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| Product | Description | |
|---|---|---|
| Enzyme of low hydrolysing | Low temperature starch hydrolysis. Applications: Apples & pears processing enzymes. Group: Enzymes. Synonyms: hydrolysing; Apples and Pears Processing Enzymes; Low temperature starch hydrolysis enzyme; Low temperature enzyme; Low temperature; starch hydrolysis;hydrolysis; Apples; Pears; Enzyme of low hydrolysing; FJE-1420. Enzyme of low hydrolysing. Appearance: powder or liquid. hydrolysing; Apples and Pears Processing Enzymes; Low temperature starch hydrolysis enzyme; Low temperature enzyme; Low temperature; starch hydrolysis;hydrolysis; Apples; Pears; Enzyme of low hydrolysing; FJE-1420. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form) or subject to client requirement. Cat No: FJE-1420. |  |
| 5-oxoprolinase (ATP-hydrolysing) | This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. This enzyme participates in glutathione metabolism. Group: Enzymes. Synonyms: pyroglutamase (ATP-hydrolysing); oxoprolinase; pyroglutamase; 5-oxoprolinase; pyroglutamate hydrolase; pyroglutamic hydrolase; L-pyroglutamate hydrolase; 5-oxo-L-prolinase; pyroglutamase. Enzyme Commission Number: EC 3.5.2.9. CAS No. 9075-46-1. 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-4510; 5-oxoprolinase (ATP-hydrolysing); EC 3.5.2.9; 9075-46-1; pyroglutamase (ATP-hydrolysing); oxoprolinase; pyroglutamase; 5-oxoprolinase; pyroglutamate hydrolase; pyroglutamic hydrolase; L-pyroglutamate hydrolase; 5-oxo-L-prolinase; pyroglutamase. Cat No: EXWM-4510. | |
| acyloxyacyl hydrolase | The substrate is lipid A on the reducing end of the toxic lipopolysaccharide (LPS) of Salmonella typhimurium and related organisms. It consists of diglucosamine, β-D-GlcN-(1? 6)-D-GlcN, attached by glycosylation on O-6 of its non-reducing residue, phosphorylated on O-4 of this residue and on O-1 of its potentially reducing residue. Both residues carry 3-(acyloxy)acyl groups on N-2 and O-3. The enzyme from human leucocytes detoxifies the lipid by hydrolysing the secondary acyl groups from O-3 of the 3-hydroxyacyl groups on the disaccharide (LPS). It also possesses a wide range of phospholipase and acyltransferase activities [e.g. EC 3.1.1.4 (phospholipase A2), EC 3.1.1.5 (lysophospholipase), EC 3.1.1.32 (phospholipase A1) and EC 3.1.1.52 (phosphatidylinositol deacylase)], hydrolysing diacylglycerol and phosphatidyl compounds, but not triacylglycerols. It has a preference for saturated C12-C16 acyl groups. Group: Enzymes. Enzyme Commission Number: EC 3.1.1.77. CAS No. 110277-64-0. 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-3505; acyloxyacyl hydrolase; EC 3.1.1.77; 110277-64-0. Cat No: EXWM-3505. | |
| adenosylcobyric acid synthase (glutamine-hydrolysing) | Requires Mg2+. NH3 can act instead of glutamine. This enzyme catalyses the four-step amidation sequence from cobyrinic acid a,c-diamide to cobyric acid via the formation of cobyrinic acid triamide, tetraamide and pentaamide intermediates. Group: Enzymes. Synonyms: CobQ; cobyric acid synthase; 5'-deoxy-5'-adenosylcobyrinic-acid-a,c-diamide:L-glutamine amido-ligase; Ado-cobyric acid synthase [glutamine hydrolyzing]. Enzyme Commission Number: EC 6.3.5.10. CAS No. 137672-90-3. 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-5803; adenosylcobyric acid synthase (glutamine-hydrolysing); EC 6.3.5.10; 137672-90-3; CobQ; cobyric acid synthase; 5'-deoxy-5'-adenosylcobyrinic-acid-a,c-diamide:L-glutamine amido-ligase; Ado-cobyric acid synthase [glutamine hydrolyzing]. Cat No: EXWM-5803. | |
| 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. | |
| aminodeoxyfutalosine synthase | This enzyme is a member of the 'AdoMet radical' (radical SAM) family. S-Adenosyl-L-methionine acts as both a radical generator and as the source of the transferred adenosyl group. The enzyme, found in several bacterial species, is part of the futalosine pathway for menaquinone biosynthesis. Group: Enzymes. Synonyms: MqnE; AFL synthase; aminofutalosine synthase; S-adenosyl-L-methionine:3-[(1-carboxyvinyl)-oxy]benzoate adenosyltransferase (bicarbonate-hydrolysing, 6-amino-6-deoxyfutalosine-forming). Enzyme Commission Number: EC 2.5.1.120. 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-2736; aminodeoxyfutalosine synthase; EC 2.5.1.120; MqnE; AFL synthase; aminofutalosine synthase; S-adenosyl-L-methionine:3-[(1-carboxyvinyl)-oxy]benzoate adenosyltransferase (bicarbonate-hydrolysing, 6-amino-6-deoxyfutalosine-forming). Cat No: EXWM-2736. | |
