
Enzyme
Subcategories of "Enzyme"
- Carbonic Anhydrase(196 products)
- Hydroxylase(36 products)
- MPO(2 products)
- Reductase(51 products)
- Tyrosinase(71 products)
Found 3620 products of "Enzyme"
Carbonodithioic Acid O-(Octahydro-4,7-methano-1H-inden-5-yl) Ester Potassium Salt
CAS:Controlled ProductFormula:C11H15KOS2Color and Shape:NeatMolecular weight:266.464C. rugosa Lipase 03, CRL 3 from Candida rugosa - ELCR03
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 03 from the yeast Candida rugosa has a temperature optimum in the 30 - 50 °C range and pH optimum between pH 7 and 8.Carboxypeptidase Y, from S. cerevisiae, recombinant, lyophilized - ECPY001
CAS:Carboxypeptidase Y (EC 3.4.16.1) is an exopeptidase enzyme. It hydrolyzes peptide bonds of C-terminal residues and it remains active in the presence of urea at low to moderate concentrations. One unit of the Carboxypeptidase Y will hydrolyze 1.0 μmole of a chromogenic peptide substrate, releasing C-terminal alanine and generating a light-absorbing product. Carboxypeptidase Y has been obtained from yeast S. cerevisiae, has a broad substrate specificity and can therefore be used in sequence analysis of proteins. Carboxypeptidase Y has a temperature optimum in the 20 – 30 °C range and pH optimum between pH 6 and 7.PNPase
Specific activity: >500 units/mg-protein.Unit definition: One unit will polymerize 1.0 micro mole of ADP, releasing 1.0 micro mole of inorganic phosphate in 15 minutes at pH 9.1 at 37 °C.
Luciferase from Vibrio fischeri
CAS:Luciferase enzymes sourced from Vibrio fischeriColor and Shape:PowderAminoacyl tRNA synthetase-IN-1
CAS:Enzyme involved in protein translation and catalyzes the aminoacylation reactionFormula:C16H25N7O7SPurity:Min. 95%Color and Shape:PowderMolecular weight:459.48 g/molProtein disulfide isomerase from bovine liver
CAS:An enzyme that catalyzes the formation and breakage of disulfide bonds in the folding of proteinsFormula:C7H5Cl2NO5SPurity:Min. 95%Molecular weight:286.09 g/molAdenylate Kinase 1, human, recombinant
Adenylate kinase 1 (EC 2.7.4.3) catalyzes interconversion between ATP, ADP and AMP by catalyzing the following reaction: ATP + AMP ⇔ 2 ADP One unit of Adenylate kinase 1 will convert 1.0 µmol ATP and 1.0 µmol AMP to 2.0 µmol ADP per min at optimum conditions.Purity:Min. 95%α-Mannosidase
CAS:α-Mannosidase (α-D-mannopyranosidase, 1,2-α-mannosidase, 1,2-α-D-mannosidase, exo-α-mannosidase, α-D-mannosidase, systematic name α-D-mannoside mannohydrolase; EC 3.2.1.24) is an enzyme that cleaves α-mannose to produce glucose. One unit of α-Mannosidase will hydrolyze 1.0 µmole of chromogenic phosphate mimic p-nitrophenyl-α-p-mannoside to p-nitrophenol in 1 minute at pH 5.0 and 37°C.
Molecular weight:65.4 g/molAminopeptidase, Aeromonas proteolytica
CAS:One unit of Aminopeptidase (3.4.11.10) will hydrolyze 1.0 μmole of L-leucine p-nitroanilide to p-nitroaniline and L-leucine per min at pH 8.0 and 25 °C.Ubiquitin thiolesterase UCHL1
CAS:Ubiquitin thiolesterase UCHL1 (Ubiquitin carboxy-terminal hydrolase L1; EC 3.1.2.15) is an enzyme that hydrolyses small C-terminal ubiquitin adducts to regenerate ubiquitin.Glutathione Reductase, baker's yeast
CAS:Glutathione Reductase, baker's yeast, is an enzyme derived from the yeast species *Saccharomyces cerevisiae*. This enzyme is sourced from baker's yeast, providing a renewable and consistent product for various biochemical applications. Its mode of action involves catalyzing the reduction of glutathione disulfide (GSSG) to the sulfhydryl form glutathione (GSH), using NADPH as an electron donor. This reaction is crucial for maintaining the intracellular redox balance by regenerating GSH, the primary cellular antioxidant.Formaldehyde Dehydrogenase
CAS:Formaldehyde dehydrogenase (EC 1.2.1.46) is an enzyme that catalyzes the following reaction: formaldehyde + NAD+ + H2O ⇌ formate + NADH + H+ One unit of formaldehyde dehydrogenase will convert 1.0 µmole of formaldehyde to formic acid per minute at pH 7.5 and 37°C in the presence of NAD+.NAD+ is available here.Lipoxidase
CAS:Lipoxidase is an enzyme, which is typically sourced from various plant tissues, animals, and some microorganisms. It functions by catalyzing the oxidation of polyunsaturated fatty acids in the presence of oxygen. This enzymatic action results in the formation of lipid hydroperoxides, which are key intermediates in various biochemical pathways, including those involved in cell signaling and the modulation of gene expression.Purity:Min. 95%Alcohol Oxidase - vacuum-dried powder, >0.6 units/mg solid
