Immunohistochemistry (IHC) : Formalin-fixed, paraffin-embedded human glioma stained with anti-IHD1 antibody using peroxidase-conjugate and DAB chromogen. Note nuclear and cytoplasmic staining of infiltrating glioma cells whereas normal glial cells are negative

rabbit anti-IDH1 (R132H) monoclonal antibody (ZR7) 6220

$160.00 – $528.00

Antibody summary

Rabbit monoclonal to IDH1 (R132H)
Suitable for: Immunohistochemistry (formalin-fixed, paraffin-embedded tissues)
Reacts with: Human
Isotype:IgG
Control: Infiltrating glioma
Visualization: Nuclear
0.1, 0.5, 1.0 mL concentrated, 7 mL prediluted

SKU: 6220parent Category: antibody Tags: anatomy, IDH1 (R132H), monoclonal, Neuropathology/Endocrine

Weight	1 lbs
Dimensions	9 × 5 × 2 in
host	mouse
isotype	IgG
clonality	monoclonal
concentration	concentrate, predilute
applications	IHC
reactivity	human
available size	0.1 mL, 0.5 mL, 1 mL concentrated, 7 mL prediluted

rabbit anti-IDH1 (R132H) monoclonal antibody ZR7 6220

antibody
Database link: human O75874
Tested applications IHC
Recommended dilutions As directed
Immunogen Recombinant fragment of human IDH1 (exact sequence is proprietary)
Size and concentration 7 mL prediluted or 0.1, 0.5, 1.0 mL and concentrated
Form liquid
Storage Instructions 2-8°C for short term, for longer term at -20°C. Avoid freeze / thaw cycles.
Purity affinity purified
Clonality monoclonal
Isotype IgG
Compatible secondaries goat anti-rabbit IgG, H&L chain specific, peroxidase conjugated, conjugated polyclonal antibody 9512 goat anti-rabbit IgG, H&L chain specific, biotin conjugated polyclonal antibody 2079 goat anti-rabbit IgG, H&L chain specific, FITC conjugated polyclonal antibody 7863 goat anti-rabbit IgG, H&L chain specific, Cross Absorbed polyclonal antibody 2371 goat anti-rabbit IgG, H&L chain specific, biotin conjugated polyclonal antibody, crossabsorbed 1715 goat anti-rabbit IgG, H&L chain specific, FITC conjugated polyclonal antibody, crossabsorbed 1720
Isotype control Rabbit polyclonal - Isotype Control

