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| Product | Description | |
|---|---|---|
| 1,3,7-trimethyluric acid 5-monooxygenase | The enzyme, characterized from the bacterium Pseudomonas sp. CBB1, is part of the bacterial C-8 oxidation-based caffeine degradation pathway. The product decomposes spontaneously to a racemic mixture of 3,6,8-trimethylallantoin. The enzyme shows no acitivity with urate. cf. EC 1.14.13.113, FAD-dependent urate hydroxylase. Group: Enzymes. Synonyms: tmuM (gene name). Enzyme Commission Number: EC 1.14.13.212. 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-0814; 1,3,7-trimethyluric acid 5-monooxygenase; EC 1.14.13.212; tmuM (gene name). Cat No: EXWM-0814. |  |
| 1,9-Nonanediol | 1,9-Nonanediol is found to be a general anesthetic that can inhibit the firefly luciferase enzyme from Photinus pyralis by competing with its normal substrate firefly luciferin. 1,9-Nonanediol can also inhibit the bacterial luciferase enzyme from Vibrio Harveyi by competing with the substrate n-decanal. Group: Biochemicals. Grades: Highly Purified. CAS No. 3937-56-2. Pack Sizes: 10g, 50g. Molecular Formula: C9H20O2, Molecular Weight: 160.25. US Biological Life Sciences. |  Worldwide |
| 1-[N-[N-(2-Aminobenzoyl)glycyl]-4-nitro-L-phenylalanyl]-L-proline | It is a substrate for the fluorescent assay of angiotensin I-converting enzyme and of the bacterial dipeptidyl carboxypeptidase from Escherichia coli. Synonyms: 2-Aminobenzoylglycyl-4-nitrophenylalanyl-proline; Abz-Gly-p-nitro-Phe-Pro-OH; L-Proline,N-(2-aminobenzoyl)glycyl-4-nitro-L-phenylalanyl-; o-Aminobenzoylglycyl-p-nitro-L-phenylalanyl-L-proline. CAS No. 67482-93-3. Molecular formula: C23H25N5O7. Mole weight: 483.47. |  |
| 2,4-dinitrotoluene dioxygenase | This enzyme, characterized from the bacterium Burkholderia sp. strain DNT, is a member of the naphthalene family of bacterial Rieske non-heme iron dioxygenases. It comprises a multicomponent system, containing a Rieske [2Fe-2S] ferredoxin, an NADH-dependent flavoprotein reductase (EC 1.18.1.3, ferredoxin-NAD+ reductase), and an α3β3 oxygenase. The enzyme forms a cis-dihydroxylated product that spontaneously rearranges to form a catechol with accompanying release of nitrite. It does not act on nitrobenzene. cf. EC 1.14.12.23, nitroarene dioxygenase. Group: Enzymes. Synonyms: dntA (gene name). Enzyme Commission Number: EC 1.14.12.24. 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-0691; 2,4-dinitrotoluene dioxygenase; EC 1.14.12.24; dntA (gene name). Cat No: EXWM-0691. | |
| 2-Aminoethyl 5-acetamido-3,5-dideoxy-D-glycero-a-D-galacto-2-nonulopyranosidonic acid | 2-Aminoethyl 5-acetamido-3,5-dideoxy-D-glycero-a-D-galacto-2-nonulopyranosidonic acid, commonly known as AEDDGA, is a significant biomedical compound utilized for treating specific bacterial infections. This remarkable product functions as an effective inhibitor of bacterial neuraminidase enzymes, thereby impeding the release of virus particles from infected cells. The structural resemblance of AEDDGA to sialic acid grants it the ability to competitively bind to the active site of neuraminidase, effectively inhibiting its catalytic activity. Synonyms: (2R,4S,5R,6R)-5-Acetamido-2-(2-aminoethoxy)-4-hydroxy-6-((1R,2R)-1,2,3-trihydroxypropyl)tetrahydro-2H-pyran-2-carboxylic acid. CAS No. 38971-42-5. Molecular formula: C13H24N2O9. Mole weight: 352.34. | |
| 2-aminomuconate deaminase | 2-Aminomuconate is an intermediate in the bacterial biodegradation of nitrobenzene. The enzyme has been isolated from several species, including Pseudomonas pseudocaligenes JS45, Pseudomonas fluorescens KU-7, Pseudomonas sp. AP3 and Burkholderia cenocepacia J2315. The reaction is spontaneous in acid conditions. Group: Enzymes. Synonyms: amnD (gene name); nbaF (gene name). Enzyme Commission Number: EC 3.5.99.5. CAS No. 201098-29-5. 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-4588; 2-aminomuconate deaminase; EC 3.5.99.5; 201098-29-5; amnD (gene name); nbaF (gene name). Cat No: EXWM-4588. | |
| 2-Methoxycarbonylphenyl 2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-b-D-glucopyranoside | 2-Methoxycarbonylphenyl 2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-b-D-glucopyranoside is a compound derived from glucose. It can be utilized as a chemical probe in drug discovery processes for investigating the interactions with certain enzymes or receptors. Additionally, it may serve as a precursor in the synthesis of potential carbohydrate-based drugs, specifically targeting diseases such as cancer or bacterial infections. CAS No. 6835-61-6. Molecular formula: C16H21NO8. Mole weight: 355.34. | |
| 3-Acetylpyridine-Adenine Dinucleotide, Oxidized (APAD) | 3-Acetylpyridine adenine dinucleotide is an NAD analog with higher oxidation potential than NAD. It can substitute for NAD as a hydrogen-accepting cofactor in many dehydrogenase reactions. For example lactate dehydrogenase from Toxoplasma, Clonorchis, and Plasmodium, bacterial lipoamide dehydrogenase, as well as mammalian dehydrogenases. This compound can also act as a proton acceptor in various transhydrogenation reactions with NADH or NADPH. Group: Coenzymes. Synonyms: aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NA. Enzyme Commission Number: EC 1.1.1.1. CAS No. 1986-8-8. Purity: Determined by increase in absorbance at 363 nm on enzymatic reduction with ADH* at pH 10.0 > 92% *ADH = Alcohol dehydrogenase (Horse liver) (EC 1.1.1.1.). APAD. Mole weight: 662.44. Storage: Keep tightly stoppered in the dark below 5°C. Moisture will reduce the purity. For prolonged storage, keep below-20°C. aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1; APAD. Cat No: NATE-0077. | |
| 3-hydroxybenzoate synthase | The enzyme, found in several bacterial species is involved in biosynthesis of secondary products. The enzyme from the bacterium Xanthomonas campestris pv. campestris also has the activity of EC 4.1.3.40, chorismate lyase. Group: Enzymes. Synonyms: chorismatase/3-hydroxybenzoate synthase; hyg5 (gene name); bra8 (gene name); XanB2. Enzyme Commission Number: EC 4.1.3.45. 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-4922; 3-hydroxybenzoate synthase; EC 4.1.3.45; chorismatase/3-hydroxybenzoate synthase; hyg5 (gene name); bra8 (gene name); XanB2. Cat No: EXWM-4922. | |
