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Homoisocitrate dehydrogenase

Homoisocitrate dehydrogenase (EC 1.1.1.87) is an enzyme that belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate:NAD+ oxidoreductase (decarboxylating).This enzyme participates in lysine biosynthesis.

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Hydroxysteroid dehydrogenase

Hydroxysteroid dehydrogenases are a group of alcohol oxidoreductases that catalyze the dehydrogenation of hydroxysteroids.

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Isopiperitenol dehydrogenase

Isopiperitenol dehydrogenase (EC 1.1.1.223) is an enzyme that belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (-)-trans-isopiperitenol:NAD+ oxidoreductase. This enzyme participates in monoterpenoid biosynthesis.

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Meteobate AC (Acid Protease)

Meteobate AC (Acid Protease) is a fungal acid protease leather bating enzyme to be used in leather beam-house processes. Meteobate AC is specially designed for bating of hides and skins already pickled or tanned by either chrome or vegetable-synthetic methods. Meteobate AC finds its application in tanneries processing long stored, pickled wet blue or vegetable synthetic crust stock requiring further bating treatment. It is particularly useful for bating of partially chrome-tanned leather for manufacturing of good quality garment leather. It specifically removes folds and creases in the pickled or tanned stocks. It can also be used for bating of carbon dioxide de-limed pelt or pelts limed in acidic conditions with oxidizing agents. Meteobate AC is extremely useful when de-liming, bating, pickling and chrome tanning are to be carried out in the same drum. This saves operational cost considerably. Meteobate AC provides increased pliability, tight but smooth grain and uniformity in dyeing. Meteobate AC is a ready –to-use formulation of enzyme and other ingredients for high-performance leather bating, giving an open, smooth silky, smooth texture and elastic grain and slippery grain. Meteobate AC also opens the collagen structure giving uniform leather bating.

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PD 0332991 HCl LAB GRADE 97%

PD 0332991 can potently inhibit CDK4 and CDK6 with IC50 of 11 nM and 16 nM. More information please visit the website: http://www.creative-enzymes.com/product/PD-0332991-HCl_2253.html

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Trimethylamine dehydrogenase

Trimethylamine dehydrogenase (EC 1.5.8.2) is an enzyme that belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with a flavin as acceptor. The systematic name of this enzyme class is trimethylamine:electron-transferring flavoprotein oxidoreductase (demethylating). This enzyme participates in methane metabolism.

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(R)-6-hydroxynicotine oxidase

D-6-hydroxynicotine oxidase;6-hydroxy-D-nicotine oxidase.

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Catechol-O-methyl transferase

Catechol-O-methyltransferase (COMT; EC 2.1.1.6) is one of several enzymes that degrade catecholamines such as dopamine, epinephrine, and norepinephrine. In humans, catechol-O-methyltransferase protein is encoded by the COMT gene. As the regulation of catecholamines is impaired in a number of medical conditions, several pharmaceutical drugs target COMT to alter its activity and therefore the availability of catecholamines.

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Dihydrokaempferol 4-reductase

Dihydrokaempferol 4-reductase (EC 1.1.1.219) is an enzyme that belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cis-3,4-leucopelargonidin:NADP+ 4-oxidoreductase This enzyme participates in flavonoid biosynthesis.

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Enzyme-thiol transhydrogenase

Enzyme-thiol transhydrogenase (glutathio belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a disulfide as acceptor. The systematic name of this enzyme class is [xanthine-dehydrogenase]:glutathione-disulfide S-oxidoreductase.his enzyme participates in glutathione metabolism.

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