target relevance
Protein names Isocitrate dehydrogenase [NADP] cytoplasmic (IDH) (IDH1) (EC 1.1.1.42) (Cytosolic NADP-isocitrate dehydrogenase) (IDPc) (NADP(+)-specific ICDH) (Oxalosuccinate decarboxylase)
Gene names IDH1,IDH1 PICD
Protein family Isocitrate and isopropylmalate dehydrogenases family
Mass 9606Da
Function Catalyzes the NADP(+)-dependent oxidative decarboxylation of isocitrate (D-threo-isocitrate) to 2-ketoglutarate (2-oxoglutarate), which is required by other enzymes such as the phytanoyl-CoA dioxygenase (PubMed:10521434, PubMed:19935646). Plays a critical role in the generation of NADPH, an important cofactor in many biosynthesis pathways (PubMed:10521434). May act as a corneal epithelial crystallin and may be involved in maintaining corneal epithelial transparency (By similarity).
Catalytic activity BINDING 75..77; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000269\|PubMed:15173171, ECO:0000269\|PubMed:19935646, ECO:0007744\|PDB:1T09, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM, ECO:0007744\|PDB:3MAP, ECO:0007744\|PDB:3MAR, ECO:0007744\|PDB:3MAS, ECO:0007744\|PDB:4I3K, ECO:0007744\|PDB:4I3L, ECO:0007744\|PDB:4KZO, ECO:0007744\|PDB:4L03, ECO:0007744\|PDB:4L04, ECO:0007744\|PDB:4L06, ECO:0007744\|PDB:4UMX, ECO:0007744\|PDB:4UMY, ECO:0007744\|PDB:4XRX, ECO:0007744\|PDB:4XS3, ECO:0007744\|PDB:5DE1, ECO:0007744\|PDB:5L57, ECO:0007744\|PDB:5L58, ECO:0007744\|PDB:5LGE, ECO:0007744\|PDB:5SUN, ECO:0007744\|PDB:5SVF, ECO:0007744\|PDB:5TQH"; BINDING 77; /ligand="substrate"; /ligand_note="ligand shared between two neighboring subunits"; /note="in other chain"; /evidence="ECO:0000269\|PubMed:15173171, ECO:0007744\|PDB:1T0L"; BINDING 82; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000269\|PubMed:15173171, ECO:0000269\|PubMed:19935646, ECO:0007744\|PDB:1T09, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM, ECO:0007744\|PDB:3MAP, ECO:0007744\|PDB:3MAR, ECO:0007744\|PDB:3MAS, ECO:0007744\|PDB:4I3K, ECO:0007744\|PDB:4I3L, ECO:0007744\|PDB:4KZO, ECO:0007744\|PDB:4L03, ECO:0007744\|PDB:4L04, ECO:0007744\|PDB:4L06, ECO:0007744\|PDB:4UMX, ECO:0007744\|PDB:4UMY, ECO:0007744\|PDB:4XRX, ECO:0007744\|PDB:4XS3, ECO:0007744\|PDB:5DE1, ECO:0007744\|PDB:5L57, ECO:0007744\|PDB:5LGE, ECO:0007744\|PDB:5SUN, ECO:0007744\|PDB:5SVF, ECO:0007744\|PDB:5TQH"; BINDING 94..100; /ligand="substrate"; /ligand_note="ligand shared between two neighboring subunits"; /note="in other chain"; /evidence="ECO:0000269\|PubMed:15173171, ECO:0007744\|PDB:1T0L"; BINDING 109; /ligand="substrate"; /ligand_note="ligand shared between two neighboring subunits"; /note="in other chain"; /evidence="ECO:0000269\|PubMed:15173171, ECO:0007744\|PDB:1T0L"; BINDING 132; /ligand="substrate"; /ligand_note="ligand shared between two neighboring subunits"; /note="in other chain"; /evidence="ECO:0000269\|PubMed:15173171, ECO:0007744\|PDB:1T0L"; BINDING 212; /ligand="substrate"; /ligand_note="ligand shared between two neighboring subunits"; /evidence="ECO:0000269\|PubMed:15173171, ECO:0007744\|PDB:1T0L"; BINDING 252; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_note="ligand shared between two neighboring subunits"; /evidence="ECO:0000305\|PubMed:15173171, ECO:0000305\|PubMed:19935646, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM"; BINDING 260; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000269\|PubMed:15173171, ECO:0000269\|PubMed:19935646, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM"; BINDING 275; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_note="ligand shared between two neighboring subunits"; /note="in other chain"; /evidence="ECO:0000305\|PubMed:15173171, ECO:0000305\|PubMed:19935646, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM"; BINDING 279; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_note="ligand shared between two neighboring subunits"; /note="in other chain"; /evidence="ECO:0000305\|PubMed:15173171, ECO:0000305\|PubMed:19935646, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM"; BINDING 310..315; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000269\|PubMed:15173171, ECO:0000269\|PubMed:19935646, ECO:0007744\|PDB:1T09, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM, ECO:0007744\|PDB:3MAP, ECO:0007744\|PDB:3MAR, ECO:0007744\|PDB:3MAS, ECO:0007744\|PDB:4I3K, ECO:0007744\|PDB:4I3L, ECO:0007744\|PDB:4KZO, ECO:0007744\|PDB:4L03, ECO:0007744\|PDB:4L04, ECO:0007744\|PDB:4L06, ECO:0007744\|PDB:4UMX, ECO:0007744\|PDB:4UMY, ECO:0007744\|PDB:4XRX, ECO:0007744\|PDB:4XS3, ECO:0007744\|PDB:5DE1, ECO:0007744\|PDB:5L57, ECO:0007744\|PDB:5L58, ECO:0007744\|PDB:5LGE, ECO:0007744\|PDB:5SUN, ECO:0007744\|PDB:5SVF, ECO:0007744\|PDB:5TQH"; BINDING 328; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000269\|PubMed:15173171, ECO:0000269\|PubMed:19935646, ECO:0007744\|PDB:1T09, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM, ECO:0007744\|PDB:3MAP, ECO:0007744\|PDB:3MAR, ECO:0007744\|PDB:3MAS, ECO:0007744\|PDB:4I3K, ECO:0007744\|PDB:4I3L, ECO:0007744\|PDB:4KZO, ECO:0007744\|PDB:4L03, ECO:0007744\|PDB:4L04, ECO:0007744\|PDB:4L06, ECO:0007744\|PDB:4UMX, ECO:0007744\|PDB:4UMY, ECO:0007744\|PDB:4XRX, ECO:0007744\|PDB:4XS3, ECO:0007744\|PDB:5DE1, ECO:0007744\|PDB:5L57, ECO:0007744\|PDB:5L58, ECO:0007744\|PDB:5LGE, ECO:0007744\|PDB:5SUN, ECO:0007744\|PDB:5SVF, ECO:0007744\|PDB:5TQH"
Subellular location Cytoplasm, cytosol. Peroxisome .
Structure Homodimer.
Post-translational modification Acetylation at Lys-374 dramatically reduces catalytic activity.
Involvement in disease DISEASE: Glioma (GLM) [MIM:137800]: 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. Note=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.; DISEASE: Note=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.
Target Relevance information above includes information from UniProt accession: O75874
The UniProt Consortium

Data

Formalin-fixed, paraffin-embedded human glioma stained with anti-IHD1 antibody using peroxidase-conjugate and DAB chromogen. Note nuclear and cytoplasmic staining of infiltrating glioma cells whereas normal glial cells are negative

Publications

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.