| 3-oxo-5α-steroid 4-dehydrogenase (acceptor) | A flavoprotein. This bacterial enzyme, characterized from Comamonas testosteroni, is involved in androsterone degradation. cf. EC 1.3.1.22, 3-oxo-5α-steroid 4-dehydrogenase (NADP+). Group: Enzymes. Synonyms: steroid 5α-reductase; 3-oxosteroid Δ4-dehydrogenase; 3-oxo-5α-steroid Δ4-dehydrogenase; steroid Δ4-5α-reductase; Δ4-3-keto steroid 5α-reductase; Δ4-3-oxo steroid reductase; Δ4-3-ketosteroid5α-oxidoreductase; &D. Enzyme Commission Number: EC 1.3.99.5. CAS No. 9036-43-5. 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-1439; 3-oxo-5α-steroid 4-dehydrogenase (acceptor); EC 1.3.99.5; 9036-43-5; steroid 5α-reductase; 3-oxosteroid Δ4-dehydrogenase; 3-oxo-5α-steroid Δ4-dehydrogenase; steroid Δ4-5α-reductase; Δ4-3-keto steroid 5α-reductase; Δ4-3-oxo steroid reductase; Δ4-3-ketosteroid5α-oxidoreductase; Δ4-3-oxosteroid-5α-reductase; 3-keto-Δ4-steroid-5α-reductase; 5α-reductase; testosterone 5α-reductase; 4-ene-3-ketosteroid-5α-oxidoreductase; Δ4-5α-dehydrogenase; 3-oxo-5α-steroid:(acceptor) Δ4-oxidoreductase; tesI (gene name). Cat No: EXWM-1439. | |
| 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-hydroxybenzaldehyde dehydrogenase (NAD+) | The bacterial enzyme (characterized from an unidentified denitrifying bacterium) is involved in an anaerobic toluene degradation pathway. The plant enzyme is involved in formation of 4-hydroxybenzoate, a cell wall-bound phenolic acid that plays a major role in plant defense against pathogens. cf. EC 1.2.1.96, 4-hydroxybenzaldehyde dehydrogenase (NADP+). Group: Enzymes. Synonyms: p-hydroxybenzaldehyde dehydrogenase (ambiguous); 4-hydroxybenzaldehyde dehydrogenase (ambiguous). Enzyme Commission Number: EC 1.2.1.64. CAS No. 61229-72-9. 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-1166; 4-hydroxybenzaldehyde dehydrogenase (NAD+); EC 1.2.1.64; 61229-72-9; p-hydroxybenzaldehyde dehydrogenase (ambiguous); 4-hydroxybenzaldehyde dehydrogenase (ambiguous). Cat No: EXWM-1166. | |
| (4-Nitrophenyl)methyl-b-D-glucopyranoside | (4-Nitrophenyl)methyl-b-D-glucopyranoside is a biochemical substrate used primarily for detecting, quantifying, and studying beta-glucosidases. These enzymes participate in important biological processes, from bacterial cell wall formation to anti-inflammatory drug activation. It can be used in the research of various diseases including Gaucher's disease. CAS No. 700368-52-1. Molecular formula: C13H17NO8. Mole weight: 315.28. | |
| 50S ribosomal protein L16 3-hydroxylase | The enzyme, characterized from the bacterium Escherichia coli, hydroxylates an arginine residue on the 50S ribosomal protein L16, and is involved in regulation of bacterial ribosome assembly. Group: Enzymes. Synonyms: ycfD (gene name). Enzyme Commission Number: EC 1.14.11.47. 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-0666; 50S ribosomal protein L16 3-hydroxylase; EC 1.14.11.47; ycfD (gene name). Cat No: EXWM-0666. | |
| Acacia | Acacia is available as white or yellowish-white thin flakes, spheroidal tears, granules, powder, or spray-dried powder. It is odorless and has a bland taste. Synonyms: Acaciae gummi; acacia gum; arabic gum; E414; gum acacia; gummi africanum; gum arabic; gummi arabicum; gummi mimosae; talhagum. CAS No. 9000-5-1. Product ID: PE-0462. Category: Emulsifying Agents; Stabilizing Agents; Suspending Agents; Tablet Binder; Viscosity-increasing Agents. Product Keywords: Binder Excipients; Emulsifier Excipients; Stabilizers; Suspending Agents; PE-0462; Acacia; Emulsifying Agents; Stabilizing Agents; Suspending Agents; Tablet Binder; Viscosity-increasing Agents; ; 9000-5-1. UNII: 5C5403N26O. Grade: Pharmceutical Excipients. Administration route: Oral; buccal or sublingual. Dosage Form: Oral preparations and buccal or sublingual tablets. Stability and Storage Conditions: Aqueous solutions are subject to bacterial or enzymatic degradation but may be preserved by initially boiling the solution for a short time to inactivate any enzymes present; microwave irradiation can also be used.Aqueous solutions may also be preserved by the addition of an antimicrobial preservative such as 0.1% w/v benzoic acid, 0.1% w/v sodium benzoate, or a mixture of 0.17% w/v methylparaben and 0.03% propylparaben. Powdered acacia should be stored in an airtight container in a cool, dry place. Source and Preparation: Acacia is the dried gummy exudate obtained from |  |
| 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. | |
| Acetate Kinase (Crude Enzyme) | In molecular biology, acetate kinase, which is predominantly found in micro-organisms, facilitates the production of acetyl-CoA byphosphorylating acetate in the presence of ATP and a divalent cation. The enzyme is important in the process of glycolysis, enzyme levels being increased in the presence of excess glucose. The growth of a bacterial mutant lacking acetate kinase has been shown to be inhibited by glucose, suggesting that the enzyme is involved in excretion of excess carbohydrate. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Synthesis; industry. Group: Enzymes. Synonyms: acetokinase; AckA; AK; acetic kinase; acetate kinase (phosphorylating). Enzyme Commission Number: EC 2.7.2.1. CAS No. 9027-42-3. Acetate kinase. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. acetokinase; AckA; AK; acetic kinase; acetate kinase (phosphorylating). Pack: 100ml. Cat No: NATE-1826. | |
| Acetolactate Synthase (Crude Enzyme) | The Acetolactate Synthase (ALS) enzyme (also known as acetohydroxy acid synthase, or AHAS) is a protein found in plants and micro-organisms. ALS catalyzes the first step in the synthesis of the branched-chain amino acids (valine, leucine, and isoleucine). It is a human protein of yet unknown function, sharing some sequence similarity with bacterial ALS, and is encoded by the ILVBL gene. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Agriculture; biotechnology; drug development; synthesis; molecular biology. Group: Enzymes. Synonyms: α-acetohydroxy acid synthetase; α-acetohydroxyacid synthase; α-acetolactate synthase; α-acetolactate synthetase; acetohydroxy acid synthetase; acetohydroxyacid synthase; acetolactate pyruvate-lyase (carboxylating); acetolactic synthetase. Enzyme Commission Number: EC 2.2.1.6. CAS No. 9027-45-6. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. α-acetohydroxy acid synthetase; α-acetohydroxyacid synthase; α-acetolactate synthase; α-acetolactate synthetase; acetohydroxy acid synthetase; acetohydroxyacid synthase; acetolactate pyruvate-lyase (carboxylating); acetolactic synthetase. Pack: 100ml. Cat No: NATE-1810. | |
| 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. | |
