132H decreases the proliferation of U87 glioma cells through upregulation of microRNA-128a
Nie Q M, et al.
Molecular Medicine Reports, 12(5), 6695-6701 (2015)
Bin Sheng Wong et al.
Nature biomedical engineering, 5(1), 26-40 (2020-09-30)
Clinical scores, molecular markers and cellular phenotypes have been used to predict the clinical outcomes of patients with glioblastoma. However, their clinical use has been hampered by confounders such as patient co-morbidities, by the tumoral heterogeneity of molecular and cellular
Shuchen Chen et al.
Cancer medicine, 11(22), 4122-4133 (2022-05-09)
Isocitrate dehydrogenase (IDH) is an appealing target for anticancer therapy, and IDH (IDH1/2) inhibitors have been approved for targeted therapy of acute myeloid leukemia (AML) and Cholangiocarcinoma. The therapeutic potential of IDH inhibitors for non-small-cell lung cancer (NSCLC) patients is

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