| apyrase | Apyrases are active against both di- and triphosphate nucleotides (NDPs and NTPs) and hydrolyse NTPs to nucleotide monophosphates (NMPs) in two distinct successive phosphate-releasing steps, with NDPs as intermediates. They differ from ATPases, which specifically hydrolyse ATP, by hydrolysing both ATP and ADP. The eukaryotic enzymes requires Ca2+, but Mg2+ can substitute. Most of the ecto-ATPases that occur on the cell surface and hydrolyse extracellular nucleotides belong to this enzyme family. Group: Enzymes. Synonyms: ATP-diphosphatase; adenosine diphosphatase; ADPase; ATP diphosphohydrolase [ambiguous]. Enzyme Commission Number: EC 3.6.1.5. CAS No. 9000-95-7. Apyrase. 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-4623; apyrase; EC 3.6.1.5; 9000-95-7; ATP-diphosphatase; adenosine diphosphatase; ADPase; ATP diphosphohydrolase [ambiguous]. Cat No: EXWM-4623. | |
| asparagine synthase (glutamine-hydrolysing) | The enzyme from Escherichia coli has two active sites that are connected by an intramolecular ammonia tunnel. The enzyme catalyses three distinct chemical reactions: glutamine hydrolysis to yield ammonia takes place in the N-terminal domain. The C-terminal active site mediates both the synthesis of a β-aspartyl-AMP intermediate and its subsequent reaction with ammonia. The ammonia released is channeled to the other active site to yield asparagine. Group: Enzymes. Synonyms: asparagine synthetase (glutamine-hydrolysing); glutamine-dependent asparagine synthetase; asparagine synthetase B; AS; AS-B. Enzyme Commission Number: EC 6.3.5.4. CAS No. 37318-72-2. 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-5807; asparagine synthase (glutamine-hydrolysing); EC 6.3.5.4; 37318-72-2; asparagine synthetase (glutamine-hydrolysing); glutamine-dependent asparagine synthetase; asparagine synthetase B; AS; AS-B. Cat No: EXWM-5807. | |
| asparaginyl-tRNA synthase (glutamine-hydrolysing) | This reaction forms part of a two-reaction system for producing asparaginyl-tRNA in Deinococcus radiodurans and other organisms lacking a specific enzyme for asparagine synthesis. In the first step, a non-discriminating ligase (EC 6.1.1.23, aspartate-tRNAAsn ligase) mischarges tRNAAsn with aspartate, leading to the formation of Asp-tRNAAsn. The aspartyl-tRNAAsn is not used in protein synthesis until the present enzyme converts it into asparaginyl-tRNAAsn (aspartyl-tRNAAsp is not a substrate for this reaction). Ammonia or asparagine can substitute for the preferred substrate glutamine. Group: Enzymes. Synonyms: Asp-AdT; Asp-tRNAAsn amidotransferase; aspartyl-tRNAAsn amidotransferase; Asn-tRNAAsn:L-glutamine amido-ligase (ADP-forming); aspartyl-tRNAAsn:L-glutamine amido-ligase (ADP-forming). Enzyme Commission Number: EC 6.3.5.6. CAS No. 37211-76-0. 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-5809; asparaginyl-tRNA synthase (glutamine-hydrolysing); EC 6.3.5.6; 37211-76-0; Asp-AdT; Asp-tRNAAsn amidotransferase; aspartyl-tRNAAsn amidotransferase; Asn-tRNAAsn:L-glutamine amido-ligase (ADP-forming); aspartyl-tRNAAsn:L-glutamine amido-ligase (ADP-forming). Cat No: EXWM-5809. | |
| aspartate-tRNAAsn ligase | When this enzyme acts on tRNAAsp, it catalyses the same reaction as EC 6.1.1.12, aspartate-tRNA ligase. It has, however, diminished discrimination, so that it can also form aspartyl-tRNAAsn. This relaxation of specificity has been found to result from the absence of a loop in the tRNA that specifically recognizes the third position of the anticodon. This accounts for the ability of this enzyme in, for example, Thermus thermophilus, to recognize both tRNAAsp (GUC anticodon) and tRNAAsn (GUU anticodon). The aspartyl-tRNAAsn is not used in protein synthesis until it is converted by EC 6.3.5.6, asparaginyl-tRNA synthase (glutamine-hydrolysing), into asparaginyl-tRNAAsn. Group: Enzymes. Synonyms: nondiscriminating aspartyl-tRNA synthetase. Enzyme Commission Number: EC 6.1.1.23. CAS No. 9027-32-1. 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-5655; aspartate-tRNAAsn ligase; EC 6.1.1.23; 9027-32-1; nondiscriminating aspartyl-tRNA synthetase. Cat No: EXWM-5655. | |