| alkene monooxygenase | This bacterial binuclear non-heme iron enzyme is a multicomponent enzyme complex comprising an oxygenase, a reductase, and a Rieske-type ferredoxin. The enzyme from the bacterium Xanthobacter sp. strain Py2 contains an additional small protein of unknown function that is essential for activity. In general, the enzyme oxygenates C2 to C6 aliphatic alkenes, although enzymes from different organisms show different substrate range. With propene as substrate, the stereospecifity of the epoxypropane formed is 95% (R) and 5% (S). Group: Enzymes. Synonyms: alkene epoxygenase; etnABCD (gene names); amoABCDE (gene names). Enzyme Commission Number: EC 1.14.13.69. CAS No. 63439-50-9. 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-0875; alkene monooxygenase; EC 1.14.13.69; 63439-50-9; alkene epoxygenase; etnABCD (gene names); amoABCDE (gene names). Cat No: EXWM-0875. | |
| aminodeoxyfutalosine nucleosidase | The enzyme, found in several bacterial species, catalyses a step in a modified futalosine pathway for menaquinone biosynthesis. While the enzyme from some organisms also has the activity of EC 3.2.2.9, adenosylhomocysteine nucleosidase, the enzyme from Chlamydia trachomatis is specific for 6-amino-6-deoxyfutalosine. Group: Enzymes. Synonyms: AFL nucleosidase; aminofutalosine nucleosidase; methylthioadenosine nucleosidase; MqnB. Enzyme Commission Number: EC 3.2.2.30. 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-3985; aminodeoxyfutalosine nucleosidase; EC 3.2.2.30; AFL nucleosidase; aminofutalosine nucleosidase; methylthioadenosine nucleosidase; MqnB. Cat No: EXWM-3985. | |
| 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. | |
| aspartate-semialdehyde dehydrogenase | In enzymology, an aspartate-semialdehyde dehydrogenase (EC 1.2.1.11) is an enzyme that is very important in the biosynthesis of amino acids in prokaryotes, fungi, and some higher plants. It forms an early branch point in the metabolic pathway forming lysine, methionine, leucine and isoleucine from aspartate. This pathway also produces diaminopimelate which plays an essential role in bacterial cell wall formation. There is particular interest in ASADH as disabling this enzyme proves fatal to the organism giving rise to the possibility of a new class of antibiotics, fungicides, and herbicides aimed at inhibiting it. Group: Enzymes. Synonyms: aspartate semialdehyde dehydrogenase; aspartic semialdehyde dehydrogenase; L-aspartate-β-semialdehyde:NADP+ oxidoreductase (phosphorylating); aspartic β-semialdehyde dehydrogenase; ASA dehydrogenase. Enzyme Commission Number: EC 1.2.1.11. CAS No. 9000-98-0. 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-1117; aspartate-semialdehyde dehydrogenase; EC 1.2.1.11; 9000-98-0; aspartate semialdehyde dehydrogenase; aspartic semialdehyde dehydrogenase; L-aspartate-β-semialdehyde:NADP+ oxidoreductase (phosphorylating); aspartic β-semialdehyde dehydrogenase; ASA dehydrogenase. Cat No: EXWM-1117. | |
| bacterial leucyl aminopeptidase | A zinc enzyme. Forms of the enzyme have been isolated from Aeromonas proteolytica, Escherichia coli and Streptococcus thermophilus. Examples are known from peptidase families M17 and M28 (of leucyl aminopeptidase and aminopeptidase Y, respectively). Group: Enzymes. Synonyms: Aeromonas proteolytica aminopeptidase. Enzyme Commission Number: EC 3.4.11.10. CAS No. 37288-67-8. Aminopeptidase. 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-4008; bacterial leucyl aminopeptidase; EC 3.4.11.10; 37288-67-8; Aeromonas proteolytica aminopeptidase. Cat No: EXWM-4008. | |
| bacterial non-heme ferritin | Ferritins are intracellular iron-storage and detoxification proteins found in all kingdoms of life. They are formed from two subunits that co-assemble in various ratios to form a spherical protein shell. Thousands of mineralized iron atoms are stored within the core of the structure. The product of dioxygen reduction by the bacterial non-heme ferritin is hydrogen peroxide, which is consumed in a subsequent reaction. Group: Enzymes. Synonyms: FtnA; HuHF. Enzyme Commission Number: EC 1.16.3.2. 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-1076; bacterial non-heme ferritin; EC 1.16.3.2; FtnA; HuHF. Cat No: EXWM-1076. | |
| benzyl 2-acetamido-4,6-di-O-benzyl-2-deoxy-α-D-glucopyranoside | Benzyl 2-acetamido-4,6-di-O-benzyl-2-deoxy-α-D-glucopyranoside - a remarkable small molecule glycoscience innovation - is widely used in the biomedical and pharmaceutical research fields owing to its potential in tackling various ailments, ranging from cancer to neurological disorders to bacterial infections. Its success can be attributed to its strong enzyme-inhibiting properties that modulate immune response pathways. Alongside this, it is also a pivotal tool for drug discovery and development as well as glycosylation research. Grades: 98%. CAS No. 73646-11-4. Molecular formula: C29H33NO6. Mole weight: 491.58. | |
| β-1,2-mannosidase | The enzyme, characterized from multiple bacterial species, catalyses the hydrolysis of terminal, non-reducing D-mannose residues from β-1,2-mannotriose and β-1,2-mannobiose. The mechanism involves anomeric inversion, resulting in the release of α-D-mannopyranose. Activity with β-1,2-mannotriose or higher oligosaccharides is higher than that with β-1,2-mannobiose. Group: Enzymes. Enzyme Commission Number: EC 3.2.1.197. 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-3881; β-1,2-mannosidase; EC 3.2.1.197. Cat No: EXWM-3881. | |
| 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. | |
| β-lytic metalloendopeptidase | From Achromobacter lyticus and Lysobacter enzymogenes. Digests bacterial cell walls. Type example of peptidase family M23. Group: Enzymes. Synonyms: Myxobacter β-lytic proteinase; achromopeptidase component; β-lytic metalloproteinase; β-lytic protease; Myxobacterium sorangium β-lytic proteinase; Myxobacter495 β-lytic proteinase. Enzyme Commission Number: EC 3.4.24.32. CAS No. 37288-92-9. 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-4314; β-lytic metalloendopeptidase; EC 3.4.24.32; 37288-92-9; Myxobacter β-lytic proteinase; achromopeptidase component; β-lytic metalloproteinase; β-lytic protease; Myxobacterium sorangium β-lytic proteinase; Myxobacter495 β-lytic proteinase. Cat No: EXWM-4314. | |
| β-methylindole-3-pyruvate reductase | The enzyme, characterized from the bacterium Streptomyces griseus, participates in the biosynthesis of indolmycin, an antibacterial drug that inhibits the bacterial tryptophan-tRNA ligase (EC 6.1.1.2). Group: Enzymes. Synonyms: ind2 (gene name). Enzyme Commission Number: EC 1.1.1.397. 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-0317; β-methylindole-3-pyruvate reductase; EC 1.1.1.397; ind2 (gene name). Cat No: EXWM-0317. | |
