GLDA E.coli, Active
Source: Escherichia Coli.Sterile Filtered colorless solution.Glycerol dehydrogenase (GldA) catalyzes the NAD-dependent oxidation of glycerol to dihydroxyacetone (glycerone) . The GldA protein allows microorganisms to use glycerol as a Source: of carbon under anaerobic conditions. Furthermore, in E.coli GldA has an imperative role by regulating the intracellular level of dihydroxyacetone by catalyzing the reverse reaction, i.e. the conversion of dihydroxyacetone into glycerol. GldA possesses an extensive substrate specificity, due to its ability to oxidize 1,2-propanediol and to reduce glycolaldehyde, methylglyoxal and hydroxyacetone into ethylene glycol, lactaldehyde and 1,2-propanediol, respectively.GLDA E.coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 390 amino acids (1-367 a.a) and having a molecular mass of 41.1kDa. GLDA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specifications
Product Name Alternative
ECK3937, JW5556, Glycerol dehydrogenase, GDH, GLDH, b3945.
Applications
Functional Assay
Purification
Greater than 95.0% as determined by SDS-PAGE.
Components
GLDA protein solution (1mg/mL) containing Phosphate buffered saline (pH7.4) and 10% glycerol.
Storage Conditions
Applications Notes
Specific activity: > 14 Units/ml. One unit will oxidize 1.0 umole of glycerol to dihydroxyacetone per minute at pH 8.0 at 25C.
Amino Acids
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