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| Product | Description | |
|---|---|---|
| 1,3,6,8-tetrahydroxynaphthalene synthase | Isolated from the fungus Colletotrichum lagenarium, and the bacteria Streptomyces coelicolor and Streptomyces peucetius. It only uses malonyl-CoA, without invovement of acetyl-CoA. Group: Enzymes. Synonyms: PKS1; THNS; SCO1206; RppA. Enzyme Commission Number: EC 2.3.1.233. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2181; 1,3,6,8-tetrahydroxynaphthalene synthase; EC 2.3.1.233; PKS1; THNS; SCO1206; RppA. Cat No: EXWM-2181. |  |
| 13-deoxydaunorubicin hydroxylase | The enzymes from the Gram-positive bacteria Streptomyces sp. C5 and Streptomyces peucetius show broad substrate specificity for structures based on an anthracycline aglycone, but have a strong preference for 4-methoxy anthracycline intermediates (13-deoxydaunorubicin and 13-dihydrodaunorubicin) over their 4-hydroxy analogues (13-deoxycarminomycin and 13-dihydrocarminomycin), as well as a preference for substrates hydroxylated at the C-13 rather than the C-14 position. Group: Enzymes. Synonyms: DoxA. Enzyme Commission Number: EC 1.14.13.181. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0780; 13-deoxydaunorubicin hydroxylase; EC 1.14.13.181; DoxA. Cat No: EXWM-0780. | |
| 1,4-dihydroxy-2-naphthoyl-CoA synthase | This enzyme is involved in the synthesis of 1,4-dihydroxy-2-naphthoate, a branch point metabolite leading to the biosynthesis of menaquinone (vitamin K2, in bacteria), phylloquinone (vitamin K1 in plants), and many plant pigments.The coenzyme A group is subsequently removed from the product by EC 3.1.2.28, 1,4-dihydroxy-2-naphthoyl-CoA hydrolase. Group: Enzymes. Synonyms: naphthoate synthase; 1,4-dihydroxy-2-naphthoate synthase; dihydroxynaphthoate synthase; o-succinylbenzoyl-CoA 1,4-dihydroxy-2-naphthoate-lyase (cyclizing); MenB; o-succinylbenzoyl-CoA dehydratase (cyclizing). Enzyme Commission Number: EC 4.1.3.36. CAS No. 61328-42-5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4913; 1,4-dihydroxy-2-naphthoyl-CoA synthase; EC 4.1.3.36; 61328-42-5; naphthoate synthase; 1,4-dihydroxy-2-naphthoate synthase; dihydroxynaphthoate synthase; o-succinylbenzoyl-CoA 1,4-dihydroxy-2-naphthoate-lyase (cyclizing); MenB; o-succinylbenzoyl-CoA dehydratase (cyclizing). Cat No: EXWM-4913. | |
| 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase | Binds 2 Mg2+ ions that are essential for activity. The enzyme participates in the biosynthetic pathways for folate (in bacteria, plants and fungi) and methanopterin (in archaea). The enzyme exists in varying types of multifunctional proteins in different organisms. The enzyme from the bacterium Streptococcus pneumoniae also harbours the activity of EC 4.1.2.25, dihydroneopterin aldolase, the enzyme from the plant Arabidopsis thaliana harbours the activity of EC 2.5.1.15, dihydropteroate synthase, while the enzyme from yeast Saccharomyces cerevisiae is trifunctional with both of the two above mentioned activities. Group: Enzymes. Synonyms: 2-amino-4-hydroxy-6-hydroxymethyldi. Enzyme Commission Number: EC 2.7.6.3. CAS No. 37278-23-2. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3222; 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase; EC 2.7.6.3; 37278-23-2; 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase; H2-pteridine-CH2OH pyrophosphokinase; 7,8-dihydroxymethylpterin-pyrophosphokinase; HPPK; 7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase; hydroxymethyldihydropteridine pyrophosphokinase; ATP:2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine 6'-diphosphotransferase. Cat No: EXWM-3222. | |
| 2-dehydro-3-deoxy-L-galactonate 5-dehydrogenase | The enzyme, characterized from agarose-degrading bacteria, is involved in a degradation pathway for 3,6-anhydro-α-L-galactopyranose, a major component of the polysaccharides of red macroalgae. Group: Enzymes. Enzyme Commission Number: EC 1.1.1.389. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0308; 2-dehydro-3-deoxy-L-galactonate 5-dehydrogenase; EC 1.1.1.389. Cat No: EXWM-0308. | |
| 2-dehydro-3-deoxy-L-rhamnonate dehydrogenase (NAD+) | The enzyme, characterized from the bacteria Sphingomonas sp. SKA58 and Sulfobacillus thermosulfidooxidans, is involved in the non-phosphorylative degradation pathway for L-rhamnose. It does not show any detectable activity with NADP+ or with other aldoses. Group: Enzymes. Synonyms: 2-keto-3-deoxy-L-rhamnonate dehydrogenase. Enzyme Commission Number: EC 1.1.1.401. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0323; 2-dehydro-3-deoxy-L-rhamnonate dehydrogenase (NAD+); EC 1.1.1.401; 2-keto-3-deoxy-L-rhamnonate dehydrogenase. Cat No: EXWM-0323. | |
| 2-epi-valiolone synthase | The enzyme, characterized from the bacteria Actinosynnema mirum and Stigmatella aurantiaca DW4/3-1, produces 2-epi-valiolone, which is believed to function as a precursor in aminocyclitol biosynthesis. It requires a divalent metal ion (Zn2+ or Co2+) and an NAD+ cofactor, which is transiently reduced during the reaction. cf. EC 4.2.3.152, 2-epi-5-epi-valiolone synthase and EC 4.2.3.154, demethyl-4-deoxygadusol synthase. Group: Enzymes. Enzyme Commission Number: EC 4.2.3.155. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5170; 2-epi-valiolone synthase; EC 4.2.3.155. Cat No: EXWM-5170. | |
| 2-hydroxyethylphosphonate dioxygenase | Requires non-heme-Fe(II). Isolated from some bacteria including Streptomyces hygroscopicus and Streptomyces viridochromogenes. The pro-R hydrogen at C-2 of the ethyl group is retained by the formate ion. Any stereochemistry at C-1 of the ethyl group is lost. One atom from dioxygen is present in each product. Involved in phosphinothricin biosynthesis. Group: Enzymes. Synonyms: HEPD; phpD (gene name); 2-hydroxyethylphosphonate:O2 1,2-oxidoreductase (hydroxymethylphosphonate forming). Enzyme Commission Number: EC 1.13.11.72. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0592; 2-hydroxyethylphosphonate dioxygenase; EC 1.13.11.72; HEPD; phpD (gene name); 2-hydroxyethylphosphonate:O2 1,2-oxidoreductase (hydroxymethylphosphonate forming). Cat No: EXWM-0592. | |
| 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase | This enzyme is part of the pathway from urate to (S)-allantoin, which is present in bacteria, plants and animals (but not in humans). Group: Enzymes. Synonyms: OHCU decarboxylase; hpxQ (gene name); PRHOXNB (gene name). Enzyme Commission Number: EC 4.1.1.97. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4847; 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase; EC 4.1.1.97; OHCU decarboxylase; hpxQ (gene name); PRHOXNB (gene name). Cat No: EXWM-4847. | |
| (3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase | The enzyme, characterized from bacteria Streptomyces toyocaensis and Amycolatopsis orientalis, is involved in the biosynthesis of (3,5-dihydroxyphenyl)glycine, a component of the glycopeptide antibiotic vancomycin. Group: Enzymes. Synonyms: DpgC. Enzyme Commission Number: EC 1.13.11.80. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0601; (3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase; EC 1.13.11.80; DpgC. Cat No: EXWM-0601. | |