| β-Nicotinamide Adenine Dinucleotide Sodium Salt Hydrate | β-Nicotinamide Adenine Dinucleotide is a coeznyme consisting of an adenine base and a nicotinamide base connected by a pair of bridging phosphate group. β-Nicotinamide Adenine Dinucleotide acts as a coenzyme in redox reactions, as a donor of ADP-ribose moieties in ADP-ribosylation reactions and also as a precursor of the second messenger molecule cyclic ADP-ribose. β-Nicotinamide Adenine Dinucleotide also acts as a substrate for bacterial DNA ligases and a group of enzymes called sirtuins that use NAD+ to remove acetyl groups from proteins. Synonyms: Adenosine 5'-(Trihydrogen Diphosphate), P'?5'-Ester with 3-(Aminocarbonyl)-1-β-D-ribofuranosylpyridinium Hydroxide Sodium Salt Hydrate; Adenine-nicotinamide Dinucleotide Sodium Salt Hydrate; CO-I Sodium Salt Hydrate; Codehydrase I Sodium Salt Hydrate; Codehydrogenase I Sodium Salt Hydrate; Coenzyme I Sodium Salt Hydrate; Cozymase I Sodium Salt Hydrate; DPN Sodium Salt Hydrate; Diphosphopyridine Nucleotide Sodium Salt Hydrate; Enzopride Sodium Salt Hydrate; NAD Sodium Salt Hydrate; NAD+ Sodium Salt Hydrate; NSC 20272 Sodium Salt Hydrate; Nadide Sodium Salt Hydrate; Nicotinamide-adenine Dinucleotide Sodium Salt Hydrate; Oxidized diphosphopyridine Nucleotide Sodium Salt Hydrate; β-Diphosphopyridine Nucleotide Sodium Salt Hydrate; β-NAD Sodium Salt Hydrate; β-NAD+ Sodium Salt Hydrate. Grades: 95%. Molecular formula: C21H26N7NaO14P2 X(H2O). Mole weight: 685.41. | |
| carboxynorspermidine decarboxylase | A pyridoxal 5'-phosphate enzyme. Part of a bacterial polyamine biosynthesis pathway. The enzyme is essential for biofilm formation in the bacterium Vibrio cholerae. The enzyme from Campylobacter jejuni only produces spermidine in vivo even though it shows activity with carboxynorspermidine in vitro. Group: Enzymes. Synonyms: carboxyspermidine decarboxylase; CANSDC; VC1623 (gene name). Enzyme Commission Number: EC 4.1.1.96. 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-4846; carboxynorspermidine decarboxylase; EC 4.1.1.96; carboxyspermidine decarboxylase; CANSDC; VC1623 (gene name). Cat No: EXWM-4846. | |
| carboxynorspermidine synthase | The reaction takes place in the opposite direction. Part of a bacterial polyamine biosynthesis pathway. L-aspartate 4-semialdehyde and propane-1,3-diamine/putrescine form a Schiff base that is reduced to form carboxynorspermidine / carboxyspermidine, respectively. The enzyme from the bacterium Vibrio cholerae is essential for biofilm formation. The enzyme from Campylobacter jejuni only produces carboxyspermidine in vivo even though it also can produce carboxynorspermidine in vitro. Group: Enzymes. Synonyms: carboxynorspermidine dehydrogenase; carboxyspermidine dehydrogenase; CASDH; CANSDH; VC1624 (gene name). Enzyme Commission Number: EC 1.5.1.43. 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-1524; carboxynorspermidine synthase; EC 1.5.1.43; carboxynorspermidine dehydrogenase; carboxyspermidine dehydrogenase; CASDH; CANSDH; VC1624 (gene name). Cat No: EXWM-1524. | |
| Cerulenin (2,3-Epoxy-4-oxo-7,10-dodecadienamide) | Antibiotic. Fatty acid synthase (FAS) inhibitor, reported to bind in equimolar ratio to B-keto-acyl- ACP synthase, thus inhibiting protein acylation. Produces metabolic effects similar to effects of leptin, but through mechanisms that are independent of, or down-stream from, both leptin and melanocortin receptors. Apoptosis inducer. Inhibitor of bacterial fatty acid synthesis (inhibits FabH, FabB and FabF condensation enzymes). Group: Biochemicals. Grades: Highly Purified. CAS No. 17397-89-6. Pack Sizes: 5mg. Molecular Formula:C12H17NO3 MOLECULAR WEIGHT: 223.3. US Biological Life Sciences. | Worldwide |
| Cerulenin (Helicocerin, NSC 116069, 2,3-Epoxy-4-oxo-7,10-dodecadienamide) | Cerulenin is an epoxy fatty acid amide isolated from the fungus Cephalosporium caerulens and identified as an antifungal in the 1960s. Over the past 40 years cerulenin has found broad application in lipid biochemistry as an inhibitor fatty acid and sterol biosynthesis. Cerulenin binds to B-keto-acyl-ACP synthase blocking the interaction of malonyl CoA. Cerulenin is also an inhibitor of bacterial fatty acid synthesis acting on the FabH, FabB and FabF condensation enzymes. Cerulenin stimulates fatty acid oxidation and inhibits HMG-CoA synthetase activity. Group: Biochemicals. Grades: Highly Purified. CAS No. 17397-89-6. Pack Sizes: 5mg. US Biological Life Sciences. | Worldwide |
| 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. | |
| cholest-4-en-3-one 26-monooxygenase [(25R)-3-oxocholest-4-en-26-oate forming] | This enzyme, found in several bacterial pathogens, is involved in degradation of the host cholesterol. It catalyses the hydroxylation of the C-26 carbon, followed by oxidation of the alcohol to the carboxylic acid via the aldehyde intermediate, initiating the degradation of the alkyl side-chain of cholesterol. The products are exclusively in the (25R) conformation. The enzyme also accepts cholesterol as a substrate. cf. EC 1.14.13.141, cholest-4-en-3-one 26-monooxygenase. The enzyme can receive electrons from ferredoxin reductase in vitro, its natural electron donor is not known yet. Group: Enzymes. Synonyms: CYP142. Enzyme Commission Number: EC 1.14.13.221. 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-0824; cholest-4-en-3-one 26-monooxygenase [(25R)-3-oxocholest-4-en-26-oate forming]; EC 1.14.13.221; CYP142. Cat No: EXWM-0824. | |
| cholesterol oxidase | Contains FAD. Cholesterol oxidases are secreted bacterial bifunctional enzymes that catalyse the first two steps in the degradation of cholesterol. The enzyme catalyses the oxidation of the 3β-hydroxyl group to a keto group, and the isomerization of the double bond in the oxidized steroid ring system from the Δ5 position to Δ6 position (cf. EC 5.3.3.1, steroid Δ-isomerase). Group: Enzymes. Synonyms: cholesterol- O2 oxidoreductase; 3β-hydroxy steroid oxidoreductase; 3β-hydroxysteroid:oxygen oxidoreductase. Enzyme Commission Number: EC 1.1.3.6. CAS No. 9028-76-6. CHOD. 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-0424; cholesterol oxidase; EC 1.1.3.6; 9028-76-6; cholesterol- O2 oxidoreductase; 3β-hydroxy steroid oxidoreductase; 3β-hydroxysteroid:oxygen oxidoreductase. Cat No: EXWM-0424. | |
| 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 |