CAS:Alcohol oxidase (EC 1.1.3.13) is an enzyme that catalyzes the following chemical reaction: a primary alcohol + O2 + H2O ⇌ an aldehyde + H2O2 One unit of alcohol oxidase will oxidize 1.0 µmole of methanol to formaldehyde per min at pH 7.5 and 25 °C.Serratiopeptidase
CAS:Serratiopeptidase (serratio peptidase, serratia peptidase, serrapeptidase, serratia E-15 protease, serralysin, serrapeptase; EC 3.4.24.40) is a proteolitic enzyme (proteinase) that is produced by Serratia marcescens.Purity:Min. 95%Color and Shape:PowderAminopeptidase I from streptomyces griseus
CAS:Aminopeptidase I is a specialized proteolytic enzyme derived from the actinobacterium Streptomyces griseus. This enzyme functions by catalyzing the cleavage of amino acids from the N-terminus of peptides, which plays a pivotal role in protein metabolism and regulation. The source of this enzyme, Streptomyces griseus, is well-regarded for producing a variety of bioactive compounds owing to its rich genetic and biochemical repertoire.Butyrylcholinesterase
Butyrylcholinesterase (BCHE, BuChE, PCHE, pseudocholinesterase, plasma cholinesterase, Acylcholine acyl-hydrolase, Choline esterase; EC 3.1.1.8, CAS No [9001-08-5]) is an enzyme that made in the liver and found mainly in blood plasma. It catalyzes the following reaction: Acylcholine + H2O → choline + carboxylic acidOne unit of Butyrylcholinesterase will change absorbance by 0.2 milliunits (mA) per minute at optimal buffer conditions and 37 ̊C. Equine serum butyrylcholinesterase is supplied as white to pale grey-green powder with activity of ≥50U/mg and specific activity of ≥300U/mg protein. It can be dissolved at 5 mg/mL concentration in 50 mM Tris-HCl pH 7.3 - 7.5, giving colorless to slightly green solution. Equine serum butyrylcholinesterase is activated by Ca2+, optimum pH 7-8, KM=18 µM (butyrylthiocholine at 25°C). Store at -20°C on arrival.Ribonuclease A
CAS:Ribonuclease A (RNase A) is widely used to break down RNA in DNA purification. RNase A catalyzes the endonucleolytic cleavage of phosphodiester bonds of RNA.Chitinase
CAS:Chitinase (systematic name (1→4)-2-acetamido-2-deoxy-β-D-glucan glycanohydrolase, EC 3.2.1.14) is a hydrolase that breaks down glycosidic bonds in chitin. One unit of chitinase will yield 1.0 mg of N-acetyl-D-glucosamine from chitin per hour at pH 6.0 and 25 °C.Formula:C17H16N8ZnPurity:Min. 95%Molecular weight:397.74 g/molC. rugosa Lipase 02, CRL 2 from Candida rugosa - ELCR02
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 02 from the yeast Candida rugosa has a temperature optimum in the 30 - 50 °C range and pH optimum between pH 7 and 8.β-1,4-Galactosyltransferase 1
β-1,4-Galactosyltransferase 1 is an enzyme that catalyzes the synthesis of the glycosaminoglycan-protein linkage in proteoglycans.Malate dehydrogenase,buffered aqueous glycerol solution, 600-1000 units/mg protein (biuret)
CAS:Malic dehydrogenase is a mitochondrial isozyme and an important catalyst in the tricarboxylic acid cycle. The enzyme catalyzes the following reaction: Oxaloacetate + β-NADH → L-Malate + β-NADOne unit will convert 1.0 μmole of oxalacetate and β-NADH to L-malate and β-NAD per min at pH 7.5 at 25 °C.Purity:Min. 95%Proteinase, Bacillus subtilis, sutilain
CAS:Proteinase, Bacillus subtilis, sutilain is a proteolytic enzyme, which is derived from the bacterium Bacillus subtilis. This enzyme exhibits a serine-type mechanism of action, characterized by its ability to cleave peptide bonds in proteins efficiently. It catalyzes the hydrolysis of proteins into peptides and amino acids, facilitating the breakdown of complex proteins into simpler, soluble forms.Purity:Min. 95%Color and Shape:PowderAsparaginase, from E.coli, recombinant, lyophilized - EASP001
Asparaginase (EC 3.5.1.1) is an enzyme that catalyzes the following reaction: Asparagine + H2O → Aspartate + NH4+ Industrially, asparaginase is used to reduce the formation of acrylamide in starch-containing food ingredients and products during production processes. Asparaginase has a temperature optimum in the 30 – 50 °C range and pH optimum between pH 8 and 9. One unit will yield 1.0 μmole of ammonia from asparagine per min.Phosphorylase B from rabbit muscle
CAS:Phosphorylase B is an enzymatic protein, specifically an isoform of glycogen phosphorylase, derived from rabbit muscle. This enzyme plays a critical role in glycogen metabolism by catalyzing the phosphorolytic cleavage of α(1→4) glycosidic bonds in glycogen, releasing glucose-1-phosphate. The rabbit muscle source provides a well-studied model due to its high enzyme activity and availability, facilitating in-depth biochemical and structural analysis.
