SRP5187
HSD17B10, GST tagged human
recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution
Synonym(s):
17b-HSD10, ABAD, ERAB, HADH2, HCD2, MHBD, SCHAD
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50 μG
$362.00
$362.00
Usually ships in 2 weeks.
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50 μG
$362.00
About This Item
$362.00
Usually ships in 2 weeks.
biological source
human
recombinant
expressed in baculovirus infected Sf9 cells
assay
≥70% (SDS-PAGE)
form
buffered aqueous glycerol solution
mol wt
~51 kDa
NCBI accession no.
application(s)
cell analysis
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... HSD17B10(3028)
General description
HSD17B10 gene encodes the protein 17-beta-hydroxysteroid dehydrogenase 10 that is a member of the short-chain dehydrogenase/reductase superfamily SCHAD. HSD17B10 gene product is a mitochondrial protein that is involved in lipid metabolism, fatty acid oxidation and steroid hormone metabolism. HSD17B10 protein has been implicated in the development of Alzheimer′s disease and mutations in the gene are the cause of 2-methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency (MHBD). Furthermore, HSD17B10 may act as a direct molecular link between beta-amyloid and mitochondrial toxicity.
Physical form
Supplied in 50mM Tris-HCl, pH 7.5, 150mM NaCl, 10mM glutathione, 0.1mM EDTA, 0.25mM DTT, 0.1mM PMSF, 25% glycerol.
Preparation Note
after opening, aliquot into smaller quantities and store at -70 °C. Avoid repeating handling and multiple freeze/thaw cycles
Storage Class
10 - Combustible liquids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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Song-Yu Yang et al.
Trends in endocrinology and metabolism: TEM, 16(4), 167-175 (2005-04-30)
Human 17beta-hydroxysteroid dehydrogenase type 10 (17beta-HSD10) is a mitochondrial enzyme encoded by the SCHAD gene, which escapes chromosome X inactivation. 17Beta-HSD10/SCHAD mutations cause a spectrum of clinical conditions, from mild mental retardation to progressive infantile neurodegeneration. 17Beta-HSD10/SCHAD is essential for
Joyce W Lustbader et al.
Science (New York, N.Y.), 304(5669), 448-452 (2004-04-17)
Mitochondrial dysfunction is a hallmark of beta-amyloid (Abeta)-induced neuronal toxicity in Alzheimer's disease (AD). Here, we demonstrate that Abeta-binding alcohol dehydrogenase (ABAD) is a direct molecular link from Abeta to mitochondrial toxicity. Abeta interacts with ABAD in the mitochondria of
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