| D-Amino acid dehydrogenase, Recombinant | D-amino-acid dehydrogenase (EC 1.4.99.1) is a bacterial enzyme that catalyses the oxidation of D-amino acids into their corresponding oxoacids. It contains both flavin and nonheme iron as cofactors. The enzyme has a very broad specificity and can act on most D-amino acids. D-amino acid + H2O + acceptor <=> a 2-oxo acid + NH3 + reduced acceptor. This reaction is distinct from the oxidation reaction catalysed by D-amino acid oxidase that uses oxygen as a second substrate, as the dehydrogenase can use many different compounds as electron acceptors, with the physiological substrate being coenzyme Q. D-amino-acid dehydrogenase is used in enzyme assays to measure substrate specificity of D-amino acids, such as DauA. Applications: D-amino-acid dehydrogenase is a bacterial enzyme that catalyses the oxidation of d-amino acids into their corresponding oxoacids. it contains flavin and nonheme iron as cofactors and has a broad specificity thereby acting on most d-amino acids. Group: Enzymes. Synonyms: D-Amino acid dehydrogenase; EC 1.4.99.1; 37205-44-0. Enzyme Commission Number: EC 1.4.99.1. CAS No. 37205-44-0. D-Amino acid dehydrogenase. Activity: >26 U/g. Storage: Store at 2-8°C. Source: E. coli. D-Amino acid dehydrogenase; EC 1.4.99.1; 37205-44-0. Cat No: NATE-0825. | |
| decaprenylphospho-β-D-erythro-pentofuranosid-2-ulose 2-reductase | The reaction is catalysed in the reverse direction. The enzyme, isolated from the bacterium Mycobacterium smegmatis, is involved, along with EC 1.1.98.3, decaprenylphospho-β-D-ribofuranose 2-oxidase, in the epimerization of trans,octacis-decaprenylphospho-β-D-ribofuranose to trans,octacis-decaprenylphospho-β-D-arabinoofuranose, the arabinosyl donor for the biosynthesis of mycobacterial cell wall arabinan polymers. Group: Enzymes. Synonyms: decaprenylphospho-β-D-ribofuranose 2'-epimerase; Rv3791; DprE2. Enzyme Commission Number: EC 1.1.1.333. 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-0247; decaprenylphospho-β-D-erythro-pentofuranosid-2-ulose 2-reductase; EC 1.1.1.333; decaprenylphospho-β-D-ribofuranose 2'-epimerase; Rv3791; DprE2. Cat No: EXWM-0247. | |
| decaprenylphospho-β-D-ribofuranose 2-dehydrogenase | The enzyme, isolated from the bacterium Mycobacterium smegmatis, is involved, along with EC 1.1.1.333, decaprenylphospho-D-erythro-pentofuranosid-2-ulose 2-reductase, in the epimerization of trans,octacis-decaprenylphospho-β-D-ribofuranose to trans,octacis-decaprenylphospho-β-D-arabinofuranose, the arabinosyl donor for the biosynthesis of mycobacterial cell wall arabinan polymers. Group: Enzymes. Synonyms: decaprenylphosphoryl-β-D-ribofuranose 2'-epimerase; Rv3790; DprE1; decaprenylphospho-β-D-ribofuranose 2-oxidase. Enzyme Commission Number: EC 1.1.98.3. 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-0440; decaprenylphospho-β-D-ribofuranose 2-dehydrogenase; EC 1.1.98.3; decaprenylphosphoryl-β-D-ribofuranose 2'-epimerase; Rv3790; DprE1; decaprenylphospho-β-D-ribofuranose 2-oxidase. Cat No: EXWM-0440. | |
| diglucosyl diacylglycerol synthase (1,6-linking) | The enzyme is found in several bacterial species. The enzyme from Bacillus subtilis is specific for glucose. The enzyme from Mycoplasma genitalium can incoporate galactose with similar efficiency, but forms mainly 1,2-diacyl-diglucopyranosyl-sn-glycerol in vivo. The enzyme from Staphylococcus aureus can also form glucosyl-glycero-3-phospho-(1'-sn-glycerol). Group: Enzymes. Synonyms: monoglucosyl diacylglycerol (1?6) glucosyltransferase; MGlcDAG (1?6) glucosyltransferase; DGlcDAG synthase (ambiguous); UGT106B1; ypfP (gene name). Enzyme Commission Number: EC 2.4.1.315. 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-2551; diglucosyl diacylglycerol synthase (1,6-linking); EC 2.4.1.315; monoglucosyl diacylglycerol (1?6) glucosyltransferase; MGlcDAG (1?6) glucosyltransferase; DGlcDAG synthase (ambiguous); UGT106B1; ypfP (gene name). Cat No: EXWM-2551. | |
| Dihydrofolate Reductase from human, Recombinant | Dihydrofolate reductase, or DHFR, is an enzyme that reduces dihydrofolic acid to tetrahydrofolic acid, using NADPH as electron donor, which can be converted to the kinds of tetrahydrofolate cofactors used in 1-carbon transfer chemistry. In humans, the DHFR enzyme is encoded by the DHFR gene. It is found in the q11?q22 region of chromosome 5. Bacterial species possesses distinct DHFR enzymes (based on their pattern of binding diaminoheterocyclic molecules), but mammalian DHFRs are highly similar. Human dhfr is an 186 amino acid protein with an apparent molecular weight of 25 kda. it is 30% homologous to the e. coli protein and up to 70% homologous to vertebrate protein... from mycobacterium smegmatis. human dihydrofolate reductase has been used in a study to investigate the stable expression of green fluorescent protein and the targeted disruption of thioredoxin peroxidase-1 gene in babesia bovis. human dihydrofolate reductase has also been used in a study to investigate the structural analysis of human dihydrofolate reductase as a binary complex. Group: Enzymes. Synonyms: DHFR; dihydrofolate reductase; DYR; DHFRP1; Tetrahydrofolate NADP+ oxidoreductase; EC 1.5.1.3; tetrahydrofolate dehydrogenase; pteridine reductase:dihydrofolate reductase; dihydrofolate reductase:thymidylate synthase; thymidylate synthetase-dihydrofolate reductase; f | |
| dye decolorizing peroxidase | Heme proteins with proximal histidine secreted by basidiomycetous fungi and eubacteria. They are similar to EC 1.11.1.16 versatile peroxidase (oxidation of Reactive Black 5, phenols, veratryl alcohol), but differ from the latter in their ability to efficiently oxidize a number of recalcitrant anthraquinone dyes, and inability to oxidize Mn(II). The model substrate Reactive Blue 5 is converted with high efficiency via a so far unique mechanism that combines oxidative and hydrolytic steps and leads to the formation of phthalic acid. Bacterial TfuDyP catalyses sulfoxidation. Group: Enzymes. Synonyms: DyP; DyP-type peroxidase. Enzyme Commission Number: EC 1.11.1.19. 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-0500; dye decolorizing peroxidase; EC 1.11.1.19; DyP; DyP-type peroxidase. Cat No: EXWM-0500. | |