| 3,6-anhydro-L-galactonate cycloisomerase | The enzyme, characterized from the marine bacteria Vibrio sp. EJY3 and Postechiella marina M091, is involved in a degradation pathway for 3,6-anhydro-α-L-galactopyranose, a major component of the polysaccharides of red macroalgae. Group: Enzymes. Synonyms: 3,6-anhydro-α-L-galactonate lyase (ring-opening); 3,6-anhydro-α-L-galactonate cycloisomerase. Enzyme Commission Number: EC 5.5.1.25. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5626; 3,6-anhydro-L-galactonate cycloisomerase; EC 5.5.1.25; 3,6-anhydro-α-L-galactonate lyase (ring-opening); 3,6-anhydro-α-L-galactonate cycloisomerase. Cat No: EXWM-5626. | |
| 3,8-divinyl chlorophyllide a reductase | The enzyme, found only in bacteriochlorophyll b-producing bacteria, catalyses the introduction of a C-8 ethylidene group. The enzyme contains a [4Fe-4S] cluster, and structurally resembles the Fe protein/MoFe protein complex of nitrogenase. It is very similar to EC 1.3.7.15, chlorophyllide a reductase, and is composed of three subunits. Two of them form the catalytic component, while the third one functions as an ATP-dependent reductase component that catalyses the electron transfer from ferredoxin to the catalytic component. Group: Enzymes. Enzyme Commission Number: EC 1.3.7.14. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1395; 3,8-divinyl chlorophyllide a reductase; EC 1.3.7.14. Cat No: EXWM-1395. | |
| 3,8-divinyl protochlorophyllide a 8-vinyl-reductase (ferredoxin) | The enzyme, found in many phototrophic bacteria, land plants, and some green and red algae, is involved in the production of monovinyl versions of (bacterio)chlorophyll pigments from their divinyl precursors. Binds two [4Fe-4S] clusters and an FAD cofactor. It can also act on 3,8-divinyl chlorophyllide a, 3,8-divinyl chlorophyll a, and chlorophyll c2. cf. EC 1.3.1.75, 3,8-divinyl protochlorophyllide a 8-vinyl-reductase (NADPH). Group: Enzymes. Synonyms: bciB (gene name); cyano-type divinyl chlorophyllide a 8-vinyl-reductase. Enzyme Commission Number: EC 1.3.7.13. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1394; 3,8-divinyl protochlorophyllide a 8-vinyl-reductase (ferredoxin); EC 1.3.7.13; bciB (gene name); cyano-type divinyl chlorophyllide a 8-vinyl-reductase. Cat No: EXWM-1394. | |
| 3,8-divinyl protochlorophyllide a 8-vinyl-reductase (NADPH) | The enzyme, found in higher plants, green algae, and some phototrophic bacteria, is involved in the production of monovinyl versions of (bacterio)chlorophyll pigments from their divinyl precursors. It can also act on 3,8-divinyl chlorophyllide a. cf. EC 1.3.7.13, 3,8-divinyl protochlorophyllide a 8-vinyl-reductase (ferredoxin). Group: Enzymes. Synonyms: DVR (gene name); bciA (gene name); [4-vinyl]chlorophyllide a reductase; 4VCR; chlorophyllide-a:NADP+ oxidoreductase; divinyl chlorophyllide a 8-vinyl-reductase; plant-type divinyl chlorophyllide a 8-vinyl-reductase. Enzyme Commission Number: EC 1.3.1.75. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1344; 3,8-divinyl protochlorophyllide a 8-vinyl-reductase (NADPH); EC 1.3.1.75; DVR (gene name); bciA (gene name); [4-vinyl]chlorophyllide a reductase; 4VCR; chlorophyllide-a:NADP+ oxidoreductase; divinyl chlorophyllide a 8-vinyl-reductase; plant-type divinyl chlorophyllide a 8-vinyl-reductase. Cat No: EXWM-1344. | |
| 3-deoxy-D-glycero-D-galacto-nononate 9-phosphatase | The enzyme, characterized from the bacterium Bacteroides thetaiotaomicron, is part of the biosynthesis pathway of the sialic acid 3-deoxy-D-glycero-D-galacto-nononate (KDN). KDN is abundant in extracellular glycoconjugates of lower vertebrates such as fish and amphibians, but is also found in the capsular polysaccharides of bacteria that belong to the Bacteroides genus. Group: Enzymes. Synonyms: 2-keto-3-deoxy-D-glycero-D-galactonononate-9-phosphate phosphatase. Enzyme Commission Number: EC 3.1.3.103. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3612; 3-deoxy-D-glycero-D-galacto-nononate 9-phosphatase; EC 3.1.3.103; 2-keto-3-deoxy-D-glycero-D-galactonononate-9-phosphate phosphatase. Cat No: EXWM-3612. | |
| 3-hydroxypropionate dehydrogenase (NADP+) | Catalyses the reduction of malonate semialdehyde to 3-hydroxypropanoate, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutanoate cycles, autotrophic CO2 fixation pathways found in some green non-sulfur phototrophic bacteria and archaea, respectively. The enzyme from Chloroflexus aurantiacus is bifunctional, and also catalyses the upstream reaction in the pathway, EC 1.2.1.75. Different from EC 1.1.1.59 [3-hydroxypropionate dehydrogenase (NAD+)] by cofactor preference. Group: Enzymes. Synonyms: 3-hydroxypropanoate dehydrogenase (NADP+); 3-hydroxypropionate:NADP+ oxidoreductase. Enzyme Commission Number: EC 1.1.1.298. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0207; 3-hydroxypropionate dehydrogenase (NADP+); EC 1.1.1.298; 3-hydroxypropanoate dehydrogenase (NADP+); 3-hydroxypropionate:NADP+ oxidoreductase. Cat No: EXWM-0207. | |
| 3-keto-5-aminohexanoate cleavage enzyme | Requires Zn2+. The enzyme, isolated from the bacteria Fusobacterium nucleatum and Cloacimonas acidaminovorans, is involved in the anaerobic fermentation of lysine. Group: Enzymes. Synonyms: kce (gene name). Enzyme Commission Number: EC 2.3.1.247. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2196; 3-keto-5-aminohexanoate cleavage enzyme; EC 2.3.1.247; kce (gene name). Cat No: EXWM-2196. | |
| 3-oxo-5,6-didehydrosuberyl-CoA thiolase | The enzyme acts in the opposite direction. The enzymes from the bacteria Escherichia coli and Pseudomonas sp. Y2 also have the activity of EC 2.3.1.174 (3-oxoadipyl-CoA thiolase). Group: Enzymes. Synonyms: paaJ (gene name). Enzyme Commission Number: EC 2.3.1.223. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2170; 3-oxo-5,6-didehydrosuberyl-CoA thiolase; EC 2.3.1.223; paaJ (gene name). Cat No: EXWM-2170. | |
| 4-hydroxy-2-oxohexanoate aldolase | Requires Mn2+ for maximal activity. The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 4.1.3.39, 4-hydroxy-2-oxovalerate aldolase. The enzyme forms a bifunctional complex with EC 1.2.1.87, propanal dehydrogenase (CoA-propanoylating), with a tight channel connecting the two subunits. Group: Enzymes. Synonyms: BphI. Enzyme Commission Number: EC 4.1.3.43. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4920; 4-hydroxy-2-oxohexanoate aldolase; EC 4.1.3.43; BphI. Cat No: EXWM-4920. | |
| 4-hydroxy-2-oxovalerate aldolase | Requires Mn2+ for maximal activity. The enzyme from the bacterium Pseudomonas putida is also stimulated by NADH. In some bacterial species the enzyme forms a bifunctional complex with EC 1.2.1.10, acetaldehyde dehydrogenase (acetylating). The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 4.1.3.43, 4-hydroxy-2-oxohexanoate aldolase. Group: Enzymes. Synonyms: 4-hydroxy-2-ketovalerate aldolase; HOA; DmpG; 4-hydroxy-2-oxovalerate pyruvate-lyase; 4-hydroxy-2-oxopentanoate pyruvate-lyase; BphI; 4-hydroxy-2-oxopentanoate pyruvate-lyase (acetaldehyde-forming). Enzyme Commission Number: EC 4.1.3.39. CAS No. 37325-52-3. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4915; 4-hydroxy-2-oxovalerate aldolase; EC 4.1.3.39; 37325-52-3; 4-hydroxy-2-ketovalerate aldolase; HOA; DmpG; 4-hydroxy-2-oxovalerate pyruvate-lyase; 4-hydroxy-2-oxopentanoate pyruvate-lyase; BphI; 4-hydroxy-2-oxopentanoate pyruvate-lyase (acetaldehyde-forming). Cat No: EXWM-4915. | |