Purity:Min. 95%Sphingomyelinase from bacillus cereus
CAS:Sphingomyelinase (SMase, Sphingomyelin phosphodiesterase, systematic name sphingomyelin cholinephosphohydrolase; EC 3.1.4.12) is an enzyme that hydrolyses sphingomyelin into phosphocholine and ceramide. One unit of sphingomyelinase will hydrolyze 1.0 µmole of chromogenic substrate analogue per minute at pH 7.4 and 37 °C.Purity:Min. 95%Lipoprotein lipase
CAS:Lipoprotein lipase is a critical enzyme used to modulate lipid processing, primarily sourced from mammalian tissues. It functions by hydrolyzing triglycerides present in circulating chylomicrons and very low-density lipoproteins. This enzymatic process liberates free fatty acids, which can subsequently be utilized as energy by peripheral tissues or stored in adipose tissue. Lipoprotein lipase is pivotal in lipid metabolism, participating in maintaining homeostasis of plasma lipid levels.Purity:Min. 95%alpha Amylase enzyme
Alpha Amylase (Amylase, α-Amylase, 1,4-α-D-glucan glucanohydrolase, glycogenase, systematic name 4-α-D-glucan glucanohydrolase; EC 3.2.1.1, CAS Number [9000-90-2]) is an enzyme that catalyses hydrolysis of large polysacharides 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. Human pancreatic Alpha Amylase is supplied as clear, colorless to light yellow liquid solution at ≥400U/mL, specific activity ≥100 U/mg protein.Store at 2-8 °C on arrival.Purity:Min. 95%Acid phosphatase
CAS:One unit will hydrolyse 1.0μmol of 4-nitrophenyl phosphate per minute at 37°C and pH 4.8. Substrate for enzyme analysis is the 4-nitrophenyl phosphate disodium hexahydrate (EN08508).Formula:C6H10O2Purity:Min. 95%Molecular weight:114.14 g/molAmidase, from Rhodococcus sp., recombinant, lyophilized - EAM02
CAS:Amidase (EC 3.5.1.4) is a hydrolase acting on carbon-nitrogen bonds in linear amides and can be used in the hydrolysis of amides to acids. Amidase 02 is of bacterial origin (R. erythropolis and has been produced in E.coli).eXrase DNA Endonuclease, research-grade
CAS:eXrase DNA endonuclease from enGenes is a recombinant endonuclease from Serratia marcescens produced in E. coli. Effectively and efficiently degrades all forms of DNA and RNA, reducing sample viscosity without proteolytic activity. As effective and efficient as other nucleases on the market, eXrase DNA endonuclease is the most cost-effective way to improve proteins yields and improve sample handing. Presented as a ready to use colourless liquid, formulated in Tris buffer at pH 8.0 with 50 % glycerol (v/v). This research grade eXrase has low endotoxin, max 0.25 EU/kU.eXrase DNA endonuclease is suitable for the effective breakdown of nucleic acids in numerous biotech settings: • Removal of residual host DNA from biotechnological products to meet regulatory standards • Reduction of viscosity and streamlined purification in downstream processing of fermentation procedures. • Reduction of viscosity in in upstream fermentation processes • Extraction and/or synthesis of flavouring nucleotides • Enhanced bioavailability of nucleotides in specific feed products • DNA degradation for the removal or prevention of biofilm formationeXrase DNA endonuclease from enGenes is made by a proprietary microbial fermentation process utilizing Escherichia coli cells. This enzyme facilitates the hydrolysis of phosphodiester bonds in various forms of DNA and RNA, including single-stranded, double-stranded, linear, circular, or supercoiled configurations, yielding smaller oligonucleotides typically composed of 2-4 base pairs. Unit-Definition: One unit (U) of the enzyme is defined as the amount required to digest calf thymus DNA, yielding acid-soluble oligonucleotides equivalent to a ΔA260nm of 1.0 within a 30-minute timeframe at pH 8.0 and 37°C. This standardization allows for consistent measurement of enzymatic activity across different batches.