| formate-phosphoribosyl aminoimidazolecarboxamide ligase | This archaeal enzyme, characterized from the methanogen Methanocaldococcus jannaschii, catalyses a step in the synthesis of purine nucleotides. It differs from the orthologous bacterial/eukaryotic enzymes, which utilize 10-formyltetrahydrofolate rather than formate and ATP. cf. EC 2.1.2.3, phosphoribosyl aminoimidazolecarboxamide formyltransferase. Group: Enzymes. Synonyms: 5-formaminoimidazole-4-carboxamide ribonucleotide synthetase; 5-formaminoimidazole-4-carboxamide-1-β-D-ribofuranosyl 5'-monophosphate synthetase; purP (gene name). Enzyme Commission Number: EC 6.3.4.23. CAS No. 9032-3-5. 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-5793; formate-phosphoribosyl aminoimidazolecarboxamide ligase; EC 6.3.4.23; 9032-03-5; 5-formaminoimidazole-4-carboxamide ribonucleotide synthetase; 5-formaminoimidazole-4-carboxamide-1-β-D-ribofuranosyl 5'-monophosphate synthetase; purP (gene name). Cat No: EXWM-5793. | |
| GalNAc5-diNAcBac-PP-undecaprenol β-1,3-glucosyltransferase | Isolated from the bacterium Campylobacter jejuni. Part of a bacterial N-linked glycosylation pathway. Group: Enzymes. Synonyms: PglI. Enzyme Commission Number: EC 2.4.1.293. 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-2527; GalNAc5-diNAcBac-PP-undecaprenol β-1,3-glucosyltransferase; EC 2.4.1.293; PglI. Cat No: EXWM-2527. | |
| GalNAc-α-(1?4)-GalNAc-α-(1?3)-diNAcBac-PP-undecaprenol α-1,4-N-acetyl-D-galactosaminyltransferase | Isolated from Campylobacter jejuni. Part of a bacterial N-linked glycosylation pathway. Group: Enzymes. Synonyms: PglH. Enzyme Commission Number: EC 2.4.1.292. 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-2526; GalNAc-α-(1?4)-GalNAc-α-(1?3)-diNAcBac-PP-undecaprenol α-1,4-N-acetyl-D-galactosaminyltransferase; EC 2.4.1.292; PglH. Cat No: EXWM-2526. | |
| γ-D-glutamyl-meso-diaminopimelate peptidase | A 45-kDa metallopeptidase from Bacillus sphaericus, the substrates being components of the bacterial spore wall. A member of peptidase family M14 (carboxypeptidase A family). Endopeptidase II has similar activity, but differs in cellular location, molecular mass and catalytic mechanism. Group: Enzymes. Synonyms: endopeptidase I; γ-D-glutamyldiaminopimelate endopeptidase; γ-D-glutamyl-L-meso-diaminopimelate peptidoglycan hydrolase; γ-glutamyl-L-meso-diaminopimelyl endopeptidase; γ-D-glutamyl-meso-diaminopimelate endopeptidase; γ-D-glutamyl-meso-diaminopimelic peptidoglycan hydrolase; γ-D-glutamyl-m. Enzyme Commission Number: EC 3.4.19.11. CAS No. 62572-28-5. 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-4083; γ-D-glutamyl-meso-diaminopimelate peptidase; EC 3.4.19.11; 62572-28-5; endopeptidase I; γ-D-glutamyldiaminopimelate endopeptidase; γ-D-glutamyl-L-meso-diaminopimelate peptidoglycan hydrolase; γ-glutamyl-L-meso-diaminopimelyl endopeptidase; γ-D-glutamyl-meso-diaminopimelate endopeptidase; γ-D-glutamyl-meso-diaminopimelic peptidoglycan hydrolase; γ-D-glutamyl-meso-diaminopimelic endopeptidase; γ-D-glutamyl-meso-D-aminopimelic endopeptidase. Cat No: EXWM-4083. | |
| γ-resorcylate decarboxylase | The enzyme, characterized from several bacterial strains, is involved in the degradation of γ-resorcylate. It contains a zinc ion and a water molecule at the active site. The reaction is reversible, but equilibrium greatly favors the decarboxylation reaction. Group: Enzymes. Synonyms: graF (gene name); tsdA (gene name). Enzyme Commission Number: EC 4.1.1.103. 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-4756; γ-resorcylate decarboxylase; EC 4.1.1.103; graF (gene name); tsdA (gene name). Cat No: EXWM-4756. | |
| [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase | This bacterial enzyme removes an adenylyl group from a modified tyrosine residue of EC 6.3.1.2, glutamine synthetase. The enzyme is bifunctional, and also performs the adenylation of this residue (cf. EC 2.7.7.42, [glutamine synthetase] adenylyltransferase). The two activities are present on separate domains. Group: Enzymes. Synonyms: adenylyl-[glutamine-synthetase]-deadenylase; [L-glutamate:ammonia ligase (ADP-forming)]-O4-(5'-adenylyl)-L-tyrosine:phosphate adenylyltransferase; [glutamate-ammonia ligase]-adenylyl-L-tyrosine phosphorylase. Enzyme Commission Number: EC 2.7.7.89. 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-3302; [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase; EC 2.7.7.89; adenylyl-[glutamine-synthetase]-deadenylase; [L-glutamate:ammonia ligase (ADP-forming)]-O4-(5'-adenylyl)-L-tyrosine:phosphate adenylyltransferase; [glutamate-ammonia ligase]-adenylyl-L-tyrosine phosphorylase. Cat No: EXWM-3302. | |
| [glutamine synthetase] adenylyltransferase | This bacterial enzyme adenylates a tyrosine residue of EC 6.3.1.2, glutamine synthetase. The enzyme is bifunctional, and also catalyses a reaction that removes the adenyl group from the modified tyrosine residue (cf. EC 2.7.7.89, [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase). The two activities are present on separate domains. Group: Enzymes. Synonyms: glutamine-synthetase adenylyltransferase; ATP:glutamine synthetase adenylyltransferase; adenosine triphosphate:glutamine synthetase adenylyltransferase; ATP:[L-glutamate:ammonia ligase (ADP-forming)] adenylyltransferase; ATP:[L-glutamate:ammonia ligase (ADP-forming)]-L-tyrosine adenylyltransferase; [glutamate-ammonia-ligase] adenylyltransferase. Enzyme Commission Number: EC 2.7.7.42. CAS No. 9077-66-1. 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-3254; [glutamine synthetase] adenylyltransferase; EC 2.7.7.42; 9077-66-1; glutamine-synthetase adenylyltransferase; ATP:glutamine synthetase adenylyltransferase; adenosine triphosphate:glutamine synthetase adenylyltransferase; ATP:[L-glutamate:ammonia ligase (ADP-forming)] adenylyltransferase; ATP:[L-glutamate:ammonia ligase (ADP-forming)]-L-tyrosine adenylyltransferase; [glutamate-ammonia-ligase] adenylyltransferase. Cat No: EXWM-3254. | |
| Hydroxynitrile Lyase from Arabidopsis thaliana, Recombinant | Hydroxynitrile lyases (Oxynitrilases) catalyze the addition of HCN to aldehydes and ketones thereby forming α-hydroxynitriles, also known as cyanohydrins. Hydroxynitrile Lyase from Arabidopsis thaliana , is used to hydrolyze mandelonitrile. Applications: Hydroxynitrile lyases (oxynitrilases) are used for various biotransformation processes and to convert a broad range of substrates. they may be used with bacterial nitrilases to generate biocatalysts. Group: Enzymes. Synonyms: hydroxynitrile lyase; oxynitrilase; Sorghum hydroxynitrile lyase; (S)-4-hydroxymandelonitrile hydroxybenzaldehyde-lyase. Enzyme Commission Number: EC 4.1.2.11. CAS No. 9075-38-1. Hydroxynitrile Lyase. Activity: >500 U/mL. Storage: at -20°C. Source: E. coli. Species: Arabidopsis thaliana. hydroxynitrile lyase; oxynitrilase; Sorghum hydroxynitrile lyase; (S)-4-hydroxymandelonitrile hydroxybenzaldehyde-lyase. Cat No: NATE-1914. | |