| 4-nitrocatechol 4-monooxygenase | Contains FAD. The enzyme catalyses the oxidation of 4-nitrocatechol with the concomitant removal of the nitro group as nitrite. Forms a two-component system with a flavoprotein reductase. The enzymes from the bacteria Lysinibacillus sphaericus JS905 and Rhodococcus sp. strain PN1 were shown to also catalyse EC 1.14.13.29, 4-nitrophenol 2-monooxygenase while the enzyme from Pseudomonas sp. WBC-3 was shown to also catalyse EC 1.14.13.167, 4-nitrophenol 4-monooxygenase. Group: Enzymes. Enzyme Commission Number: EC 1.14.13.166. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0765; 4-nitrocatechol 4-monooxygenase; EC 1.14.13.166. Cat No: EXWM-0765. | |
| 4-sulfomuconolactone hydrolase | The enzyme was isolated from the bacteria Hydrogenophaga intermedia and Agrobacterium radiobacter S2. It catalyses a step in the degradation of 4-sulfocatechol. Group: Enzymes. Enzyme Commission Number: EC 3.1.1.92. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3521; 4-sulfomuconolactone hydrolase; EC 3.1.1.92. Cat No: EXWM-3521. | |
| 5-methyltetrahydrofolate: corrinoid/iron-sulfur protein Co-methyltransferase | Catalyses the transfer of a methyl group from the N5 group of methyltetrahydrofolate to the 5-methoxybenzimidazolylcobamide cofactor of a corrinoid/Fe-S protein. Involved, together with EC 1.2.7.4, carbon-monoxide dehydrogenase (ferredoxin) and EC 2.3.1.169, CO-methylating acetyl-CoA synthase, in the reductive acetyl coenzyme A (Wood-Ljungdahl) pathway of autotrophic carbon fixation in various bacteria and archaea. Group: Enzymes. Synonyms: acsE (gene name). Enzyme Commission Number: EC 2.1.1.258. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1862; 5-methyltetrahydrofolate: corrinoid/iron-sulfur protein Co-methyltransferase; EC 2.1.1.258; acsE (gene name). Cat No: EXWM-1862. | |
| 6-carboxytetrahydropterin synthase | Binds Zn2+. Isolated from the bacteria Bacillus subtilis and Escherichia coli. The reaction is part of the biosynthesis pathway of queuosine.The enzyme from Escherichia coli can also convert 6-pyruvoyl-5,6,7,8-tetrahydropterin and sepiapterin to 6-carboxy-5,6,7,8-tetrahydropterin. Group: Enzymes. Synonyms: CPH4 synthase; queD (gene name); ToyB; ykvK (gene name). Enzyme Commission Number: EC 4.1.2.50. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4887; 6-carboxytetrahydropterin synthase; EC 4.1.2.50; CPH4 synthase; queD (gene name); ToyB; ykvK (gene name). Cat No: EXWM-4887. | |
| 7,8-dihydroneopterin epimerase | The enzyme, which has been characterized in bacteria and plants, also has the activity of EC 4.1.2.25, dihydroneopterin aldolase. The enzyme from the bacterium Mycobacterium tuberculosis has an additional oxygenase function (EC 1.13.11.81, 7,8-dihydroneopterin oxygenase). Group: Enzymes. Enzyme Commission Number: EC 5.1.99.8. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5440; 7,8-dihydroneopterin epimerase; EC 5.1.99.8. Cat No: EXWM-5440. | |
| acetaldehyde dehydrogenase (acetylating) | Also acts, more slowly, on glycolaldehyde, propanal and butanal. In several bacterial species this enzyme forms a bifunctional complex with EC 4.1.3.39, 4-hydroxy-2-oxovalerate aldolase. The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 1.2.1.87, propanal dehydrogenase (propanoylating). Involved in the meta-cleavage pathway for the degradation of phenols, methylphenols and catechols. NADP+ can replace NAD+ but the rate of reaction is much slower. Group: Enzymes. Synonyms: aldehyde dehydrogenase (acylating); ADA; acylating acetaldehyde dehyrogenase; DmpF; BphJ. Enzyme Commission Number: EC 1.2.1.10. CAS No. 9028-91-5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1116; acetaldehyde dehydrogenase (acetylating); EC 1.2.1.10; 9028-91-5; aldehyde dehydrogenase (acylating); ADA; acylating acetaldehyde dehyrogenase; DmpF; BphJ. Cat No: EXWM-1116. | |
| acyl-homoserine-lactone acylase | Acyl-homoserine lactones (AHLs) are produced by a number of bacterial species and are used by them to regulate the expression of virulence genes in a process known as quorum-sensing. Each bacterial cell has a basal level of AHL and, once the population density reaches a critical level, it triggers AHL-signalling which, in turn, initiates the expression of particular virulence genes. Plants or animals capable of degrading AHLs would have a therapeutic advantage in avoiding bacterial infection as they could prevent AHL-signalling and the expression of virulence genes in quorum-sensing bacteria. This quorum-quenching enzyme removes the fatty-acid side chain from the homoserine l...ion, as found in N-(3-oxododecanoyl)-L-homoserine lactone, do not affect this activity. Group: Enzymes. Synonyms: acyl-homoserine lactone acylase; AHL-acylase; AiiD; N-acyl-homoserine lactone acylase; PA2385 protein; quorum-quenching AHL acylase; quorum-quenching enzyme; QuiP. Enzyme Commission Number: EC 3.5.1.97. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4489; acyl-homoserine-lactone acylase; EC 3.5.1.97; acyl-homoserine lactone acylase; AHL-acylase; AiiD; N-acyl-homoserine lactone acylase; PA2385 protein; quorum-quenching AHL acylase; quorum-quenching enzyme; QuiP. Cat No: EXWM-4489. | |
| adenylyl-sulfate kinase | The human phosphoadenosine-phosphosulfate synthase (PAPSS) system is a bifunctional enzyme (fusion product of two catalytic activities). In a first step, sulfate adenylyltransferase catalyses the formation of adenosine 5'-phosphosulfate (APS) from ATP and inorganic sulfate. The second step is catalysed by the adenylylsulfate kinase portion of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthase, which involves the formation of PAPS from enzyme-bound APS and ATP. In contrast, in bacteria, yeast, fungi and plants, the formation of PAPS is carried out by two individual polypeptides, sulfate adenylyltransferase (EC 2.7.7.4) and adenylyl-sulfate kinase (EC 2.7.1.25). Group: Enzymes. Synonyms: adenylylsulfate kinase (phosphorylating); 5'-phosphoadenosine sulfate kinase; adenosine 5'-phosphosulfate kinase; adenosine phosphosulfate kinase; adenosine phosphosulfokinase; . Enzyme Commission Number: EC 2.7.1.25. CAS No. 9012-38-8. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3055; adenylyl-sulfate kinase; EC 2.7.1.25; 9012-38-8; adenylylsulfate kinase (phosphorylating); 5'-phosphoadenosine sulfate kinase; adenosine 5'-phosphosulfate kinase; adenosine phosphosulfate kinase; adenosine phosphosulfokinase; adenosine-5'-phosphosulfate-3'-phosphokinase; APS kinase. Cat No: EXWM-3055. | |
| ADP-dependent NAD(P)H-hydrate dehydratase | Acts equally well on hydrated NADH and hydrated NADPH. NAD(P)H spontaneously hydrates to both the (6S)- and (6R)- isomers. The enzyme from bacteria consists of two domains, one of which acts as an NAD(P)H-hydrate epimerase that interconverts the two isomers to a 60:40 ratio (cf. EC 5.1.99.6), while the other catalyses the dehydration. Hence the enzyme can restore the complete mixture of isomers into NAD(P)H. The enzyme has no activity with ATP, contrary to the enzyme from eukaryotes (cf. EC 4.2.1.93, ATP-dependent NAD(P)H-hydrate dehydratase). Group: Enzymes. Synonyms: (6S)-β-6-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine-dinucleotide hydro-lyase(ADP-hydrolysing); (6S)-6-β-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine-dinucleotide hydro-lyase (ADP-hydrolysing; NADH-forming). Enzyme Commission Number: EC 4.2.1.136. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4977; ADP-dependent NAD(P)H-hydrate dehydratase; EC 4.2.1.136; (6S)-β-6-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine-dinucleotide hydro-lyase(ADP-hydrolysing); (6S)-6-β-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine-dinucleotide hydro-lyase (ADP-hydrolysing; NADH-forming). Cat No: EXWM-4977. | |
