Enzymes play a key role in the metabolic activities of all organisms from human to microbial. The abnormality in metabolism leads to many metabolic disorders. Studies have shown that many metabolic disorders are resulted from enzyme deficiency. Enzymes also have a wide range of applications in microbial biotechnology and the diagnosis process. They have been widely used in clinical examination as preferred markers in disease states such as myocardial infarction, jaundice, pancreatitis, cancer, neurodegenerative disorders, etc. They provide insight into the disease process through the ability of diagnosis, prognosis, and assessment of response therapy.
|Cat No.||Product Name||Activity||Appearance||EC No.||CAS No.||Inquiry|
|DIA-135||Native Microorganism Cholesterol Esterase||5.0U/mg-solid or more||Light brown amorphous powder, lyophilized||EC 22.214.171.124||9026-00-0||Get a quote|
|DIA-136||Native Pseudomonas sp. Cholesterol Oxidase||15 U/mg-solid or more (contg. approx. 40% of stabilizers)||Yellowish amorphous powder, lyophilized||EC 126.96.36.199||9026-00-0|
|DIA-138||Native Microorganism Cholesterol Oxidase||12U/mg-solid or more||Yellowish amorphous powder, lyophilized||EC 188.8.131.52||9028-76-6|
|DIA-145||Native Microorganism Glucose-6-phosphate Dehydrogenase||200U/mg-solid or more||White amorphous powder, lyophilized||EC 184.108.40.206||9001-40-5|
|DIA-181||Native Microorganism Alkaline phosphatase||Protein concentration is approximately 20 mg/ml.||Inquiry||EC 220.127.116.11||9001-78-9|
|DIA-182||Native Microorganism N-Acetylneuraminic acid aldolase||15U/mg-solid or more (30U/mg-protein or more), (containing approx. 30% of stabilizers)||Yellowish amorphous powder, lyophilized||EC 18.104.22.168||9027-60-5|
|DIA-190||Native Rhizopus sp. Glucoamylase||30U/mg-solid or more||White amorphous powder (salt-free), lyophilized||EC 22.214.171.124||9032-08-0|
|DIA-199||Native Pediococcus sp. L-α-glycerophosphate oxidase||40 U/mg-solid or more (containing approx. 40% of stabilizers)||Yellowish amorphous powder, lyophilized||EC 126.96.36.199||9046-28-0|
|DIA-202||Native Microorganism Hexokinase||150U/mg-solid or more||White amorphous powder, lyophilized||EC 188.8.131.52||9001-51-8|
|DIA-208||Native Microorganism Lactate oxidase||80U/mg-solid or more||Yellowish amorphous powder, lyophilized||EC 184.108.40.206||9028-72-2|
|DIA-211||Native Microorganism Lipoprotein lipase||1.0U/mg-solid or more||Light brown amorphous powder, lyophilized||EC 220.127.116.11||9004-02-8|
|DIA-213||Native Flavobacterium sp. Proline specific endopeptidase||5.0U/mg-solid or more||White amorphous powder, lyophilized||EC 18.104.22.168||72162-84-6|
|DIA-218||Native Microorganism Xanthine oxidase||10U/mg-solid or more||Reddish brown amorphous powder, lyophilized||EC 22.214.171.124||9054-84-6|
|DIA-275||Diaphorase from microorganism||500U/mg-solid or more||Inquiry||EC 1.6.99.-||9001-18-7|
Sterol esterase, also known as cholesterol esterase, belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is steryl-ester acylhydrolase. This enzyme participates in bile acid biosynthesis. DIA-135 is useful for enzymatic determination of total cholesterol when coupled with cholesterol oxidase in clinical analysis.
Cholesterol oxidase belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donors with oxygen as acceptor. The systematic name of this enzyme class is cholesterol:oxygen oxidoreductase. This enzyme participates in bile acid biosynthesis. DIA-136 is useful for enzymatic determination of cholesterol in serum when coupled with cholesterol esterase in clinical analysis.
Cholesterol oxidase belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donors with oxygen as acceptor. The systematic name of this enzyme class is cholesterol:oxygen oxidoreductase. This enzyme participates in bile acid biosynthesis. DIA-138 is useful for enzymatic determination of cholesterol in serum when coupled with cholesterol esterase in clinical analysis.
Glucose-6-phosphate dehydrogenase (G6PD or G6PDH) is a cytosolic enzyme that catalyzes the chemical reaction: D-glucose-6-phosphate + NADP+ ↔ 6-phospho-D-glucono-1,5-lactone + NADPH + H+. This enzyme is in the pentose phosphate pathway, a metabolic pathway that supplies reducing energy to cells (such as erythrocytes) by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH). DIA-145 is useful for enzymatic determination of NAD+(NADP+) and G-6-P, and activities of phosphoglucose isomerase, phosphoglucomutase and hexokinase. The enzyme is also used for enzymatic determination of glucose and creatine phosphokinase activity when coupled with hexokinase.
