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Native Microorganism Creatine Amidohydrolase LAB GRADE

In enzymology, a creatinase (EC 3.5.3.3) is an enzyme that catalyzes the chemical reaction: creatine + H2O ↔sarcosine + urea. Thus, the two substrates of this enzyme are creatine and H2O, whereas its two products are sarcosine and urea. The native enzyme was shown to be made up of two subunit monomers via SDS-polyacrylamide gel electrophoresis. Creatinase has been found to be most active at pH 8 and is most stable between ph 6-8 for 24 hrs. at 37 degrees. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. This enzyme participates in arginine and proline metabolism.http://www.creative-enzymes.com/product/Native-Microorganism-Creatine-Amidohydrolase_781.html
 

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Native Microorganism Creatinine Deiminase LAB GRADE 97%

In enzymology, a creatinine deaminase (EC 3.5.4.21) 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.http://www.creative-enzymes.com/product/Native-Microorganism-Creatinine-Deiminase_782.html

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Native Microorganism D-lactate dehydrogenase LAB GRADE

A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another.http://www.creative-enzymes.com/product/Native-Microorganism-Dlactate-Dehydrogenase_803.html
 

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Native Microorganism Malate Dehydrogenase LAB GRADE 97%

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.http://www.creative-enzymes.com/product/Native-Microorganism-Malate-Dehydrogenase_756.html

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Native Pseudomonas sp. Lipoprotein lipase LAB GRADE 98%

Lipoprotein lipase (LPL) (EC 3.1.1.34) 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.http://www.creative-enzymes.com/product/Native-Pseudomonas-Sp-Lipoprotein-Lipase_806.html

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Native Porcine Adenosine 5'-Triphosphatase LAB GRADE 97%

ATPases are a class of enzymes that catalyze the decomposition of ATP into ADP and a free phosphate ion. This dephosphorylation reaction releases energy, which the enzyme (in most cases) harnesses to drive other chemical reactions that would not otherwise occur. This process is widely used in all known forms of life. Some such enzymes are integral membrane proteins (anchored within biological membranes), and move solutes across the membrane, typically against their concentRation gradient. These are called transmembrane ATPases.http://www.creative-enzymes.com/product/Native-Porcine-Adenosine-5Triphosphatase_1042.html

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Native Porcine heart Lactate dehydrogenase LAB GRADE 97%

A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another.http://www.creative-enzymes.com/product/Native-Porcine-Heart-Lactate-Dehydrogenase_802.html

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Abl Kinase Mutant active human, recombinant LAB GRADE 98%

Abelson murine leukemia viral oncogene homolog 1 also known as ABL1 is a protein that, in humans, is encoded by the ABL1 gene (previous symbol ABL) located on chromosome 9. c-Abl is sometimes used to refer to the version of the gene found within the mammalian genome, while v-Abl refers to the viral gene.http://www.creative-enzymes.com/product/Abl-Kinase-Mutant-Active-Human-Recombinant_1629.html

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Alpha-Lytic Protease M190A Mutant, recombinant LAB GRADE

Alpha-lytic protease (aLP) is an alternative specificity protease for proteomics applications, whose wild-type (WT) version cleaves after T, A, S, and V residues. The M190A (Met190 → Ala190) mutant of aLP has different cleavage specificities, and cleaves after M, F, and L residues. Both the WT and M190A forms of aLP geneRate peptides of similar average length as trypsin.http://www.creative-enzymes.com/product/AlphaLytic-Protease-M190A-Mutant-Recombinant_1713.html
 

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Native Aerococcuss viridans Lactate Oxidase LAB GRADE 97%

In enzymology, a lactate 2-monooxygenase (EC 1.13.12.4) is an enzyme that catalyzes the chemical reaction: (S)-lactate + O2 ↔ acetate + CO2 + H2O. Thus, the two substrates of this enzyme are (S)-lactate and O2, whereas its 3 products are acetate, CO2, and H2O.http://www.creative-enzymes.com/product/Native-Aerococcuss-Viridans-Lactate-Oxidase_752.html

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