Cellulose catalase
Cellulose catalase is an enzyme-based product, designed specifically to act as a catalyst in the oxidative processes associated with cellulose applications. It is derived from a microbial source, where bacilli or fungi are employed to produce robust catalase enzymes in a fermentation process. The mode of action involves the catalase enzyme’s ability to facilitate the decomposition of hydrogen peroxide into water and oxygen, thereby reducing oxidative damage during cellulose processing.
eXrase DNA Endonuclease, tech-grade
CAS:eXrase DNA endonuclease from enGenes is a recombinant endonuclease from Serratia marcescens produced in E. coli. Effectively and efficiently degrades all forms of DNA and RNA, reducing sample viscosity without proteolytic activity. As effective and efficient as other nucleases on the market, eXrase DNA endonuclease is the most cost-effective way to improve proteins yields and improve sample handing. Presented as a ready to use colourless liquid, formulated in Tris buffer at pH 8.0 with 50 % glycerol (v/v). This tech grade version is our most cost effective endonuclease for R&D applications. eXrase DNA endonuclease is suitable for the effective breakdown of nucleic acids in numerous biotech settings: • Removal of residual host DNA from biotechnological products to meet regulatory standards • Reduction of viscosity and streamlined purification in downstream processing of fermentation procedures. • Reduction of viscosity in in upstream fermentation processes • Extraction and/or synthesis of flavouring nucleotides • Enhanced bioavailability of nucleotides in specific feed products • DNA degradation for the removal or prevention of biofilm formationeXrase DNA endonuclease from enGenes is made by a proprietary microbial fermentation process utilizing Escherichia coli cells. This enzyme facilitates the hydrolysis of phosphodiester bonds in various forms of DNA and RNA, including single-stranded, double-stranded, linear, circular, or supercoiled configurations, yielding smaller oligonucleotides typically composed of 2-4 base pairs. Unit-Definition: One unit (U) of the enzyme is defined as the amount required to digest calf thymus DNA, yielding acid-soluble oligonucleotides equivalent to a ΔA260nm of 1.0 within a 30-minute timeframe at pH 8.0 and 37°C. This standardization allows for consistent measurement of enzymatic activity across different batches.Citrate lyase from klebsiella pneumonia ≥0.20 unit/mg solid
CAS:Citrate lyase (also known as ATP citrate synthase, EC 2.3.3.8) is an enzyme that catalyzes the following reaction:citrate + ATP + CoA → oxaloacetate + Acetyl-CoA + ADP + PiEnzymatic activity: One unit will convert 1.0 micromole of citrate to oxalacetate per minute at pH 7.6 and 25 °C in the presence of required cofactors. Citrate lyase is supplied lyophylized, with activity ≥0.20 unit/mg solid.Purity:Min. 95%Urate oxidase (from Yeast)
CAS:Urate Oxidase, also known as uricase, catalizes the following reaction: Uric acid + O2 + H2O → 5-hydroxyisourate + H2O2.Formula:C18H26N5O14PPurity:Min. 95%Molecular weight:567.4 g/molDiaphorase (from Clostridium kluyveri)
CAS:Diaphorase (lipoyl dehydrogenase, EC 1.8.1.4) is an NAD+/NADH-dependent oxidoreductase. One unit of diaphorase will convert 1.0 μmole NADH into NAD+ the presence of substrate at pH 7.5 and 25 °C.Purity:Min. 95%Deoxycytidine Kinase, human, recombinant
Deoxycytidine kinase (dCK, EC 2.7.1.74) is an enzyme that catalyzes the following reaction: dC + ATP → dCMP + ADP It can also use UTP as a donor of the phosphate group, and it can phosphorylate other deoxyribonucleosides (e.g. dA, dG) as well as nucleoside analogues (like clofarabine). One unit of dCK will convert 1.0 µmole of dC and ATP to dCMP and ADP per minute at pH 7.5 and 37°C.Purity:Min. 95%3,4-Dihydroxybenzylamine hydrobromide
CAS:3,4-Dihydroxybenzylamine hydrobromide inhibits DNA polymerase and melanoma growth, varying with tyrosinase activity.Formula:C7H10BrNO2Purity:98.49%Color and Shape:Light Beige Crystalline PowderMolecular weight:220.06Immobilized Lipase Kit, 7 unique immobilized EUCODIS® Lipases, immobilized by adsorption and covalent binding - ELIM Kit
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 immobilized Lipase kit contains 7 different lipases, immobilised on a hydrophobic carrier either by adsorption or covalent linkage. Immobilized lipases can be utilized in various reaction types, and are optimal for all reactions in organic solvents or solvent-free systems.Oxalate Oxidase, freeze-dried, from Wheat
CAS:Oxalate Oxidase, freeze-dried, from Wheat is an enzyme preparation which is derived from wheat and functions through the oxidative degradation of oxalate. This enzyme catalyzes the conversion of oxalate into carbon dioxide and hydrogen peroxide, utilizing oxygen as a co-substrate in the process. The activity of Oxalate Oxidase is crucial in biological and biochemical applications where oxalate degradation is required.Ref: 3D-ETS012.6
10U711.00€1KU4,680.00€25U551.00€2KU8,189.00€50U914.00€100U1,044.00€0.1KU1,020.00€0.5KU2,925.00€1000U5,429.00€2000U9,481.00€0.25KU1,802.00€Ubiquitin Conjugating enzyme E2C Human Recombinant
Ubiquitin Conjugating enzyme E2C (other names UBE2C, UBCH10, dJ447F3.2, ubiquitin conjugating enzyme E2 C; EC 2.3.2.24) is an essential mediator of mitotic destruction events and cell cycle progression. It catalyzes the destruction of cyclins A and B in conjunction with the anaphase-promoting complex, and therefore, plays an important role in the control of the cell exit from mitosis This activity is essential at then end of mitosis for the inactivation of their partner kinase Cdc2 and exit from mitosis into G1 of the next cell cycle. In addition, UBE2C bears homology to yeast PAS2, a gene that is essential for biogenesis of peroxisomes. UBE2C is useful for in vitro ubiquitinylation reactions.Protein phosphatase 2C
CAS:Protein phosphatase 2C is a key enzyme, which is a serine/threonine-specific phosphatase, derived from various organisms including humans, plants, and bacteria. This enzyme plays a pivotal role in cellular signaling by removing phosphate groups from serine and threonine residues on target proteins, a process known as dephosphorylation. This action is crucial for the regulation of diverse cellular functions, including stress responses, cell division, and apoptosis.Protease from Streptomyces griseus
CAS:Protease enzymes break down proteins and are essential for many biological processes, including digestion, cellular regulation and blood clotting. They are also used in many industrial and biotechnological applications for example in food processing and in detergents.