| indolepyruvate C-methyltransferase | The enzyme, characterized from the bacterium Streptomyces griseus, is involved in the biosynthesis of the antibacterial drug indolmycin. Group: Enzymes. Synonyms: ind1 (gene name); indolepyruvate methyltransferase; indolepyruvate 3-methyltransferase; indolepyruvic acid methyltransferase; S-adenosyl-L-methionine:indolepyruvate C-methyltransferase. Enzyme Commission Number: EC 2.1.1.47. CAS No. 54576-88-4. 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-1951; indolepyruvate C-methyltransferase; EC 2.1.1.47; 54576-88-4; ind1 (gene name); indolepyruvate methyltransferase; indolepyruvate 3-methyltransferase; indolepyruvic acid methyltransferase; S-adenosyl-L-methionine:indolepyruvate C-methyltransferase. Cat No: EXWM-1951. | |
| L-allo-isoleucine:holo-[CmaA peptidyl-carrier protein] ligase | This two-domain protein from the bacterium Pseudomonas syringae contains an adenylation domain (A domain) and a thiolation domain (T domain). It catalyses the adenylation of L-allo-isoleucine and its attachment to the T domain. The enzyme is involved in the biosynthesis of the toxin coronatine, which mimics the plant hormone jasmonic acid isoleucine. Coronatine promotes opening of the plant stomata allowing bacterial invasion, which is followed by bacterial growth in the apoplast, systemic susceptibility, and disease. Group: Enzymes. Synonyms: CmaA. Enzyme Commission Number: EC 6.2.1.46. 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-5705; L-allo-isoleucine:holo-[CmaA peptidyl-carrier protein] ligase; EC 6.2.1.46; CmaA. Cat No: EXWM-5705. | |
| limulus clotting factor C | From the hemocyte granules of the horseshoe crabs Limulus and Tachypleus. Factor C is activated by Gram-negative bacterial lipopolysaccharides and chymotrypsin. Inhibited by antithrombin III. In peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: factor C; limulus factor C. Enzyme Commission Number: EC 3.4.21.84. CAS No. 115743-27-6. 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-4176; limulus clotting factor C; EC 3.4.21.84; 115743-27-6; factor C; limulus factor C. Cat No: EXWM-4176. | |
| linalool 8-monooxygenase | A heme-thiolate protein (P-450). The secondary electron donor is a specific [2Fe-2S] ferredoxin from the same bacterial strain. Group: Enzymes. Synonyms: P-450lin; CYP111. Enzyme Commission Number: EC 1.14.13.151. 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-0751; linalool 8-monooxygenase; EC 1.14.13.151; P-450lin; CYP111. Cat No: EXWM-0751. | |
| long-chain acyl-protein thioester reductase | Together with a hydrolase component (EC 3.1.2.2 and EC 3.1.2.14) and a synthetase component (EC 6.2.1.19), this enzyme forms a multienzyme fatty acid reductase complex that produces the long-chain aldehyde substrate of the bacterial luciferase enzyme (EC 1.14.14.3). The enzyme is acylated by receiving an acyl group from EC 6.2.1.19, and catalyses the reduction of the acyl group, releasing the aldehyde product. The enzyme is also able to accept the acyl group from a long-chain acyl-CoA. Group: Enzymes. Synonyms: luxC (gene name); acyl-CoA reductase; acyl coenzyme A reductase; long-chain-aldehyde:NADP+ oxidoreductase (acyl-CoA-forming); long-chain-fatty-acyl-CoA reductase. Enzyme Commission Number: EC 1.2.1.50. CAS No. 50936-56-6. 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-1154; long-chain acyl-protein thioester reductase; EC 1.2.1.50; 50936-56-6; luxC (gene name); acyl-CoA reductase; acyl coenzyme A reductase; long-chain-aldehyde:NADP+ oxidoreductase (acyl-CoA-forming); long-chain-fatty-acyl-CoA reductase. Cat No: EXWM-1154. | |
| Luciferase | Luciferase is an analytical enzyme used as a component of lysis solution to measure luminescence signals. It has been used to investigate the sensitivity of dark mutants of various luminescent bacterial strains to reactive oxygen species. Synonyms: EC 1.14.14.3; Bacterial Luciferase; Luciferase from Photobacterium fischeri. Grades: >95%. CAS No. 9014-00-0. | |
| mannuronan 5-epimerase | The enzyme epimerizes the C-5 bond in some β-D-mannuronate residues in mannuronan, converting them to α-L-guluronate residues, and thus modifying the mannuronan into alginate. It is found in brown algae and alginate-producing bacterial species from the Pseudomonas and Azotobacter genera. Group: Enzymes. Synonyms: algG (gene name); alginate epimerase; C5-mannuronan epimerase; mannuronan C-5-epimerase. Enzyme Commission Number: EC 5.1.3.37. 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-5424; mannuronan 5-epimerase; EC 5.1.3.37; algG (gene name); alginate epimerase; C5-mannuronan epimerase; mannuronan C-5-epimerase. Cat No: EXWM-5424. | |
| mannuronan synthase | The enzyme catalyses the polymerization of β-D-mannuronate residues into a mannuronan polymer, an intermediate in the biosynthesis of alginate. It is found in brown algae and in alginate-producing bacterial species from the Pseudomonas and Azotobacter genera. Group: Enzymes. Synonyms: mannuronosyl transferase; alginate synthase (incorrect); alg8 (gene name); alg44 (gene name); GDP-D-mannuronate:alginate D-mannuronyltransferase. Enzyme Commission Number: EC 2.4.1.33. CAS No. 37257-31-1. 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-2567; mannuronan synthase; EC 2.4.1.33; 37257-31-1; mannuronosyl transferase; alginate synthase (incorrect); alg8 (gene name); alg44 (gene name); GDP-D-mannuronate:alginate D-mannuronyltransferase. Cat No: EXWM-2567. | |
| muramoylpentapeptide carboxypeptidase | A bacterial enzyme that requires a divalent cation for activity. Does not cleave the C-terminal D-alanine from the product of the above reaction, UDP-N-acetyl-muramoyl-L-alanyl-γ-D-glutamyl-6-carboxy-L-lysyl-D-alanine. Competitively inhibited by penicillins and cephalosporins. Group: Enzymes. Synonyms: D-alanine carboxypeptidase I; DD-carboxypeptidase; D-alanine carboxypeptidase; D-alanyl-D-alanine carboxypeptidase; D-alanine-D-alanine-carboxypeptidase; carboxypeptidase D-alanyl-D-alanine; carboxypeptidase I; UDP-N-acetylmuramoyl-tetrapeptidyl-D-alanine alanine-hydrolase; D-alanyl-D-alanine peptidase; DD-peptidase; penicillin binding protein 5; PBP5; PdcA; VanY. Enzyme Commission Number: EC 3.4.17.8. CAS No. 9077-67-2. 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-4080; muramoylpentapeptide carboxypeptidase; EC 3.4.17.8; 9077-67-2; D-alanine carboxypeptidase I; DD-carboxypeptidase; D-alanine carboxypeptidase; D-alanyl-D-alanine carboxypeptidase; D-alanine-D-alanine-carboxypeptidase; carboxypeptidase D-alanyl-D-alanine; carboxypeptidase I; UDP-N-acetylmuramoyl-tetrapeptidyl-D-alanine alanine-hydrolase; D-alanyl-D-alanine peptidase; DD-peptidase; penicillin binding protein 5; PBP5; PdcA; VanY. Cat No: EXWM-4080. | |
