Enzima

Nepicastat hydrochloride (RS-25560-197 hydrochloride) is a selective, orally active, dopamine-beta-hydroxylase inhibitor that crosses the blood-brain barrier.

<p>Methyl cinnamate, a tyrosinase inhibitor and a flavoring compound, has antimicrobial, antiadipogenic, vasorelaxant, and anti-inflammatory effects.</p>

2,3-dihydro-1H-indene-5-sulfonamide is Carbonic anhydrase 12 (human) inhibitor.

Dichlorphenamide (Diclofenamide) is a carbonic anhydrase inhibitor that is used in the treatment of glaucoma.

2-Ketoglutaric acid is a reversible inhibitor of tyrosinase (IC50=15 mM). 2-Ketoglutaric acid is an intermediate of the Krebs cycle. High-Quality, Low-Cost!

XMD16-5 blocks TNK2, linked to advanced lung/prostate cancers and breast cancer metastasis in mice; disrupts signaling in several tumors.

Benzolamide (CL 11366) inhibits carbonic anhydrase effectively and low-threshold calcium currents in hippocampal pyramidal neurons.

Taxifolin (Dihydroquercetin) is a flavonoid in many plants such as Taxus chinensis, Siberian larch, Cedrus deodara and so on.

Beta-Tocopherol has effects on human erythroleukemia cell (HEL) adhesion induced by phorbol 12-myristate 13-acetate (PMA).Cost-effective and quality-assured.

p-Fluoro-L-phenylalanine: TH substrate, studies enzyme regulation, binds E. coli L-leucine receptor, KD 0.26μM.

<p>Guanoclor (VATENSOL) (INN), also known as guanochlor, is a sympatholytic drug. It is known to bind to non-adrenergic sites in pig kidney membranes.</p>

2-Ketoglutaric acid Sodium (AKG) is a key molecule in the TCA cycle.

α-Arbutin (4-hydroxyphenyl-D-lucopyranoside) is a synthetic and functional active ingredient for skin lightening.

D-Tyrosine inhibits melanin production and biofilm formation, promoting biofilm dispersal without hindering bacterial growth.

3-O-Ethyl-L-ascorbic acid is a cosmetic tyrosinase inhibitor with whitening ability and is a stabilized vitamin C derivative.

Benzenesulfonamide (Benzosulfonamide) ia an inhibitor of carbonic anhydrases.

Telotristat, active metabolite of LX1606, is an oral tryptophan hydroxylase inhibitor with potential antiserotonergic effects.

CDK2 is a member of the Ser/Thr protein kinase family.

<p>Applications Necroptosis is a regulated caspase-independent cell death mechanism that results in morphological features resembling necrosis. Necrostatin-1 is an inhibitor of RIP1 kinase that prevents the death of TNF-α-treated FADD-deficient Jurkat cells. Necrostatin-1 has been used to investigate the pathological importance of necroptosis in ischemic brain injury and myocardial infarction.<br>References Foresti, R., et al: J. Biol. Chem., 272, 18411 (1997); Cardenas, A., et al.: J. Neurochem., 74, 2041 (2000); Degterev, et al.: Nat. Chem. Biol., 1, 112 (2005); Hitomi, J., et al.: Cell, 135, 1311 (2008);<br></p>

Ectonucleotide pyrophosphatase-phosphodiesterase 3 (ENPP3), a protein detected in the human uterus, has been found to play an important role in the development

TPSAB1, namely tryptase alpha/beta-1, is a serine protease with trypsin­like activity.

HER3/ERBB3 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag.

Plasmodium falciparum lactate dehydrogenase (PfLDH) is a key enzyme for energy generation of malarial parasites and is considered to be a potential antimalarial

PTGS2, also known as COX-2, is s component of Prostaglandin-endoperoxide synthase (PTGS).

Urokinase/uPA Protein, Rat, Recombinant (His) is expressed in HEK293 mammalian cells with His tag.

(R)-Trolox is a selective tyrosinase inhibitor used in food, cosmetics, and pharmaceutical products.