| aklavinone 12-hydroxylase | The enzymes from the Gram-positive bacteria Streptomyces peucetius and Streptomyces purpurascens participate in the biosynthesis of daunorubicin, doxorubicin and rhodomycins. The enzyme from Streptomyces purpurascens is an FAD monooxygenase. Group: Enzymes. Synonyms: DnrF; RdmE; aklavinone 11-hydroxylase (incorrect). Enzyme Commission Number: EC 1.14.13.180. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0779; aklavinone 12-hydroxylase; EC 1.14.13.180; DnrF; RdmE; aklavinone 11-hydroxylase (incorrect). Cat No: EXWM-0779. | |
| alanine carboxypeptidase | From soil bacteria. The enzyme from Corynebacterium equi also hydrolyses N-benzoylglycine and N-benzoyl-L-aminobutyric acid. Group: Enzymes. Synonyms: N-benzoyl-L-alanine-amidohydrolase. Enzyme Commission Number: EC 3.4.17.6. CAS No. 37288-70-3. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4079; alanine carboxypeptidase; EC 3.4.17.6; 37288-70-3; N-benzoyl-L-alanine-amidohydrolase. Cat No: EXWM-4079. | |
| Alanine Racemase (Crude Enzyme) | This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. This enzyme participates in alanine and aspartatemetabolism and D-alanine metabolism. It employs one cofactor, pyridoxal phosphate. At least two compounds, 3-Fluoro-D-alanine and D-Cycloserine are known to inhibit this enzyme. The D-alanine produced by alanine racemase is used for peptidoglycan biosynthesis. Peptidoglycan is found in the cell walls of all bacteria, including many which are harmful to humans. The enzyme is absent in higher eukaryotes but found everywhere in prokaryotes, making alanine racemase a great target for antimicrobial drug...udies have shown that without the alr gene being expressed, the bacteria would need an external source of D-alanine in order to survive. Therefore, the alr gene is a feasible target for antimicrobial drugs. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Drug development; pharmacology; medicine; pharmacology. Group: Enzymes. Synonyms: L-alanine racemase. Enzyme Commission Number: EC 5.1.1.1. CAS No. 9024-06-0. Alanine Racemase. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. L-alanine racemase. Pack: 100ml. Cat No: NATE-1854. | |
| allantoate deiminase | This enzyme is part of the ureide pathway, which permits certain organisms to recycle the nitrogen in purine compounds. This enzyme, which liberates ammonia from allantoate, is present in plants and bacteria. In plants it is localized in the endoplasmic reticulum. Requires manganese. Group: Enzymes. Synonyms: allantoate amidohydrolase. Enzyme Commission Number: EC 3.5.3.9. CAS No. 37289-13-7. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4535; allantoate deiminase; EC 3.5.3.9; 37289-13-7; allantoate amidohydrolase. Cat No: EXWM-4535. | |
| allophanate hydrolase | Along with EC 3.5.2.15 (cyanuric acid amidohydrolase) and EC 3.5.1.84 (biuret amidohydrolase), this enzyme forms part of thecyanuric-acid metabolism pathway, which degrades s-triazide herbicides, such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine], in bacteria. The yeast enzyme (but not that from green algae) also catalyses the reaction of EC 6.3.4.6, urea carboxylase, thus bringing about the hydrolysis of urea to CO2 and NH3 in the presence of ATP and bicarbonate. The enzyme from Pseudomonas sp. strain ADP has a narrow substrate specificity, being unable to use the structurally analogous compounds urea, hydroxyurea or methylcarbamate as substrate. Group: Enzymes. Synonyms: allophanate lyase; AtzF; TrzF. Enzyme Commission Number: EC 3.5.1.54. CAS No. 9076-72-6. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4443; allophanate hydrolase; EC 3.5.1.54; 9076-72-6; allophanate lyase; AtzF; TrzF. Cat No: EXWM-4443. | |
| α-mannan endo-1,2-α-mannanase | The enzyme, characterized from the gut bacteria Bacteroides thetaiotaomicron and Bacteroides xylanisolvens, can also catalyse the reaction of EC 3.2.1.130, glycoprotein endo-α-1,2-mannosidase. Group: Enzymes. Enzyme Commission Number: EC 3.2.1.198. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3882; α-mannan endo-1,2-α-mannanase; EC 3.2.1.198. Cat No: EXWM-3882. | |
| α-N-Acetylgalactosaminidase from Chryseobacterium meningosepticum, Recombinant | α-N-acetylgalactosaminidase (EC 3.2.1.49) is a glycoside hydrolase from bacteria and animals, also known as nagalase. The human gene that codes for this enzyme is NAGA. Mutations in this gene and the deficiency in alpha-N-acetylgalactosaminidase activity have been identified as the cause of Schindler disease. Group: Enzymes. Synonyms: EC 3.2.1.49; α-N-acetylgalactosaminidase; Alpha-N-acetylgalactosaminidase; α-acetylgalactosaminidase; N-acetyl-α-D-galactosaminidase; N-acetyl-α-galactosaminidase; α-NAGAL; α-NAGA; α-GalNAcase. α-NAGA. Mole weight: 47 kDa. Storage: at -20°C. Source: E. coli. Species: Chryseobacterium meningosepticum. EC 3.2.1.49; α-N-acetylgalactosaminidase; Alpha-N-acetylgalactosaminidase; α-acetylgalactosaminidase; N-acetyl-α-D-galactosaminidase; N-acetyl-α-galactosaminidase; α-NAGAL; α-NAGA; α-GalNAcase. Cat No: NATE-1259. | |
| Arginine Deiminase (Crude Enzyme) | 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. This enzyme is widely expressed in bacteria, including streptococcus and actinomyces. The bacterial arginine deiminase expression could be regulated by various environmental factors. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Drug development; medicine; pharmacology. Group: Enzymes. Synonyms: arginine dihydrolase; citrulline iminase; L-arginine deiminase. Enzyme Commission Number: EC 3.5.3.6. CAS No. 9027-98-9. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. arginine dihydrolase; citrulline iminase; L-arginine deiminase. Pack: 100ml. Cat No: NATE-1841. | |
| arogenate dehydrogenase | Arogenate dehydrogenases may utilize NAD+ (EC 1.3.1.43), NADP+ (EC 1.3.1.78), or both (EC 1.3.1.79). NAD+-specific enzymes have been reported from some bacteria and plants. Some enzymes also possess the activity of EC 1.3.1.12, prephenate dehydrogenase. Group: Enzymes. Synonyms: arogenic dehydrogenase (ambiguous); cyclohexadienyl dehydrogenase; pretyrosine dehydrogenase (ambiguous); L-arogenate:NAD+ oxidoreductase; arogenate dehydrogenase (NAD+). Enzyme Commission Number: EC 1.3.1.43. CAS No. 64295-75-6. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1315; arogenate dehydrogenase; EC 1.3.1.43; 64295-75-6; arogenic dehydrogenase (ambiguous); cyclohexadienyl dehydrogenase; pretyrosine dehydrogenase (ambiguous); L-arogenate:NAD+ oxidoreductase; arogenate dehydrogenase (NAD+). Cat No: EXWM-1315. | |
| arsenate reductase (glutaredoxin) | A molybdoenzyme. The enzyme is part of a system for detoxifying arsenate. Although the arsenite formed is more toxic than arsenate, it can be extruded from some bacteria by EC 3.6.3.16, arsenite-transporting ATPase; in other organisms, arsenite can be methylated by EC 2.1.1.137, arsenite methyltransferase, in a pathway that produces non-toxic organoarsenical compounds. cf. EC 1.20.4.4, arsenate reductase (thioredoxin). Group: Enzymes. Synonyms: ArsC (ambiguous). Enzyme Commission Number: EC 1.20.4.1. CAS No. 146907-46-2. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1240; arsenate reductase (glutaredoxin); EC 1.20.4.1; 146907-46-2; ArsC (ambiguous). Cat No: EXWM-1240. | |