Alkaline phosphatase (ALP or ALKP) is a hydrolase enzyme responsible for removing phosphate groups from many types of molecules, including nucleotides, proteins, and alkaloids. The process of removing the phosphate group is called dephosphorylation. As the name suggests, alkaline phosphatases are most effective in an alkaline environment. It is sometimes used synonymously as basic phosphatase. Alkaline phosphatase has become a useful tool in molecular biology laboratories, since DNA normally possesses phosphate groups on the 5' end. Alkaline phosphatase is also used as a label for enzyme immunoassays.
N-acetylneuraminate lyase, also known as N-acetylneuraminic acid aldolase, is an enzyme that catalyzes the chemical reaction: N-acetylneuraminate ↔ N-acetyl-D-mannosamine + pyruvate. Hence, this enzyme has one substrate, N-acetylneuraminate, and two products, N-acetyl-D-mannosamine and pyruvate. This enzyme belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. DIA-182 is useful for enzymatic determination of N-acetylneuraminic acid and sialic acid when coupled with the related enzymes in clinical analysis. For industrial use, this enzyme is useful for enzymatic synthesis of sialic acid.
Glucan 1,4-alpha-glucosidase (glucoamylase, amyloglucosidase (AMG), or gamma-amylase) is an enzyme located on the brush border of the small intestine with system name 4-alpha-D-glucan glucohydrolase. This enzyme catalyzes the following chemical reaction: Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose. Most forms of the enzyme can rapidly hydrolyze 1,6-alpha-D-glycosidic bonds when the next bond in the sequence is 1,4. This enzyme is useful for structural investigation of carbohydrates and for enzymatic determination of α-amylase when coupled with the related enzymes in clinical analysis.
In enzymology, a glycerol-3-phosphate oxidase (glycerol-3-phosphate oxidase) 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 donors with oxygen as acceptor. This enzyme participates in glycerophospholipid metabolism. It employs one cofactor, FAD. This enzyme is useful for enzymatic determination of triglyceride when coupled with lipoprotein lipase and glycerokinase in clinical analysis.
Hexokinase is an enzyme that phosphorylates hexoses (six-carbon sugars), forming hexose phosphate. In most organisms, glucose is the most important substrate of hexokinases, and glucose-6-phosphate the most important product. Hexokinase can transfer an inorganic phosphate group from ATP to a substrate. Hexokinases should not be confused with glucokinase, which is a specific isoform of hexokinase. While other hexokinases are capable of phosphorylating several hexoses, glucokinase acts with a 50-fold lower substrate affinity and its only hexose substrate is glucose. The enzyme is useful for enzymatic determination of glucose, adenosine-5'-triphosphate (ATP) and creatine phosphokinase when coupled with glucose-6-phosphate dehydrogenase.
Lactate oxidase, also known as lactate 2-monooxygenase, belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O with incorporation of one atom of oxygen (internal monooxygenases o internal mixed-function oxidases). This enzyme participates in pyruvate metabolism. It employs one cofactor, FMN. DIA-208 is useful for enzymatic determination of L-lactate.
Lipoprotein lipase (LPL) is a member of the lipase gene family, which includes pancreatic lipase, hepatic lipase, and endothelial lipase. It is a water-soluble enzyme that hydrolyzes triglycerides in lipoproteins, such as those found in chylomicrons and very low-density lipoproteins (VLDL), into two free fatty acids and one monoacylglycerol molecule. It is also involved in promoting the cellular uptake of chylomicron remnants, cholesterol-rich lipoproteins, and free fatty acids. LPL requires ApoC-II as a cofactor. This enzyme is useful for enzymatic determination of triglyceride in serum when coupled with L-α-glycerophosphate oxidase and glycerol kinase.
Proline specific endopeptidase is inhibited by diisopropylfluorophosphate and may therefore be classified as a serine endopeptidase. The enzyme specifically hydrolyzed Pro-X peptide bonds. With Glu at position X, low rates of hydrolysis were observed; otherwise the enzyme exhibited little preference for particular amino acid residues at position X. A similar substrate preference was observed with respect to the amino acid residue preceding the prolyl residue in the substrate.
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. This enzyme is useful for enzymatic determination of inorganic phosphorus, 5'-nucleotidase and adenosine deaminase when coupled with Purine-nucleoside phosphorylase and uricase.
Diaphorase or dihydrolipoyl dehydrogenase is a flavoprotein enzyme capable of oxidizing the reduced form of NAD (NADH). This lipoamide dehydrogenase is a component of the glycine cleavage system, as well as of the alpha-ketoacid dehydrogenase complexes. Diaphorase has great practical value in tumor chemotherapy. With the association between diaphorase and tumor, we can guide the application of bioreductive drugs, improve the selectivity of treatment and provide a theoretical basis for the development of new bioreductive drugs.
Creative Enzymes provides enzyme products for diagnostic use. These products have passed a series of quality control (QC) assays to ensure high quality. Please contact us if you have any questions or specific needs.