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Native Microorganism Creatinine Deiminase LAB GRADE

In enzymology, a creatinine deaminase (EC is an enzyme that catalyzes the chemical reaction: creatinine + H2O ↔ N-methylhydantoin + NH3. Thus, the two substrates of this enzyme are creatinine and H2O, whereas its two products are N-methylhydantoin and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is creatinine iminohydrolase.

Native Microorganism Malate Dehydrogenase LAB GRADE

Malate dehydrogenase is an enzyme in the citric acid cycle that catalyzes the conversion of malate into oxaloacetate (using NAD+) and vice versa (this is a reversible reaction). Malate dehydrogenase is not to be confused with malic enzyme, which catalyzes the conversion of malate to pyruvate producing NADPH. Malate dehydrogenase is also involved in gluconeogenesis, the synthesis of glucose from smaller molecules. Pyruvate in the mitochondria is acted upon by pyruvate carboxylase to form oxaloacetate, a citric acid cycle intermediate. In order to get the oxaloacetate out of the mitochondria, malate dehydrogenase reduces it to malate, and it then traverses the inner mitochondrial membrane. Once in the cytosol, the malate is oxidized back to oxaloacetate by cytosolic malate dehydrogenase. Finally, phosphoenol-pyruvate carboxy kinase (PEPCK) converts oxaloacetate to phosphoenol pyruvate.

Native Microorganism Sarcosine Oxidase LAB GRADE 97%

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.

Native Pichia pastoris Alcohol Oxidase LAB GRADE 97%

In enzymology, an alcohol oxidase (EC 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.

Native Pseudomonas sp. Lipoprotein lipase LAB GRADE

Lipoprotein lipase (LPL) (EC 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.

Acetylcholinesterase Human, recombinant LAB GRADE 96%

Acetylcholinesterase, also known as AChE or acetylhydrolase, is a hydrolase that hydrolyzes the neurotransmitter acetylcholine. AChE is found at mainly neuromuscular junctions and cholinergic brain synapses, where its activity serves to terminate synaptic transmission. It belongs to carboxylesterase family of enzymes. It is the primary target of inhibition by organophosphorus compounds such as nerve agents and pesticides.

Adenosine deaminase Bovine, recombinant LAB GRADE 97%

Adenosine deaminase is an enzyme (EC involved in purine metabolism. It is needed for the breakdown of adenosine from food and for the turnover of nucleic acids in tissues. Present in virtually all mammalian cells, its primary function in Humans is the development and maintenance of the immune system.

Native Bacillus sp. Amylase, Maltogenic LAB GRADE 97%

Glucan 1,4-alpha-maltohydrolase (EC, maltogenic alpha-amylase, 1,4-alpha-D-glucan alpha-maltohydrolase) is an enzyme with system name 4-alpha-D-glucan alpha-maltohydrolase. This enzyme catalyses the following chemical reaction:hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the non-reducing ends of the chains. This enzyme acts on starch and related polysaccharides and oligosaccharides.

Native Bacillus subtilis Bilirubin oxidase LAB GRADE

In enzymology, a bilirubin oxidase (EC is an enzyme that catalyzes the chemical reaction 2 bilirubin + O2↔ 2 biliverdin + 2 H2O. Thus, the two substrates of this enzyme are bilirubin and O2, whereas its two products are biliverdin and H2O. This enzyme belongs to the family of oxidoreductases, to be specific those acting on the CH-CH group of donor with oxygen as acceptor. This enzyme participates in porphyrin and chlorophyll metabolism.

Native E. coli Alanine Aminotransferase LAB GRADE 97%

Alanine transaminase (ALT) is a transaminase enzyme (EC It is also called alanine aminotransferase (ALAT) and was formerly called serum glutamate-pyruvate transaminase (SGPT) or serum glutamic-pyruvic transaminase (SGPT). ALT is found in plasma and in various body tissues, but is most common in the liver. It catalyzes the two parts of the alanine cycle. Serum ALT level, serum AST (aspartate transaminase) level, and their ratio (AST/ALT ratio) are commonly measured clinically as biomarkers for liver health. The tests are part of blood panels.

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