| arsenate reductase (thioredoxin) | The enzyme, characterized in bacteria of the Firmicutes phylum, is specific for thioredoxin. It has no activity with glutaredoxin [cf. EC 1.20.4.1, arsenate reductase (glutaredoxin)]. Although the arsenite formed is more toxic than arsenate, it can be extruded from some bacteria by EC 3.6.3.16, arsenite-transporting ATPase; in other organisms, arsenite can be methylated by EC 2.1.1.137, arsenite methyltransferase, in a pathway that produces non-toxic organoarsenical compounds. The enzyme also has the activity of EC 3.1.3.48, protein-tyrosine-phosphatase. Group: Enzymes. Synonyms: ArsC (ambiguous). Enzyme Commission Number: EC 1.20.4.4. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1243; arsenate reductase (thioredoxin); EC 1.20.4.4; ArsC (ambiguous). Cat No: EXWM-1243. | |
| aryl-sulfate sulfotransferase | The enzyme, characterized from bacteria that colonize the human and mouse intestine, catalyses the transfer of a sulfate group from a phenol sulfate ester to other phenolic compounds. Activity is enhanced by Mg2+ and Mn2+. Unlike EC 2.8.2.9, tyrosine-ester sulfotransferase and EC 2.8.2.1, aryl sulfotransferase, the enzyme does not act on 3'-phosphoadenylyl sulfate or adenosine 3',5'-bisphosphate.The level of sulfation of polyphenols depends on the positions of the hydroxyl groups. Hydroxy groups of tyrosine residues in peptides such as angiotensin can also act as acceptors. The reaction proceeds according to a ping pong bi bi mechanism. Group: Enzymes. Synonyms: arylsulfate-phenol sulfotransferase; arylsulfotransferase; ASST; arylsulfate sulfotransferase; arylsulfate:phenol sulfotransferase; astA (gene name). Enzyme Commission Number: EC 2.8.2.22. CAS No. 158254-86-5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3381; aryl-sulfate sulfotransferase; EC 2.8.2.22; 158254-86-5; arylsulfate-phenol sulfotransferase; arylsulfotransferase; ASST; arylsulfate sulfotransferase; arylsulfate:phenol sulfotransferase; astA (gene name). Cat No: EXWM-3381. | |
| assimilatory sulfite reductase (ferredoxin) | An iron protein. The enzyme participates in sulfate assimilation. While it is usually found in cyanobacteria, plants and algae, it has also been reported in bacteria. Different from EC 1.8.99.5, dissimilatory sulfite reductase, which is involved in prokaryotic sulfur-based energy metabolism. cf. EC 1.8.1.2, assimilatory sulfite reductase (NADPH). Group: Enzymes. Synonyms: ferredoxin-sulfite reductase; SIR (gene name); sulfite reductase (ferredoxin). Enzyme Commission Number: EC 1.8.7.1. CAS No. 37256-50-1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1680; assimilatory sulfite reductase (ferredoxin); EC 1.8.7.1; 37256-50-1; ferredoxin-sulfite reductase; SIR (gene name); sulfite reductase (ferredoxin). Cat No: EXWM-1680. | |
| assimilatory sulfite reductase (NADPH) | Contains siroheme, [4Fe-4S] cluster, FAD and FMN. The enzyme, which catalyses the six-electron reduction of sulfite to sulfide, is involved in sulfate assimilation in bacteria and yeast. Different from EC 1.8.99.5, dissimilatory sulfite reductase, which is involved in prokaryotic sulfur-based energy metabolism. cf. EC 1.8.7.1, assimilatory sulfite reductase (ferredoxin). Group: Enzymes. Synonyms: sulfite reductase (NADPH); sulfite (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADPH-sulfite reductase; NADPH-dependent sulfite reductase; H2S-NADP oxidoreductase; sulfite reductase (NADPH2); MET5 (gene name); MET10 (gene name); cysI (gene name); cysJ (gene name). Enzyme Commission Number: EC 1.8.1.2. CAS No. 9029-35-0. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1646; assimilatory sulfite reductase (NADPH); EC 1.8.1.2; 9029-35-0; sulfite reductase (NADPH); sulfite (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADPH-sulfite reductase; NADPH-dependent sulfite reductase; H2S-NADP oxidoreductase; sulfite reductase (NADPH2); MET5 (gene name); MET10 (gene name); cysI (gene name); cysJ (gene name). Cat No: EXWM-1646. | |
| ATP-dependent NAD(P)H-hydrate dehydratase | Acts equally well on hydrated NADH and hydrated NADPH. NAD(P)H spontaneously hydrates to both the (6S)- and (6R)- isomers, and these are interconverted by EC 5.1.99.6, NAD(P)H-hydrate epimerase, to a 60:40 ratio. Hence EC 4.2.1.93 together with EC 5.1.99.6 can restore the mixture of hydrates into NAD(P)H. The enzyme from eukaryotes has no activity with ADP, contrary to the enzyme from bacteria (cf. EC 4.2.1.136, ADP-dependent NAD(P)H-hydrate dehydratase). Group: Enzymes. Synonyms: reduced nicotinamide adenine dinucleotide hydrate dehydratase; ATP-dependent H4NAD(P)+OH dehydratase; (6S)-β-6-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine-dinucleotide hydro-lyase(ATP-hydrolysing); (6S)-6-β-hydroxy-1,4,5,6-tetrahydronicotinamide-. Enzyme Commission Number: EC 4.2.1.93. CAS No. 116669-08-0. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5077; ATP-dependent NAD(P)H-hydrate dehydratase; EC 4.2.1.93; 116669-08-0; reduced nicotinamide adenine dinucleotide hydrate dehydratase; ATP-dependent H4NAD(P)+OH dehydratase; (6S)-β-6-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine-dinucleotide hydro-lyase(ATP-hydrolysing); (6S)-6-β-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine-dinucleotide hydro-lyase (ATP-hydrolysing; NADH-forming). Cat No: EXWM-5077. | |
| β-Agarase I from E. coli, Recombinant | Agarase is an enzyme with system name agarose 4-glycanohydrolase. It found in agarolytic bacteria and is the first enzyme in the agar catabolic pathway. It is responsible for allowing them to use agar as their primary source of Carbon and enables their ability to thrive in the ocean. Agarases are classified as either α-agarases or β-agarases based upon whether they degrade αor β linkages in agarose, breaking them into oligosaccharides. When secreted, α-agarases yield oligosaccharides with 3.6 anhydro-L-galactose at the reducing end whereas β-agarases result in D-galactose residues. Β-agarase cleaves the agarose subunit, unsubstituted...garase i can be used to purify both large (> 50 kb) and small (< 50 kb) fragments of dna from gels. the remaining carbohydrate molecules and β-agarase i will not, in general, interfere with subsequent dna manipulations such as restriction endonuclease digestion, ligation, and transformation. Group: Enzymes. Synonyms: agarase; AgaA; AgaB; endo-β-agarase; agarose 3-glycanohydrolase; EC 3.2.1.81; 37288-57-6. Agarase. Storage: at -20°C. Form: 50 mM Bis Tris-HCl (pH 6.5), 1 mM Na2EDTA and 50% glycerol. Source: E. coli. Species: E. coli. agarase; AgaA; AgaB; endo-β-agarase; agarose 3-glycanohydrolase; EC 3.2.1.81; 37288-57-6; β-Agarase I. Cat No: NATE-1282. | |