| 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-lactamase | A group of enzymes of varying specificity hydrolysing β-lactams; some act more rapidly on penicillins, some more rapidly on cephalosporins. The latter were formerly listed as EC 3.5.2.8, cephalosporinase. Group: Enzymes. Synonyms: penicillinase; cephalosporinase; neutrapen; penicillin β-lactamase; exopenicillinase; ampicillinase; penicillin amido-β-lactamhydrolase; penicillinase I, II; β-lactamase I-III; β-lactamase A, B, C; β-lactamase AME I; cephalosporin-β-lactamase. Enzyme Commission Number: EC 3.5.2.6. CAS No. 9073-60-3. β-Lactamase. 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-4508; β-lactamase; EC 3.5.2.6; 9073-60-3; penicillinase; cephalosporinase; neutrapen; penicillin β-lactamase; exopenicillinase; ampicillinase; penicillin amido-β-lactamhydrolase; penicillinase I, II; β-lactamase I-III; β-lactamase A, B, C; β-lactamase AME I; cephalosporin-β-lactamase. Cat No: EXWM-4508. | |
| biotin-[propionyl-CoA-carboxylase (ATP-hydrolysing)] ligase | This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. This enzyme participates in biotin metabolism. Group: Enzymes. Synonyms: biotin-[propionyl-CoA-carboxylase (ATP-hydrolysing)] synthetase; biotin-propionyl coenzyme A carboxylase synthetase; propionyl coenzyme A holocarboxylase synthetase. Enzyme Commission Number: EC 6.3.4.10. CAS No. 37318-67-5. 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-5779; biotin-[propionyl-CoA-carboxylase (ATP-hydrolysing)] ligase; EC 6.3.4.10; 37318-67-5; biotin-[propionyl-CoA-carboxylase (ATP-hydrolysing)] synthetase; biotin-propionyl coenzyme A carboxylase synthetase; propionyl coenzyme A holocarboxylase synthetase. Cat No: EXWM-5779. | |
| Biotinylated Luciferase from E. coli, Recombinant | Luciferase is an enzyme that catalyzes production of light from luciferin in the presence of Mg2+-ATP and oxygen. The reaction of this enzyme with luciferin, ATP, and O2 results in the emission of light. Luciferase activity can be inhibited by general anesthetics including isoflurane and ketamine/medetomidine thereby affecting the sensitivity of bioluminescence imaging. Group: Enzymes. Synonyms: Photinus-luciferin 4-monooxygenase (ATP-hydrolysing); firefly luciferase; luciferase (firefly luciferin); Photinus luciferin 4-monooxygenase (adenosine triphosphate-hydrolyzing); firefly luciferin luciferase; Photinus pyralis luciferase; EC 1.13.12.7; 61970-00-1. Enzyme Commission Number: EC 1.13.12.7. Luciferase. Mole weight: ca. 70 kDa. Activity: > 1.0 x 10^10 relative light units (RLU)/ml Specific activity: 1.9 x 10^11 RLU/mg purified protein. Stability: stable at 25°C for at least one week (liquid form). Appearance: Liquid form. Storage: at -20°C. Source: E. coli. Species: E. coli. Photinus-luciferin 4-monooxygenase (ATP-hydrolysing); firefly luciferase; luciferase (firefly luciferin); Photinus luciferin 4-monooxygenase (adenosine triphosphate-hydrolyzing); firefly luciferin luciferase; Photinus pyralis luciferase; EC 1.13.12.7; 61970-00-1. Cat No: NATE-1254. | |
