94577
DL-α-Hydroxyglutaric acid disodium salt
≥95.0% (GC)
Synonym(s):
(RS)-2-Hydroxypentanedioic acid disodium salt, Disodium 2-hydroxyglutarate
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About This Item
Linear Formula:
C5H6O5Na2
CAS Number:
Molecular Weight:
192.08
NACRES:
NA.28
PubChem Substance ID:
UNSPSC Code:
12352204
MDL number:
Product Name
DL-α-Hydroxyglutaric acid disodium salt, ≥95.0% (GC)
InChI key
DZHFTEDSQFPDPP-UHFFFAOYSA-L
SMILES string
[Na+].[Na+].OC(CCC([O-])=O)C([O-])=O
InChI
1S/C5H8O5.2Na/c6-3(5(9)10)1-2-4(7)8;;/h3,6H,1-2H2,(H,7,8)(H,9,10);;/q;2*+1/p-2
assay
≥95.0% (GC)
form
powder or crystals
impurities
≤6.0% water
storage temp.
2-8°C
2-8°C
Quality Level
Related Categories
Biochem/physiol Actions
D-(or R-) enantiomer of α-hydroxyglutaric acid is a cancer related biomarker of diagnostic value, whereas the L-(or S-) enantiomer of α-hydroxyglutaric acid is a biomarker for certain neurometabolic, inherited disorder diseases. It has no known physiological function in eukaryotes. It is toxic to the brain and increases the susceptibility to develop brain tumors.
Packaging
Bottomless glass bottle. Contents are inside inserted fused cone.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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Cancer: A metabolic metamorphosis.
Abigail S Krall et al.
Nature, 496(7443), 38-40 (2013-04-05)
Jelena Lazovic et al.
Neuro-oncology, 14(12), 1465-1472 (2012-10-24)
The arginine 132 (R132) mutation of isocitrate dehydrogenase -1 (IDH1(R132)) results in production of 2-hydroxyglutarate (2-HG) and is associated with a better prognosis compared with wild-type (WT) in glioma patients. The majority of lower-grade gliomas express IDH1(R132), whereas this mutation
Cancer-associated IDH mutations: biomarker and therapeutic opportunities
K E Yen
Oncogene (2010)
Cancer-associated IDH1 mutations produce 2-hydroxyglutarate
Lenny Dang
Nature (2009)
Fang Wang et al.
Science (New York, N.Y.), 340(6132), 622-626 (2013-04-06)
A number of human cancers harbor somatic point mutations in the genes encoding isocitrate dehydrogenases 1 and 2 (IDH1 and IDH2). These mutations alter residues in the enzyme active sites and confer a gain-of-function in cancer cells, resulting in the
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