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Sarcosine oxidase (SAO) is an enzyme that catalyzes the oxidative demethylation of sarcosine to yield glycine, H2O2, 5, 10-CH2-tetrahydrofolate in a reaction requiring H4-tetrahydrofolate and oxygen. sarcosine + H2O + O2 = glycine + formaldehyde + H2O2.http://www.creative-enzymes.com/product/Native-Microorganism-Sarcosine-Oxidase_767.html
Xanthine oxidase is a form of xanthine oxidoreductase, a type of enzyme that generates reactive oxygen species. These enzymes catalyze the oxidation of hypoxanthine to xanthine and can further catalyze the oxidation of xanthine to uric acid. These enzymes play an important role in the catabolism of purines in some species, including humans.http://www.creative-enzymes.com/product/Native-Microorganism-Xanthine-Oxidase_814.html
In enzymology, a glycerol-3-phosphate oxidase (EC 1.1.3.21) is an enzyme that catalyzes the chemical reaction: sn-glycerol 3-phosphate + O2↔ glycerone phosphate + H2O2. Thus, the two substrates of this enzyme are sn-glycerol 3-phosphate and O2, whereas its two products are glycerone phosphate and H2O2.http://www.creative-enzymes.com/product/Native-Pediococcus-Sp-Glycerol3phosphate-Oxidase_750.html
In enzymology, a glycerol-3-phosphate oxidase (EC 1.1.3.21) is an enzyme that catalyzes the chemical reaction: sn-glycerol 3-phosphate + O2 ↔ glycerone phosphate + H2O2. Thus, the two substrates of this enzyme are sn-glycerol 3-phosphate and O2, whereas its two products are glycerone phosphate and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. This enzyme participates in glycerophospholipid metabolism. It employs one cofactor, FAD.http://www.creative-enzymes.com/product/Native-Pediococcus-Sp-L-glycerophosphate-Oxidase_795.html
In enzymology, an alcohol oxidase (EC 1.1.3.13) is an enzyme that catalyzes the chemical reaction:a primary alcohol + O2↔ an aldehyde + H2O2. Thus, the two substRates of this enzyme are primary alcohol and O2, whereas its two products are aldehyde and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. It employs one cofactor, FAD.http://www.creative-enzymes.com/product/Native-Pichia-Pastoris-Alcohol-Oxidase_1050.html
Aconitase catalyses the stereo-specific isomerization of citRate to isocitRate via cis-aconitate in the tricarboxylic acid cycle. Aconitase is inhibited by cyanide, sulfide and copper and mercury at low concentRations. It is competitively inhibited by trans-aconitate. Aconitase contains an internal Fe-S cluster which is responsible for its activity.http://www.creative-enzymes.com/product/Native-Porcine-Aconitase_1037.html
In enzymology, an aminoacylase (EC 3.5.1.14) is an enzyme that catalyzes the chemical reaction:N-acyl-L-amino acid + H2O↔ carboxylate + L-amino acid. Thus, the two substRates of this enzyme are N-acyl-L-amino acid and H2O, whereas its two products are carboxylate and L-amino acid. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. This enzyme participates in urea cycle and metabolism of amino groups.http://www.creative-enzymes.com/product/Native-Porcine-Acylase-I_1040.html
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