Purity:Min. 95%Color and Shape:Powderβ-Glucanase 2, thermostable
CAS:Thermostable β-Glucanase 2 is an enzyme that hydrolases β-Glucans into glucose. One unit of β-Glucanase 2 will produce 1.0 μmole of glucose from β-glucan per minute at pH 5.8 and 70 °C.Purity:Min. 95%Chymase
CAS:Chymase (alternative names mast cell protease 1, mast cell serine proteinase, skeletal muscle protease, EC 3.4.21.39) is a serine protease, found in mast cells and basophil granulocytes.Purity:Min. 95%Lactase - >300U/mg
CAS:beta-Galactosidase (EC 3.2.1.23, shortly beta-Gal, also know as lactase) catalyses the hydrolysis of beta-d-galactoside in the presence of water to galactose and alcohol, or lactose into glucose and galactose. beta-Gal has a molecular weight of 540,000 and is composed of four identical subunits of MW 135,000, each with an independent active site. The enzyme has divalent metals as cofactors, with chelated Mg2+ ions required to maintain active site conformation. The molecule contains numerous sulfhydryl groups and is glycosylated.L-Asparaginase
CAS:L-Asparaginase (EC 3.5.1.1) is an enzyme that catalyzes the following reaction: L-Asparagine + H2O → L-Aspartate + NH4+ One unit will yield 1.0 μmole of ammonia from L-asparagine per min at pH 8.6 and 37 °C.Purity:Min. 95%Glutathione peroxidase
CAS:Glutathione peroxidase (EC 1.11.1.9) is an enzyme that reduces peroxides to limit oxidative damage, by catalyzing the following reaction: 2 GSH + H2O2 → GS–SG + 2 H2O One unit of glutathione peroxidase will catalyze the conversion of 1.0 µmole of H2O2 per minute at pH 7.0 and 25 °C in the presence of reduced glutathione. Reduced glutahione is available here.Purity:Min. 95%Molecular weight:84,500 g/molNitrilase
CAS:Nitrilase (nitrile aminohydrolase; EC 3.5.5.1) in an enzyme that catalyzes hydrolysis of nitriles to carboxilic acids and ammonia: R-CN + 2 H2O → R-COO- + NH4+ One unit of nitrilase will yield 1.0 μmol of ammonia per minute under optimal reaction conditions using acrylonitrile as a substrate.
Purity:Min. 95%Transglutaminase from guinea pig liver
CAS:Transglutaminase (2.3.2.13) is an enzyme that catalyzes formation of isopeptide bonds between the γ-carboxamide groups ( -(C=O)NH2 ) of glutamine side chains and amino groups. The donor of the amino group is usually (but not always) an ε-amino group ( -NH2 ) of lysine residue. The reaction also releases ammonia: Gln-(C=O)NH2 + NH2-Lys → Gln-(C=O)NH-Lys + NH3One unit of transglutaminase will catalyze the formation of 1.0 μmole transglutamination product per min at pH 6.0 and 37 °C.Purity:Min. 95%α-N-Acetylglucosaminidase
CAS:α-N-Acetylglucosaminidase (recombinant Human NAGLU Protein), degrades heparan sulfate by hydrolysis of terminal GlcNAc resides in N-acetyl-alpha-D-glucosaminides of heparan sulfate.Activity is measured by its ability to hydrolyse 4-Nitrophenyl 2-acetamido-2-deoxy-a-D-glucopyranoside EN03208 or EM31027. The specific activity is >900 pmol/min/μg, as measured under the decribed conditions.Purity:(Sds-Page) Min. 95%Chloroperoxidase, aqueous suspension
CAS:Chloroperoxidase (also known as chloride peroxidase, systemic name chloride:hydrogen-peroxide oxidoreductase, EC 1.11.1.10) is an enzyme that catalyzes chlorination of organic compounds. Overall reaction is the following:R-H + Cl− + H2O2 + H+ → R-Cl + 2 H2O; reaction intermediate is hypochlorous acid (HOCl). One unit of chloroperoxidase will convert 1.0 μmole of substrate per minute.