Lipase 12 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-7.5 and temp. optimum at >60°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 12 was shown to hydrolyze p-Nitrophenyl esters of butyrate (60 % activity compared to octanoate), octanoate (100 %), laurate (51 %), palmitate (30 %), stearate (14 %), arachidate (0.2 %) and behenate (0.2 %).

<p>Ribonuclease H from Escherichia Coli is the enzyme that breaks down RNA strand in RNA-DNA duplexes. It acts by cleaving the phosphodiester bonds of RNA and produces 3' hydroxyl and a 5' phosphate groups at the cleavage site. A common use of Ribonuclease H is to remove RNA template after reverse transcription reaction.</p>

Lipase 67 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 7-8 and temp. optimum at 30°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 67 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (37 %), laurate (3 %) and palmitate (0.2 %).

Alpha Amylase (Amylase, α-Amylase, 1,4-α-D-glucan glucanohydrolase, glycogenase, PPA; systematic name 4-α-D-glucan glucanohydrolase; EC 3.2.1.1, CAS Number [9000-90-2]) is an enzyme that catalyzes hydrolysis of large polysaccharides into smaller fragments. Alpha amylase targets alpha bonds of 1→4 glycosidic linkages of poly- and oligosaccharides with three or more D-glucose units. One unit of Alpha Amylase will catalyze the hydrolysis of 1.0 μmol of 2-chloro-4-nitrophenyl-α-D-maltotrioside to yield 2-chloro-4-nitrophenol per minute at 37°C. Porcine pancreatic Alpha Amylase is supplied as lyophilized, off-white to white powder, lyophilized from tris chloride and mannitol, pH 7.2. Activity is ≥70U/mL, specific activity ≥100 U/mg protein. Store at -20°C on arrival.

<p>Lipase 13 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-8 and temp. optimum at 35-45°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 13 was shown to hydrolyze p-Nitrophenyl esters of butyrate (87 % activity compared to octanoate), octanoate (100 %), palmitate (44 %), stearate (21 %) and arachidate (2 %).</p>

<p>Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces. Lipases/esterases can be used as versatile tools in hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. The lipase from the yeast Y. lipolytica has a temperature optimum in the 30 - 40 °C range and pH optimum between pH 7 and 8.</p>

<p>Catalyst for signal development in immunoassays</p>

<p>Alpha-L-iduronidase is a glycoside hydrolase enzyme that cleaves the non-reducing, terminal alpha-L-iduronic acid residues from polysaccharides and oligosaccharides. Alpha-L-iduronidase is involved in the lysosomal degradation of glycosaminoglycans and its deficiency leads to the accumulation of dermatan sulphate and heparan sulphate in tissues, a condition known as mucopolysaccharidosis I (MPS I). Alpha-L-iduronidase activity can be detected and quantified in an assay using a fluorogenic substrate 4MU-alpha-L-idopyranosiduronic acid. Alpha-L-iduronidase is also used in a 2-step assay for Hunter syndrome (MPS II) testing in combination with 4-MU-alpha-L-idopyranosiduronic acid 2-sulphate.<br>This enzyme is supplied as a 2 mg/mL aqueous solution in 25 mM sodium acetate, 150 mM NaCl, 50% glycerol, pH 5.0 from a bacterial source, recombinantly expressed in Escherichia coli (see application notes for more details). Alpha-L-iduronidase is also available as lyophilisate (FA181881)</p>

<p>(R)-Mandelonitrile lyase (systematic name mandelonitrile benzaldehyde-lyase (hydrogen cyanide-forming), other names are D-oxynitrilase, D-alpha-hydroxynitrile lyase, (R)-oxynitrilase, oxynitrilase, mandelonitrile benzaldehyde-lyase, ydroxynitrile lyase; EC 4.1.2.10) is the enzyme that catalyzes the following reaction:mandelonitrile ⇌ hydrogen cyanide + benzaldehydeOne unit of (R)-mandelonitrile lyase will convert 1.0 μmol of mandelonitrile per minute under optimal conditions.</p>

Alpha Amylase, powder, is an enzyme preparation that acts as a catalyst for the hydrolysis of starch, breaking it down into simpler sugars like maltose and glucose. This enzyme is derived from microbial or fungal sources, commonly via fermentation processes using strains of bacteria or fungi specifically optimized for enzyme production.

