Human IDH1 Protein 2854

$270.00 – $900.00

Summary

Expression: E.coli
Pure: Yes (HPLC)
Amino Acid Range: Ser2-Leu414

SKU: 2854parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	O75874
express system	E.coli
product tag	C-His
purity	> 95% as determined by Tris-Bis PAGE;> 90% as determined by HPLC
background	Isocitrate dehydrogenase (IDH) is a metabolic enzyme that converts isocitrate to α-ketoglutarate (α-KG). Genetic gain-of-function mutations in IDH1 and IDH2 confer a neomorphic activity that allow reduction of α -KG to (R)-2- hydroxyglutarate, the accumulation of which results in the development of cancers like low grade gliomas and leukemia.Isocitrate dehydrogenase 1 (IDH1) is the most frequently mutated metabolic gene in cancer.
molecular weight	The protein has a predicted MW of 47.35 kDa same as Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Human IDH1 Protein 2854

protein

Size and concentration 100, 500µg and liquid
Form Liquid
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped with dry ice.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
Isocitrate dehydrogenase (IDH) is a metabolic enzyme that converts isocitrate to α-ketoglutarate (α-KG). Genetic gain-of-function mutations in IDH1 and IDH2 confer a neomorphic activity that allow reduction of α -KG to (R)-2- hydroxyglutarate, the accumulation of which results in the development of cancers like low grade gliomas and leukemia.Isocitrate dehydrogenase 1 (IDH1) is the most frequently mutated metabolic gene in cancer.
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.
Target Relevance information above includes information from UniProt accession: O75874
The UniProt Consortium

Data

The purity of Human IDH1 is greater than 95% as determined by SEC-HPLC.

Human IDH1 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

pmid	title	authors	citation
We haven't added any publications to our database yet.

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.