Color and Shape:PowderSuperoxide dismutase PEG
Superoxide dismutase coupled to polyethylene glycol. Superoxide dismutase (EC 1.15.1.1) is an enzyme that catalyzes the following reaction: 2 H+ + 2 O2− → O2 + H2O2 thus converting an extremely reactive and cytotoxic superoxide radical into oxygen and (significantly less reactive) hydrogen peroxide.
Plasmin
CAS:Plasmin, human is a serin protease which present in the blood and is involved in the cleavage of cross-linked fibrin, a process known as fibrinolysis.One unit will produce one micromole of P-Nitroanilide from D-Val-Leu-Lys-P-Nitroanilide per minute at pH 7.5 at 37°CPyruvate kinase (from Rabbit muscle), ammonium sulfate suspension
CAS:Pyruvate kinase (from Rabbit muscle), ammonium sulfate suspension is an enzyme product, which is a purified protein extracted from the muscle tissue of rabbits. This enzyme plays a crucial role in glycolysis, specifically catalyzing the transphosphorylation of phosphoenolpyruvate (PEP) to pyruvate, generating ATP from ADP in the process. This step is a key regulatory point in the glycolytic pathway, which is essential for cellular energy production.
Purity:Min. 95%Cytochrome C oxidase
CAS:Cytochrome C oxidase (originally assigned EC 1.9.3.1, now re-assigned EC 7.1.1.9) is an enzyme that catalyzes the following reaction: 4 Fe2+ – cytochrome c + 4 H+ + O2 → 4 Fe3+ – cytochrome c + 2 H2OCreatinase from pseudomonas sp.
CAS:Creatinase (EC 3.5.3.3) is an enzyme that catalyzes the fellowing reaction: creatine + H2O ⇌ sarcosine + ureaOne unit of creatinase will hydrolyze 1.0 µmole of creatine into sarcosine and urea per min at pH 7.5 and 37 °C.Purity:Min. 95%EUCODIS® Nitrilhydratase 23, recombinant enzyme - ENH023
Nitrile hydratase 23 recombinantly expressed in E. coli comes in a freeze-dried formulation. Nitrile hydratases can be utilized to convert nitriles into their corresponding amides, e.g. to produce acrylamide from acrylonitrile. Additional applications include the removal of nitriles from industrial wastewater. Our nitrile hydratases have been tested for hydrolysis of the following substrates:cyclohexanecarbonitrile, cinnamonitrile, benzonitrile, methacrylonitrile, pivalonitrile.
Casein Kinase 2
Casein kinase 2 (CK2, CSNK2; EC 2.7.11.1) is a constitutively active serine and threonine protein kinase. It plays a role in a range of cellular processes, including DNA repair, cell cycle control, metabolic regulation, circadian rhythms and more. Its known substrates include hundreds of proteins. One unit of CK2 will phosphorylate of 1 pmol of of peptide substrate in 1 minute at 30°C and presence of ATP.Formula:C45H73N19O24Purity:Min. 95%Molecular weight:1,264.17 g/molEUCODIS® CalB01 IA, engineered variant of Candida antarctica Lipase B, immobilized by adsorption on hydrophobic carrier - ELCB01IA
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 CalB01 IA lipase has been immobilized on a hydrophobic carrier by adsorption. The immobilized CalB01 lipase has a temperature optimum in the 40 - 50 °C range and pH optimum between pH 5 and 8.C. rugosa Lipase 01, CRL 1 from Candida rugosa - ELCR01
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 01 from the yeast Candida rugosa has a temperature optimum in the 30 - 50 °C range and pH optimum between pH 7 and 8.Secreted Phospholipase A2-IIA, human, recombinant
The secreted phospholipase A2-IIA (sPLA2-IIA, PLA2, systematic name phosphatidylcholine 2-acylhydrolase; EC 3.1.1.4) is an enzyme that catalyses the hydrolysis of glycerophospholipids at the sn2 position, yielding 1-acylglycerophosphocholine and a fatty acid. One unit of secreted phospholipase A2-IIA will hydrolyze 1.0 μmole of substrate per min under optimal conditions.Purity:Min. 95%Mannitol dehydrogenase from leuconostoc mesenteroides
CAS:Mannitol dehydrogenase (MDH, mannitol 2-dehydrogenase, EC 1.1.1.67) is an enzyme that catalyzes the following reaction: D-mannitol + NAD+ ⇌ D-fructose + NADH + H+ One unit of mannitol dehydrogenase will generate 1.0 μmole of D-fructose per min in the presence of NAD+ at pH 8.6 and 40°C. NAD+ is available here and NADH is available here, depending on whether you require the reaction to proceed from left to right or from righ to left, respectively.