| betaine-aldehyde dehydrogenase | In many bacteria, plants and animals, the osmoprotectant betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. This enzyme is involved in the second step and appears to be the same in plants, animals and bacteria. In contrast, different enzymes are involved in the first reaction. In plants, this reaction is catalysed by EC 1.14.15.7 (choline monooxygenase), whereas in animals and many bacteria it is catalysed by either membrane-bound EC 1.1.99.1 (choline dehydrogenase) or soluble EC 1.1.3.17 (choline oxidase). In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 (glycine/sarcosine N-methyltransferase) and EC 2.1.1.157 (sarcosine/dimethylglycine N-methyltransferase). Group: Enzymes. Synonyms: betaine aldehyde oxidase; BADH; betaine aldehyde dehydrogenase; BetB. Enzyme Commission Number: EC 1.2.1.8. CAS No. 9028-90-4. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1182; betaine-aldehyde dehydrogenase; EC 1.2.1.8; 9028-90-4; betaine aldehyde oxidase; BADH; betaine aldehyde dehydrogenase; BetB. Cat No: EXWM-1182. | |
| Beta Lactamase from E.coli, Recombinant | Beta-lactamase is a type of enzyme (EC 3.5.2.6) produced by some bacteria that is responsible for their resistance to beta-lactam antibiotics like penicillins, cephalosporins, cephamycins and carbapenems. These antibiotics have a common element in their molecular structure: a four-atom ring known as a beta-lactam. The lactamase enzyme breaks that ring open, deactivating the molecule's antibacterial properties. Group: Enzymes. Synonyms: b-Lactamase; EC 3.5.2.6; TEM precursor; β-lactamase. Enzyme Commission Number: EC 3.5.2.6. Purity: Greater than 90.0% as determined by: (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. β-Lactamase. Mole weight: 29 kDa. Activity: 700IU/mg. Stability: Lyophilized Beta Lactamase although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Beta Lactamase Recombinant should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles. Form: Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM Phosphate buffer pH-7. Source: E. coli. Species: E. coli. b-Lactamase; EC 3.5.2.6; TEM precursor; β-lactamase. Cat No: NATE-1886. | |
| bile acid CoA-transferase | The enzyme, characterized from the gut bacterium Clostridium scindens, catalyses the last step in bile acid 7α-dehydroxylation, the removal of the CoA moiety from the products. By using a transferase rather than hydrolase, the bacteria conserve the thioester bond energy, saving ATP molecules. Clostridium scindens possesses two forms of the enzyme, encoded by the baiF and baiK genes. While the enzymes have a broad acceptor specificity and can use allocholate, ursodeoxycholate, and β-muricholate, the donor specificity is more strict. BaiF acts on lithocholoyl-CoA and deoxycholoyl-CoA, and BaiK acts only on the latter. Group: Enzymes. Synonyms: baiF (gene name); baiK (gene name); bile acid coenzyme A transferase. Enzyme Commission Number: EC 2.8.3.25. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3421; bile acid CoA-transferase; EC 2.8.3.25; baiF (gene name); baiK (gene name); bile acid coenzyme A transferase. Cat No: EXWM-3421. | |
| Biotin | Biotin, also known as vitamin B7, is a water-soluble enzyme cofactor generated by intestinal bacteria or obtained from diet. Biotin is a growth factor present in minute amounts in every living cell. It is involved in metabolism of fats and carbohydrates, cell growth, as well as protein synthesis. Vitamin supplement in health care products. Uses: Ingredient of health care products. Synonyms: D-biotin; Vitamin H; Coenzyme R; Vitamin B7; BIOTIN; 1H-Thieno[3,4-d]imidazole-4-pentanoic acid, hexahydro-2-oxo-, [3aS-(3aα,4β,6aα)]-; FACTOR S; BIOS H; Ritatin; biosii; BIOTINUM; D-Biotin; Bios-IIb; Meribin; cis-Tetrahydro-2-oxothieno(3,4-d)imidazoline-4-valeric acid; 1swk; Meribin; Factor S (vitamin); Injacom H; Lutavit H2; D-Biotin. Grades: 98%. CAS No. 58-85-5. Molecular formula: C10H16N2O3S. Mole weight: 244.31. |  |
| bleomycin hydrolase | The molecule is a homohexamer in which the monomers have a papain-like tertiary structure (in peptidase family C1). The active sites are on the walls of a central channel through the molecule, and access of substrate molecules to them is obstructed by this and by the C-terminus of each polypeptide chain. Bleomycin can scarcely be the natural substrate, and there are reports of limited endopeptidase activity. Known from bacteria as well as eukaryotic organisms. Hydrolase H from chicken muscle has many similarities to bleomycin hydrolase, but hydrolyses Ph-CO-Arg-2-naphthylamine as well as aminopeptidase substrates. Group: Enzymes. Synonyms: aminopeptidase C (Lactococcus lactis). Enzyme Commission Number: EC 3.4.22.40. CAS No. 53096-17-6. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4215; bleomycin hydrolase; EC 3.4.22.40; 53096-17-6; aminopeptidase C (Lactococcus lactis). Cat No: EXWM-4215. | |
| butanoyl-CoA dehydrogenase (NAD+, ferredoxin) | This flavin containg enzyme, isolated from the bacteria Acidaminococcus fermentans and butanoate-producing Clostridia species, couples the exergonic reduction of (E)-but-2-enoyl-CoA to butanoyl-CoA with NADH to the endergonic reduction of ferredoxin by NADH, using electron bifurcation to overcome the steep energy barrier in ferredoxin reduction. Group: Enzymes. Synonyms: bifurcating butyryl-CoA dehydrogenase; butyryl-CoA dehydrogenase/Etf complex; Etf-Bcd complex; bifurcating butanoyl-CoA dehydrogenase; butanoyl-CoA dehydrogenase/Etf complex. Enzyme Commission Number: EC 1.3.1.109. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1281; butanoyl-CoA dehydrogenase (NAD+, ferredoxin); EC 1.3.1.109; bifurcating butyryl-CoA dehydrogenase; butyryl-CoA dehydrogenase/Etf complex; Etf-Bcd complex; bifurcating butanoyl-CoA dehydrogenase; butanoyl-CoA dehydrogenase/Etf complex. Cat No: EXWM-1281. | |
| capsular-polysaccharide-transporting ATPase | ABC-type (ATP-binding cassette-type) ATPase, characterized by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. An enzyme that exports capsular polysaccharide from Gram-negative bacteria. Group: Enzymes. Enzyme Commission Number: EC 3.6.3.38. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4676; capsular-polysaccharide-transporting ATPase; EC 3.6.3.38. Cat No: EXWM-4676. | |
| carminomycin 4-O-methyltransferase | The enzymes from the Gram-positive bacteria Streptomyces sp. C5 and Streptomyces peucetius are involved in the biosynthesis of the anthracycline daunorubicin. In vitro the enzyme from Streptomyces sp. C5 also catalyses the 4-O-methylation of 13-dihydrocarminomycin, rhodomycin D and 10-carboxy-13-deoxycarminomycin. Group: Enzymes. Synonyms: DnrK; DauK. Enzyme Commission Number: EC 2.1.1.292. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1899; carminomycin 4-O-methyltransferase; EC 2.1.1.292; DnrK; DauK. Cat No: EXWM-1899. | |
| Catalase (Crude Enzyme) | Catalase is a common enzyme found in nearly all living organisms exposed to oxygen (such as bacteria, plants, and animals). It catalyzes the decomposition of hydrogen peroxide to water and oxygen. It is a very important enzyme in protecting the cell from oxidative damage by reactive oxygen species (ROS). Likewise, catalase has one of the highest turnover numbers of all enzymes; one catalase molecule can convert approximately 5 million molecules of hydrogen peroxide to water and oxygen each minute. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Medicine; synthesis; analysis; biotechnology; industry. Group: Enzymes. Synonyms: hydrogen-peroxide:hydrogen-peroxide oxidoreductase. Enzyme Commission Number: EC 1.11.1.6. CAS No. 9001-5-2. CAT. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. hydrogen-peroxide:hydrogen-peroxide oxidoreductase. Pack: 100ml. Cat No: NATE-1795. | |