| mycolysin | From Streptomyces griseus, S. naraensis, and S. cacaoi. Specificity similar to that of thermolysin, but much more sensitive to inhibition by mercaptoacetyl-Phe-Leu. Little structural similarity to other bacterial metalloendopeptidases. Type example of peptidase family M5. Formerly included in EC 3.4.24.4. Group: Enzymes. Synonyms: pronase component; Streptomyces griseus neutral proteinase; actinase E; SGNPI. Enzyme Commission Number: EC 3.4.24.31. CAS No. 153190-34-2. 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-4313; mycolysin; EC 3.4.24.31; 153190-34-2; pronase component; Streptomyces griseus neutral proteinase; actinase E; SGNPI. Cat No: EXWM-4313. | |
| N-3-Hydroxybutyryl-L-homoserine lactone | N-3-Hydroxybutyryl-L-homoserine lactone (3-OH-C4-HSL) is an acyl-homoserine lactone, that can be isolated from Vibrionaceae. N-3-Hydroxybutyryl-L-homoserine lactone is a signaling molecule that is involved in bacterial quorum sensing (QS). N-3-Hydroxybutyryl-L-homoserine lactone senses the density of bacterial population, regulates the cellular process, such as bioluminescence, biofilm formation, and exo-enzyme production [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: 3-OH-C4-HSL; N-3-Hydroxybutanoyl-L-homoserine lactone; N-3-Hydroxybutyryl-L-HSL. CAS No. 1325550-06-8. Pack Sizes: 1 mg; 5 mg; 10 mg. Product ID: HY-158730. |  |
| N-Acetyl-2-O-methyl-a-D-neuraminic acid methyl ester | N-Acetyl-2-O-methyl-a-D-neuraminic acid methyl ester (NAMME) is a synthetically-derived sialic acid variant that has been harnessed extensively in biomedicine as an impediment to sialidase enzymes. Its pleiotropic nature of anti-viral and anti-bacterial effects along with its anti-tumor prowess has fueled scientific interest in NAMME. Its molecular dexterity to actuate viral cell entry inhibition substantiates its potential as a therapeutic agent for numerous pathologies ranging from influenza, HIV to cancer. Adding feather to its cap, NAMME exhibits a remarkable synergism with select chemotherapeutic drugs, conferring a unique therapeutic edge in cancer treatment. Hence, NAMME continues to serve as an invaluable tool for biomedical researchers fighting the war against major human diseases. Synonyms: 2-O-Methyl-a-D-N-acetylneuraminic acid methyl ester. CAS No. 6730-26-3. Molecular formula: C13H23NO9. Mole weight: 337.32. | |
| N-acetyldemethylphosphinothricin P-methyltransferase | The enzyme was originally characterized from bacteria that produce the tripeptides bialaphos and phosalacine, which inhibit plant and bacterial glutamine synthetases. It is a radical S-adenosyl-L-methionine (SAM) enzyme that contains a [4Fe-4S] center and a methylcob(III)alamin cofactor. According to the proposed mechanism, the reduced iron-sulfur center donates an electron to SAM, resulting in homolytic cleavage of the carbon-sulfur bond to form a 5'-deoxyadenosyl radical that abstracts the hydrogen atom from the P-H bond of the substrate, forming a phosphinate-centered radical. This radical reacts with methylcob(III)alamin to produce the methylated product and cob...hosphinothricin-L-alanyl-L-alanine or N-acetyl-demethylphosphinothricin-L-alanyl-L-leucine, the intermediates in the biosynthesis of bialaphos and phosalacine, respectively. This transformation produces the only example of a carbon-phosphorus-carbon linkage known to occur in nature. Group: Enzymes. Synonyms: phpK (gene name); bcpD (gene name); P-methylase. Enzyme Commission Number: EC 2.1.1.326. 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-1934; N-acetyldemethylphosphinothricin P-methyltransferase; EC 2.1.1.326; phpK (gene name); bcpD (gene name); P-methylase. Cat No: EXWM-1934. | |
| N-acetylgalactosamine-N,N'-diacetylbacillosaminyl-diphospho-undecaprenol 4-α-N-acetylgalactosaminyltransferase | Isolated from Campylobacter jejuni. Part of a bacterial N-linked glycosylation pathway. Group: Enzymes. Synonyms: PglJ. Enzyme Commission Number: EC 2.4.1.291. 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-2525; N-acetylgalactosamine-N,N'-diacetylbacillosaminyl-diphospho-undecaprenol 4-α-N-acetylgalactosaminyltransferase; EC 2.4.1.291; PglJ. Cat No: EXWM-2525. | |
| NAD+-protein-arginine ADP-ribosyltransferase | Protein mono-ADP-ribosylation is a reversible post-translational modification that plays a role in the regulation of cellular activities. Arginine residues in proteins act as acceptors. Free arginine, agmatine [(4-aminobutyl)guanidine], arginine methyl ester and guanidine can also do so. The enzyme from some, but not all, species can also use NADP+ as acceptor (giving rise to Nω-[(2'-phospho-ADP)-D-ribosyl]-protein-L-arginine as the product), but more slowly. The enzyme catalyses the NAD+-dependent activation of EC 4.6.1.1, adenylate cyclase. Some bacterial enterotoxins possess similar enzymic activities. (cf. EC 2.4.2.36 NAD+-diphthamide ADP-ribosyltransferase). Group: Enzymes. Synonyms: AD. Enzyme Commission Number: EC 2.4.2.31. CAS No. 81457-93-4. 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-2659; NAD+-protein-arginine ADP-ribosyltransferase; EC 2.4.2.31; 81457-93-4; ADP-ribosyltransferase; mono(ADP-ribosyl)transferase; NAD+:L-arginine ADP-D-ribosyltransferase; NAD(P)+-arginine ADP-ribosyltransferase; NAD(P)+:L-arginine ADP-D-ribosyltransferase; mono-ADP-ribosyltransferase; ART; ART1; ART2; ART3; ART4; ART5; ART6; ART7; NAD(P)+-protein-arginine ADP-ribosyltransferase; NAD(P)+:protein-L-arginine ADP-D-ribosyltransferase. Cat No: EXWM-2659. | |
| Native Bacillus amyloliquefaciens Protease | Bacterial protease produced by submerged fermentation of a selected strain of Bacillus amyloliquefaciens. Secretion of protease by Bacillus amyloliquefaciens can be inhibited by treatment with the fatty acid synthetase inhibitor cerulenin. Bacterial protease produced by submerged fermentation of a selected strain of bacillus amyloliquefaciens. secretion of protease by bacillus amyloliquefaciens can be inhibited by treatment with the fatty acid synthetase inhibitor cerulenin. Applications: Protease from bacillus amyloliquefaciens has been used for the unhairing of hides and skins. it has also been used in a study to investigate peptide bond formation using the carbamoylmethyl ester as the acyl donor. Group: Enzymes. Synonyms: Protease; Neutrase. CAS No. 9001-92-7. Protease. Form: liquid, > 0.8 U/g. Source: Bacillus amyloliquefaciens. Protease; Neutrase. Cat No: NATE-0632. | |
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