Purity:Min. 95%Cathepsin B from human placenta
CAS:Cathepsin B is a lysosomal proteolytic enzyme of the cysteine protease family. It is present in all mammalian cells. It is essential for the intracellular protein turnover. Cathepsin B may be a useful tool in Alzheimer′s research, as it may have a role in the natural defense against the disease.Purity:Min. 95%HCAIX-IN-2
CAS:HCAIX-IN-2 (compound 9d) is a selective inhibitor of carbonic anhydrase and acts on hCA IX (Ki: 24.6 nM) and hCA XII (Ki: 45.3 nM).Formula:C19H16N8O4SColor and Shape:SolidMolecular weight:452.45SU 10603
CAS:SU 10603 is a specific inhibitor of 17α-hydroxylase (also known as CYP17A1 and P450c17) used to study steroid hormone synthesis.Formula:C15H12ClNOPurity:99.93% - 99.96%Color and Shape:SolidMolecular weight:257.72hCAI/II-IN-3
CAS:"hCAI/II-IN-3 (compound 5b) is a potent dual hCA I/II inhibitor with Ki: 51.25nM (I), 13.15nM (II), helps treat AMS."Formula:C16H18N4O4S2Color and Shape:SolidMolecular weight:394.47hCAIX-IN-6
CAS:6B and 14g inhibit tumor-associated HCA IX with low nanomolar potency; 6K targets HCA XII. All are potential cancer drug leads.Formula:C18H12N2O4SColor and Shape:SolidMolecular weight:352.36hCAII-IN-1
CAS:hCAII-IN-1 (7f) inhibits CA II/IX with Kis 1.2 nM/113.6 nM, potential for cancer treatment.Formula:C21H21BrN6O4SColor and Shape:SolidMolecular weight:533.4hCAXII-IN-2
CAS:hCAXII-IN-2 is a potent inhibitor of hCA XII (Ki: 84.2 nM) and hCA IX (Ki: 268.5 nM), with low activity on hCA I/II.Formula:C21H18ClN3O4Color and Shape:SolidMolecular weight:411.84DTP348
CAS:DTP348: Oral carbonic anhydrase IX inhibitor & hypoxic cell radiosensitizer with sulfamide & 5-nitroimidazole components.Formula:C6H11N5O4SColor and Shape:SolidMolecular weight:249.25PGDS Protein, Human, Recombinant
Hematopoietic Prostaglandin D Synthase (HPGDS) belongs to the GST superfamily and Sigma family.Color and Shape:Lyophilized PowderMolecular weight:26 KDa (reducing condition)Ref: TM-TMPJ-00690
1mg2,758.00€5µg113.00€10µg178.00€20µg284.00€50µg523.00€100µg779.00€200µg1,142.00€500µg1,923.00€hCAXII-IN-4
CAS:hCAXII-IN-4 is a selective and potent CA XII inhibitor with a Ki value of 6.4 nM for human CA XII.Formula:C22H27N5O6SColor and Shape:SolidMolecular weight:489.54hCAI/II-IN-2
CAS:hCAI/II-IN-2 (2b) inhibits hCA I/II (Ki: 40.97 nM, 15.15 nM) and IX (61.88 nM), fights AMS with anti-hypoxic effects, but has low cellular activity.Formula:C12H12N4O5S2Color and Shape:SolidMolecular weight:356.38Tyrosinase-IN-7
CAS:Tyrosinase-IN-7 is a small-molecule tyrosinase inhibitor (IC50 1.57 μM) that suppresses melanin activity and cell growth with low cytotoxicity.Formula:C15H10O5Purity:99%Color and Shape:SolidMolecular weight:270.24hCA IX-IN-2
hCA IX-IN-2 is a highly potent and selective inhibitor of hCA IX, exhibiting an inhibition constant (K I) value of 32.1 nM and demonstrating anti-proliferativeFormula:C23H24N2O4STeColor and Shape:SolidMolecular weight:552.11hCAIX/XII-IN-6
hCAIX/XII-IN-6: Oral carbonic anhydrase inhibitor, targets hCA I/II/IV/IX/XII, aids rheumatoid arthritis research. Ki: 6697/2950/4093/4.1/7.7 nM.Formula:C26H23N3O6S4Color and Shape:SolidMolecular weight:601.74hCAIX-IN-8
CAS:hCAIX-IN-8, a selective hCAIX inhibitor, IC50: 0.024 μM. Also affects CAII, CAVA (IC50s: 1.99, 1.10 μM), limits cell migration, and induces apoptosis.Formula:C19H16N4O6Color and Shape:SolidMolecular weight:396.35hCAIX-IN-10
