G6880
α-Glycerophosphate Dehydrogenase from rabbit muscle
Type X, lyophilized powder, ≥100 units/mg protein
Sinónimos:
sn-Glycerol-3-phosphate Dehydrogenase from rabbit muscle, sn-Glycerol-3-phosphate:NAD+ 2-oxidoreductase
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Número CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-982-3
MDL number:
Specific activity:
≥100 units/mg protein
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Type X
Quality Level
form
lyophilized powder
specific activity
≥100 units/mg protein
composition
Protein, ≥75%
foreign activity
Lactic dehydrogenase, pyruvate kinase, aldolase, and glyceraldehyde-3-phosphate dehydrogenase ≤0.01%, Triosephosphate isomerase ≤0.02%
shipped in
wet ice
storage temp.
−20°C
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Application
α-glycerophosphate dehydrogenase was used in 2-deoxy-ribose 5-phosphate aldolase (DERA) cleavage (retroaldol) assay.
Biochem/physiol Actions
α-glycerophosphate dehydrogenase catalyzes the conversion of dihydroxyacetone to glycerol phosphate.
Physical form
Lyophilized sulfate-free powder containing buffer salts as citrate and EDTA
Analysis Note
Protein determined by biuret
Other Notes
One unit will convert 1.0 μmole of dihydroxyacetone phosphate to α-glycerophosphate per min at pH 7.4 at 25 °C.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Clase de almacenamiento
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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Grace DeSantis et al.
Bioorganic & medicinal chemistry, 11(1), 43-52 (2002-12-07)
2-Deoxyribose-5-phosphate aldolase (DERA, EC 4.1.2.4) catalyzes the reversible aldol reaction between acetaldehyde and D-glyceraldehyde-3-phosphate to generate D-2-deoxyribose-5-phosphate. It is unique among the aldolases as it catalyzes the reversible asymmetric aldol addition reaction of two aldehydes. In order to expand the
Yongxiu Fan et al.
Parasitology research, 109(3), 621-626 (2011-03-17)
Glycerol 3-phosphate dehydrogenase (GPD) plays an important role in the energy metabolism and nutrition metabolism. In order to know about the biological functions of GPD of Clonorchis sinensis (C. sinensis), we identified a complete gene coding GPD from C. sinensis
Vishist K Jain et al.
Applied microbiology and biotechnology, 93(1), 131-141 (2011-07-02)
Saccharomyces cerevisiae maintains a redox balance under fermentative growth conditions by re-oxidizing NADH formed during glycolysis through ethanol formation. Excess NADH stimulates the synthesis of mainly glycerol, but also of other compounds. Here, we investigated the production of primary and
Branka Stirn Kranjc et al.
Graefe's archive for clinical and experimental ophthalmology = Albrecht von Graefes Archiv fur klinische und experimentelle Ophthalmologie, 247(11), 1505-1515 (2009-07-18)
To compare the organization of human and rat ocular medial recti muscles (MR). The cryosections of human and rat MR were processed for myofibrillar ATPase (mATPase), succinate dehydrogenase and glycerol-3-phosphate dehydrogenase. To reveal myosin heavy chain (MyHC) isoforms, specific monoclonal
Zhong-peng Guo et al.
Journal of industrial microbiology & biotechnology, 38(8), 935-943 (2010-09-09)
The GPD2 gene, encoding NAD(+)-dependent glycerol-3-phosphate dehydrogenase in an industrial ethanol-producing strain of Saccharomyces cerevisiae, was deleted. And then, either the non-phosphorylating NADP(+)-dependent glyceraldehyde-3-phosphate dehydrogenase (GAPN) from Bacillus cereus, or the NADP(+)-dependent glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from Kluyveromyces lactis, was expressed
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