<p>PAIRED PRODUCTS AVAILABLE:</p>

<p>Lipase 04 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-7 and temp. optimum at 60-70°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 04 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (68 %), laurate (2 %), palmitate (2 %), stearate (2 %), arachidate (2 %) and behenate (2 %).</p>

Lipase CR 03 is an industrial-grade enzyme product that is derived from microbial sources, specifically engineered for robust and efficient catalytic activity. The enzyme is extracted utilizing advanced fermentation techniques that capitalize on the prolific nature of specific strains known for lipase production. Its mode of action involves the hydrolysis of ester bonds in triglycerides, converting them into free fatty acids and glycerol. This catalytic process is critical in various biochemical pathways and industrial reactions.

o-Glycosidase (O-Glycanase, endo-a-acetylgalactosaminidase, endo-a-N-acetylgalactosaminidase; EC 3.2.1.97) is an enzyme that specifically removes N-acetylgalactosamine disaccharides, that were attached to serine's or threonine's side-chain oxygen (hence o-Glycosidase). One unit of o-Glycosidase will hydrolyze 1.0 mmole of of substrate per minute at 37 °C and pH 5.0.

Lipase immo Kit 01 is an advanced biochemical tool designed for the immobilization of lipase, an enzyme commonly sourced from microorganisms. This innovative kit utilizes a sophisticated immobilization matrix to enhance enzyme stability and reusability. By binding the enzyme to a solid support, the kit facilitates repeated and continuous use in various reactions without significant loss of activity.

<p>Test sample of Cymit Quimica's Phospholipase D 040 Halal and Kosher Food grade bulk enzyme (EPLD840.6). With one of the most competitive activity rates on the global market and manufactured in Europe, this enzyme is perfect for use in food, diagnostic, therapeutic and nutraceutical industries worldwide.  Phospholipase D is an enzyme that is expressed in almost all types of organisms and whose activity can be harnessed to synthesize critical raw materials, for example phosphatidylserine. Phosphatidylserine has shown itself to be an important functional ingredient in reducing cognitive dysfunction and dementia in the field of nutraceuticals. As a Halal and Kosher food grade enzyme, Cymit Quimica's Phospholipase D is an excellent candidate for a diverse variety of food industry applications. Furthermore our enzyme can be used in diagnostic assays, creating first-class drug delivery systems and APIs. Product is a lyopholised solid</p>

Peroxidase 013 belongs to the class of the heme-family peroxidases and can be utilized for catalyzing oxidation/epoxidation of unsaturated C-C bonds, N- or S-oxidation, ether cleavage and alcohol/aldehyde oxidation reactions. The Peroxidase 12 has a temperature optimum in the 20 - 40 °C range and pH optimum between pH 5 and 8.

<p>Xanthine oxidase is an enzyme that catalyzes the hydroxylation of hypoxanthine to xanthine and xanthine to uric acid</p>

<p>Sialic acid aldolase - crystalline is a purified enzyme product, which is typically derived from microbial sources, such as certain bacteria, that have evolved to metabolize sialic acids. This enzyme catalyzes a reversible aldol reaction between sialic acid and pyruvate, facilitating the cleavage or formation of sialic acid from N-acetylmannosamine and pyruvate. By breaking the carbon-carbon bond in sialic acid, sialic acid aldolase plays a critical role in the degradation and biosynthesis pathways of sialic acid, which are key factors in numerous biological processes.</p>

Creatinine amidohydrolase (also sometimes reffered as creatininase, EC 3.5.2.10) is an enzyme that catalyses the following reaction: creatinine + H2O ⇌ creatine  One unit of creatinine amidohydrolase will produce 1.0 µmole of creatine at pH 7.5 and 37 °C.

Lipase 56 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 8 and temp. optimum at 40-50°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 56 was shown to hydrolyze p-Nitrophenyl esters of butyrate (79 % activity compared to octanoate), octanoate (100 %), laurate (51 %), palmitate (29 %), stearate (15 %), arachidate (0.2 %) and behenate (0.1 %).