CAS:"hCAIX-IN-10 (6i) selectively inhibits carbonic anhydrase IX/XII (Ki: 61.5/586.8 nM), markers in tumor cells, affecting acid-base balance."Formula:C28H21N3O3SColor and Shape:SolidMolecular weight:479.55hCAIX-IN-7
CAS:hCAIX-IN-7 (6c) selectively inhibits tumor-related isoform hCAIX (KI: 410.6 nM) and weakly affects hCAI/II (KI: >10000 nM).Formula:C18H12FNO3Color and Shape:SolidMolecular weight:309.29Carbonic anhydrase inhibitor 13
CAS:Carbonic anhydrase inhibitor 13 (compound 7) is a potent inhibitor of carbonic anhydrase (CA).Formula:C17H15N5O3S2Color and Shape:SolidMolecular weight:401.46Carbonic anhydrase inhibitor 11
CAS:Potent carbonic anhydrase inhibitor VI targets CA II, IX, XII with Ki: 40, 39, 900 nM respectively.Formula:C19H15F3N4O3S2Color and Shape:SolidMolecular weight:468.47hCAIX/XII-IN-4
CAS:hCAIX/XII-IN-4 inhibits CAIX/XII with Ki: 4.5 nM (CAXII), 23.6 nM (CAIX), and >10000 nM (CAI/CAII).Formula:C20H16N2O5Color and Shape:SolidMolecular weight:364.35hCAIX-IN-3
CAS:hCAII-IN-3 (7e) selectively inhibits CA II/IX with Kis of 124.2/30.5 nM, showing promise for cancer treatment.Formula:C21H21BrN6O4SColor and Shape:SolidMolecular weight:533.4hCAIX-IN-14
CAS:hCAIX-IN-14 is a potent inhibitor of human CA IX with a K i value of 134.8 nM .Formula:C11H17ClN6O2SColor and Shape:SolidMolecular weight:332.81Quinethazone
CAS:Quinethazone is a thiazide diuretic used to treat hypertension. Common side effects include dizziness, dry mouth, nausea, and low potassium levels.Formula:C10H12ClN3O3SColor and Shape:Fibrous Crystals From 50% Acetone Physical Description Fibrous Crystals Or White Powder (Ntp 1992)Molecular weight:289.74Carbonic anhydrase inhibitor 7
CAS:Potent hCA inhibitor; targets hCA IX, II, XII, I with Ki: 6.5, 7.1, 72.1, 255.8 nM respectively.Formula:C23H17N3O5SColor and Shape:SolidMolecular weight:447.46hCAXII-IN-1
CAS:hCAXII-IN-1 selectively inhibits HCA IX/XII, promising for new cancer drug development.Formula:C20H17NO5Color and Shape:SolidMolecular weight:351.35hCA I-IN-2
CAS:hCA I-IN-2 (6d) inhibits hCA I (Ki: 18.8 nM) more selectively over II, IX, XII (Ki: 375.1, 1721, 283.9 nM).Formula:C26H20BrN5O3SColor and Shape:SolidMolecular weight:562.44FC11409B
CAS:FC11409B is a CAIX inhibitor, inhibiting breast cancer invasion and metastasis.Formula:C29H23BF4N2O3SColor and Shape:SolidMolecular weight:566.38hCAI/II-IN-4
CAS:hCAI/II-IN-4 inhibits hCA I & II (Ki: 16.95 & 15.22 nM), hCA IX (Ki: 27.04 nM), has anti-hypoxia benefits and is low-toxic for AMS research.Formula:C15H15N3O5S2Color and Shape:SolidMolecular weight:381.43Methazolamide-d6
CAS:Methazolamide-d6 is a GC/LC-MS standard for measuring methazolamide, a glaucoma drug that lowers eye pressure and fluid, reduces seizures, and combats ROS.Formula:C5H2D6N4O3S2Color and Shape:SolidMolecular weight:242.31hCAXII-IN-5
CAS:hCAXII-IN-5, or compound 6o, is a potent, selective hCAXII inhibitor with Ki values: hCAI & II >10000, hCAIX 286.1, hCAXII 1.0 nM.Formula:C23H22N2O4Color and Shape:SolidMolecular weight:390.43Carbonic anhydrase inhibitor 14
CAS:CA inhibitor 14 blocks hCA I/II/IX/XII (K i of 1203/99.7/9.4/27.7 nM) and CDK2 (IC50: 20.3 μM), showing antitumor effects.Formula:C18H17N7O2SColor and Shape:SolidMolecular weight:395.44hCAXII-IN-3
CAS:hCAXII-IN-3 (Compound 6o) is a selective inhibitor of human carbonic anhydrase XII (hCAXII) (Ki: 10.0 nM).Formula:C26H20BrN5O3SColor and Shape:SolidMolecular weight:562.44hCAIX/XII-IN-3
CAS:Compound 6q inhibits hCAIX/CAXII; K i : hCAI >10000 nM, hCAII >10000 nM, hCAIX 66.2 nM, hCAXII 4.4 nM.Formula:C20H13F3N2O4Color and Shape:SolidMolecular weight:402.32