| CDP-paratose synthase | The enzyme is involved in synthesis of paratose and tyvelose, unusual 3,6-dideoxyhexose sugars that form part of the O-antigen in the lipopolysaccharides of several enteric bacteria. Isolated from Salmonella enterica subsp. enterica serovar Typhi (Salmonella typhi). Group: Enzymes. Synonyms: rfbS (gene name). Enzyme Commission Number: EC 1.1.1.342. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0257; CDP-paratose synthase; EC 1.1.1.342; rfbS (gene name). Cat No: EXWM-0257. | |
| cellobionic acid phosphorylase | The enzyme occurs in cellulolytic bacteria and fungi. It catalyses the reversible phosphorolysis of cellobionic acid. In the synthetic direction it produces 4-O-β-D-glucopyranosyl-D-glucuronate from α-D-glucose 1-phosphate and D-glucuronate with low activity. Group: Enzymes. Enzyme Commission Number: EC 2.4.1.321. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2558; cellobionic acid phosphorylase; EC 2.4.1.321. Cat No: EXWM-2558. | |
| chloramphenicol O-acetyltransferase | Chloramphenicol acetyltransferase (or CAT) is a bacterial enzyme (EC 2.3.1.28) that detoxifies the antibiotic chloramphenicol and is responsible for chloramphenicol resistance in bacteria. This enzyme covalently attaches an acetyl group from acetyl-CoA to chloramphenicol, which prevents chloramphenicol from binding to ribosomes. A histidine residue, located in the C-terminal section of the enzyme, plays a central role in its catalytic mechanism. Group: Enzymes. Synonyms: chloramphenicol acetyltransferase; chloramphenicol acetylase; chloramphenicol transacetylase; CAT I; CAT II; CAT III. Enzyme Commission Number: EC 2.3.1.28. CAS No. 9040-7-7. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2205; chloramphenicol O-acetyltransferase; EC 2.3.1.28; 9040-07-7; chloramphenicol acetyltransferase; chloramphenicol acetylase; chloramphenicol transacetylase; CAT I; CAT II; CAT III. Cat No: EXWM-2205. | |
| chlorophyllide a hydrolase | This enzyme, found in green sulfur bacteria (Chlorobiaceae) and green filamentous bacteria (Chloroflexaceae), catalyses the first committed step in the biosynthesis of bacteriochlorophylls c, d and e, the removal of the C-132-methylcarboxyl group from chlorophyllide a. The reaction is very similar to the conversion of pheophorbide a to pyropheophorbide a during chlorophyll a degradation, which is catalysed by EC 3.1.1.82, pheophorbidase. Group: Enzymes. Synonyms: bciC (gene name). Enzyme Commission Number: EC 3.1.1.100. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3436; chlorophyllide a hydrolase; EC 3.1.1.100; bciC (gene name). Cat No: EXWM-3436. | |
| choline monooxygenase | The spinach enzyme, which is located in the chloroplast, contains a Rieske-type [2Fe-2S] cluster, and probably also a mononuclear Fe centre. Requires Mg2+. Catalyses the first step of glycine betaine synthesis. In many bacteria, plants and animals, betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. Different enzymes are involved in the first reaction. In plants, the reaction is catalysed by this enzyme whereas in animals and many bacteria it is catalysed by either membrane-bound EC 1.1.99.1 (choline dehydrogenase) or soluble EC 1.1.3.17 (choline oxidase). The enzyme involved in the second step, EC 1.2.1.8 (betaine-aldehyde dehydrogenase), appears to be the same in plants, animals and bacteria. In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 (glycine/sarcosine N-methyltransferase) and EC 2.1.1.157 (sarcosine/dimethylglycine N-methyltransferase). Group: Enzymes. Enzyme Commission Number: EC 1.14.15.7. CAS No. 118390-76-4. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0950; choline monooxygenase; EC 1.14.15.7; 118390-76-4. Cat No: EXWM-0950. | |
| chorismate lyase | This enzyme catalyses the first step in the biosynthesis of ubiquinone in Escherichia coli and other Gram-negative bacteria. The yeast Saccharomyces cerevisiae can synthesize ubiquinone from either chorismate or tyrosine. Group: Enzymes. Synonyms: CL; CPL; UbiC. Enzyme Commission Number: EC 4.1.3.40. CAS No. 157482-18-3. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4917; chorismate lyase; EC 4.1.3.40; 157482-18-3; CL; CPL; UbiC. Cat No: EXWM-4917. | |
| Cilastatin Ammonium Salt | Cilastatin Ammonium Salt is the ammonium salt of Cilastatin, which is a dipeptidase inhibitor of renal enzyme dehydropeptidase-I and leukotriene D4 peptidase. It inhibits metabolism of LTD4 to LTE4 and the hydrolysis of β-lactam antibiotics. It reduces toxic accumulation of cyclosporin A in kidney proximal tubule epithelial cells. It can be combined intravenously with imipenem in order to protect it from dehydropeptidase. It suppresses both host and target metabolism of the broad-spectrum antibiotic imipenem, improving its efficacy. It usually confers antibiotic resistance to certain bacteria because itself does not have antibiotic activity. It has nephroprotective effects. Synonyms: (2Z)-7-[[(2R)-2-amino-2-carboxyethyl]thio]-2-[[[(1S)-2,2-dimethylcyclopropyl]carbonyl]amino]-2-heptenoic Acid Ammonium Salt; MK-791 Ammonium Salt. Grades: > 95%. CAS No. 877674-82-3. Molecular formula: C16H29N3O5S. Mole weight: 375.48. | |
| Cilastatin sodium | Cilastatin sodium is the sodium salt of cilastatin, which is a dipeptidase inhibitor of renal enzyme dehydropeptidase-I and leukotriene D4 peptidase. It inhibits metabolism of LTD4 to LTE4 and the hydrolysis of β-lactam antibiotics. It reduces toxic accumulation of cyclosporin A in kidney proximal tubule epithelial cells. It can be combined intravenously with imipenem in order to protect it from dehydropeptidase. It suppresses both host and target metabolism of the broad-spectrum antibiotic imipenem, improving its efficacy. It usually confers antibiotic resistance to certain bacteria because itself does not have antibiotic activity. It has nephroprotective effects. Synonyms: L 642957; MK 791; L642957; MK791; L-642957; MK-791; [R-[R*,S*-(Z)]]-7-[(2-Amino-2-carboxyethyl)thio]-2-[[(2,2-dimethylcyclopropyl)carbonyl]amino]-2-heptenoic Acid Monosodium Salt; (2Z) ?-7- [ [ (2R) ?-2-Amino-2-carboxyethyl] ?thio] ?-2- [ [ [ (1S) ?-2, ?2-dimethylcyclopropyl] ?carbonyl] ?amino] ?-2-heptenoic Acid Sodium Salt; sodium S-((Z)-6-carboxy-6-((S)-2,2-dimethylcyclopropane-1-carboxamido)hex-5-en-1-yl)-L-cysteinate. Grades: ≥99% by HPLC. CAS No. 81129-83-1. Molecular formula: C16H25N2NaO5S. Mole weight: 380.43. | |
| Ciprofloxacin Hydrochloride 10mg/ml | Ciprofloxacin Hydrochloride is a high activity fluoroquinolone antibiotic effective against a broad spectrum of gram positive and negative bacteria such as Pseudomonas, Salmonella, streptococcus and Staphylococcus. Effective against mycoplasma (12 days). Ciprofloxacin differs from other quinolones in that it has a fluorine atom at the 6-position, a piperazine moiety at the 7-position, and a cyclopropyl ring at the 1-position. The bactericidal action of ciprofloxacin results from interference with the enzyme DNA gyrase which is needed for the synthesis of bacterial DNA. Ciprofloxacin has been shown to be active against most strains of the following organisms:Gram-Positive Ba...aris; Providencia rettgeri; Providencia stuartii; Pseudomonas aeruginosa; Salmonella enteritidis; Salmonella typhi; Serratia marcescens; Shigella flexneri; Shigella sonnei; Vibrio cholerae; Vibrio parahaemolyticus; Vibrio vulnificus; Yersinia enterocolitica. Other Organisms:Chlamydia trachomatis (only moderately susceptible); Mycobacterium tuberculosis (only moderately susceptible).Also Available:C5074: Ciprofloxacin Hydrochloride. Group: Biochemicals. Alternative Names: Sterile-filtered aqueous solution. Grades: Molecular Biology Grade. CAS No. 86393-32-0. Pack Sizes: 10ml, 5x10ml. Molecular Formula: C17H18FN3O3 HCl H2O, Molecular Weight: 385.8. US Biological Life Sciences. |  Worldwide |
| Ciprofloxacin Hydrochloride, Monohydrate | Ciprofloxacin Hydrochloride is a high activity fluoroquinolone antibiotic effective against a broad spectrum of gram positive and negative bacteria such as Pseudomonas, Salmonella, streptococcus and Staphylococcus. Effective against mycoplasma (12 days). Ciprofloxacin differs from other quinolones in that it has a fluorine atom at the 6-position, a piperazine moiety at the 7-position, and a cyclopropyl ring at the 1-position. The bactericidal action of ciprofloxacin results from interference with the enzyme DNA gyrase which is needed for the synthesis of bacterial DNA. Ciprofloxacin has been shown to be active against most strains of the following organisms:Gram-Positive ...a typhi; Serratia marcescens; Shigella flexneri; Shigella sonnei; Vibrio cholerae; Vibrio parahaemolyticus; Vibrio vulnificus; Yersinia enterocolitica. Other Organisms:Chlamydia trachomatis (only moderately susceptible); Mycobacterium tuberculosis (only moderately susceptible).Also Available:C5075: Ciprofloxacin Hydrochloride 10mg/ml. Group: Biochemicals. Alternative Names: 1-Cyclopropyl-6-fluoro-1,4-dihydro-4-oxo-7-(1-piperazinyl)-3-quinolinecarboxylic Acid Hydrochloride; Bay Q3939 Hydrochloride. Grades: Molecular Biology Grade. CAS No. 86393-32-0. Pack Sizes: 1g, 10g, 25g, 50g. Molecular Formula: C17H18FN3O3 HCl H2O, Molecular Weight: 385.8. US Biological Life Sciences. | Worldwide |
| CMP-N,N'-diacetyllegionaminic acid synthase | Isolated from the bacteria Legionella pneumophila and Campylobacter jejuni. Involved in biosynthesis of legionaminic acid, a sialic acid-like derivative that is incorporated into virulence-associated cell surface glycoconjugates which may include lipopolysaccharide (LPS), capsular polysaccharide, pili and flagella. Group: Enzymes. Synonyms: CMP-N,N'-diacetyllegionaminic acid synthetase; neuA (gene name); legF (gene name). Enzyme Commission Number: EC 2.7.7.82. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3295; CMP-N,N'-diacetyllegionaminic acid synthase; EC 2.7.7.82; CMP-N,N'-diacetyllegionaminic acid synthetase; neuA (gene name); legF (gene name). Cat No: EXWM-3295. | |
| CoA:oxalate CoA-transferase | The enzymes characterized from the bacteria Escherichia coli and Acetobacter aceti can also use formyl-CoA and oxalate (EC 2.8.3.16, formyl-CoA transferase) or formyl-CoA and acetate, with significantly reduced specific activities. Group: Enzymes. Synonyms: acetyl-coenzyme A transferase; acetyl-CoA oxalate CoA-transferase; ACOCT; YfdE; UctC. Enzyme Commission Number: EC 2.8.3.19. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3414; CoA:oxalate CoA-transferase; EC 2.8.3.19; acetyl-coenzyme A transferase; acetyl-CoA oxalate CoA-transferase; ACOCT; YfdE; UctC. Cat No: EXWM-3414. | |
| coproporphyrinogen dehydrogenase | This enzyme differs from EC 1.3.3.3, coproporphyrinogen oxidase, by using S-adenosyl-L-methionine (AdoMet) instead of oxygen as oxidant. It occurs mainly in bacteria, whereas eukaryotes use the oxygen-dependent oxidase. The reaction starts by using an electron from the reduced form of the enzyme's [4Fe-4S] cluster to split AdoMet into methionine and the radical 5'-deoxyadenosin-5'-yl. This radical initiates attack on the 2-carboxyethyl groups, leading to their conversion into vinyl groups. This conversion, -?CH-CH2-COO- ? -CH=CH2 + CO2 + e- replaces the electron initially used. Group: Enzymes. Synonyms: oxygen-independent coproporphyrinogen-III oxidase; HemN; coproporphyrinogen III oxidase. Enzyme Commission Number: EC 1.3.98.3. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1418; coproporphyrinogen dehydrogenase; EC 1.3.98.3; oxygen-independent coproporphyrinogen-III oxidase; HemN; coproporphyrinogen III oxidase. Cat No: EXWM-1418. | |
| Cyclodextrins | Cyclodextrins occur as white, practically odorless, fine crystalline powders, having a slightly sweet taste. Some cyclodextrin derivatives occur as amorphous powders. Synonyms: Cavitron; cyclic oligosaccharide; cycloamylose; cycloglucan; Encapsin; Schardinger dextrin. Product ID: PE-0591. Category: Solubilizing Agents; Stabilizing Agents. Product Keywords: Stabilizers; Solubilizer Excipients; PE-0591; Cyclodextrins; Solubilizing Agents; Stabilizing Agents;. UNII: Z1LH97KTRM. Grade: Pharmceutical Excipients. Administration route: α-cyclodextrin (injection); β-cyclodextrin (oral; topical); γ-cyclodextrin (IV injections). Dosage Form: α-cyclodextrin (injection preparations); β-cyclodextrin (oral tablets, topical gels); γ-cyclodextrin (IV injections). Stability and Storage Conditions: β-Cyclodextrin and other cyclodextrins are stable in the solid state if protected from high humidity. Cyclodextrins should be stored in a tightly sealed container, in a cool, dry place. Source and Preparation: Cyclodextrins are manufactured by the enzymatic degradation of starch using specialized bacteria. For example, b-cyclodextrin is produced by the action of the enzyme cyclodextrin glucosyltransferase upon starch or a starch hydrolysate. An organic solvent is used to direct the reaction that produces b-cyclodextrin, and to prevent the growth of microorganisms during the enzymatic reaction. The inso |  |
| cyclo(L-leucyl-L-leucyl) synthase | The reaction proceeds following a ping-pong mechanism forming a covalent intermediate between an active site serine and the first L-leucine residue. The proteins from bacteria of the genus Bacillus also form small amounts of cyclo(L-phenylalanyl-L-leucyl) and cyclo(L-leucyl-L-methionyl). Group: Enzymes. Synonyms: YvmC; cLL synthase; cyclodileucine synthase. Enzyme Commission Number: EC 2.3.2.22. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2296; cyclo(L-leucyl-L-leucyl) synthase; EC 2.3.2.22; YvmC; cLL synthase; cyclodileucine synthase. Cat No: EXWM-2296. | |
| cytochrome-c oxidase | A cytochrome of the a type containing copper. The reduction of O2 to water is accompanied by the extrusion of four protons from the intramitochondrial compartment. Several bacteria appear to contain analogous oxidases. Group: Enzymes. Synonyms: cytochrome oxidase; cytochrome a3; cytochrome aa3; Warburg's respiratory enzyme; indophenol oxidase; indophenolase; complex IV (mitochondrial electron transport); ferrocytochrome c oxidase; NADH cytochrome c oxidase. Enzyme Commission Number: EC 1.9.3.1. CAS No. 9001-16-5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1687; cytochrome-c oxidase; EC 1.9.3.1; 9001-16-5; cytochrome oxidase; cytochrome a3; cytochrome aa3; Warburg's respiratory enzyme; indophenol oxidase; indophenolase; complex IV (mitochondrial electron transport); ferrocytochrome c oxidase; NADH cytochrome c oxidase. Cat No: EXWM-1687. | |
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