| carbamoyl-phosphate synthase (ammonia) | The enzyme catalyses the first committed step in the urea cycle. The reaction proceeds via three separate chemical reactions: phosphorylation of hydrogencarbonate to carboxyphosphate; a nucleophilic attack of ammonia on carboxyphosphate yielding carbamate; and the phosphorylation of carbamate forming carbamoyl phosphate. Two moles of ATP are utilized for the synthesis of one molecule of carbamyl phosphate, making the reaction essentially irreversible. The enzyme requires the allosteric activator N-acetyl-L-glutamate. cf. EC 6.3.5.5, carbamoyl-phosphate synthase (glutamine-hydrolysing). Group: Enzymes. Synonyms: carbon-dioxide-ammonia ligase; carbamoylphosphate synthase; carbamylphosphate synthetase; carbamoylphosphate synthase (ammonia); carbamoylphosphate synthetase; carbamylphosphate s. Enzyme Commission Number: EC 6.3.4.16. CAS No. 9026-23-7. 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-5785; carbamoyl-phosphate synthase (ammonia); EC 6.3.4.16; 9026-23-7; carbon-dioxide-ammonia ligase; carbamoylphosphate synthase; carbamylphosphate synthetase; carbamoylphosphate synthase (ammonia); carbamoylphosphate synthetase; carbamylphosphate synthetase I; CPSI (gene name); carbon-dioxide:ammonia ligase (ADP-forming, carbamate-phosphorylating). Cat No: EXWM-5785. | |
| carbamoyl-phosphate synthase (glutamine-hydrolysing) | The product carbamoyl phosphate is an intermediate in the biosynthesis of arginine and the pyrimidine nucleotides. The enzyme from Escherichia coli has three separate active sites, which are connected by a molecular tunnel that is almost 100 ? in length. The amidotransferase domain within the small subunit of the enzyme hydrolyses glutamine to ammonia via a thioester intermediate. The ammonia migrates through the interior of the protein, where it reacts with carboxyphosphate to produce the carbamate intermediate. The carboxyphosphate intermediate is formed by the phosphorylation of hydrogencarbonate by ATP at a site contained within the N-terminal half of the large ... (gene name); CAD (gene name); hydrogen-carbonate:L-glutamine amido-ligase (ADP-forming, carbamate-phosphorylating). Enzyme Commission Number: EC 6.3.5.5. CAS No. 37233-48-0. 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-5808; carbamoyl-phosphate synthase (glutamine-hydrolysing); EC 6.3.5.5; 37233-48-0; carbamoyl-phosphate synthetase (glutamine-hydrolysing); carbamyl phosphate synthetase (glutamine); carbamoylphosphate synthetase II; glutamine-dependent carbamyl phosphate synthetase; carbamoyl phosphate synthetase; CPS; carbon-dioxide:L-glutamine amido-ligase (ADP-forming, carbam | |
| c[G(2',5')pS-A(3',5')pS], isomer 1 and isomer 2 | c[G(2',5')pS-A(3',5')pS] is an isomeric di-thiophosphate analogue of c[G(2',5')pA(3',5')p], the metazoan cyclic dinucleotide second messenger. It is resistant against the 2'3'-cGAMP hydrolysing enzyme ENPP1, and compared to natural 2'3'-cGAMP, it exhibits higher potency in inducing IFN-β secretion from human THP1 monocytes. Grades: ≥ 95% by HPLC. CAS No. 1638242-56-4 / 1638243-00-1. Molecular formula: C20H24N10O11P2S2 (free acid). Mole weight: 706.6 (free acid). |  |
| CTP synthase (glutamine hydrolysing) | The enzyme contains three functionally distinct sites: an allosteric GTP-binding site, a glutaminase site where glutamine hydrolysis occurs (cf. EC 3.5.1.2, glutaminase), and the active site where CTP synthesis takes place. The reaction proceeds via phosphorylation of UTP by ATP to give an activated intermediate 4-phosphoryl UTP and ADP. Ammonia then reacts with this intermediate generating CTP and a phosphate. The enzyme can also use ammonia from the surrounding solution. Group: Enzymes. Synonyms: UTP-ammonia ligase; cytidine triphosphate synthetase; uridine triphosphate aminase; cytidine 5'-triphosphate synthetase; CTPS (gene name); pyrG (gene name); CTP synthase; UTP:ammonia ligase (ADP-forming). Enzyme Commission Number: EC 6.3.4.2. CAS No. 9023-56-7. 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-5789; CTP synthase (glutamine hydrolysing); EC 6.3.4.2; 9023-56-7; UTP-ammonia ligase; cytidine triphosphate synthetase; uridine triphosphate aminase; cytidine 5'-triphosphate synthetase; CTPS (gene name); pyrG (gene name); CTP synthase; UTP:ammonia ligase (ADP-forming). Cat No: EXWM-5789. | |
| cyanophycinase | The enzyme is highly specific for the branched polypeptide cyanophycin and does not hydrolyse poly-L-aspartate or poly-L-arginine. A serine-type exopeptidase that belongs in peptidase family S51. Group: Enzymes. Synonyms: cyanophycin degrading enzyme; β-Asp-Arg hydrolysing enzyme; CGPase; CphB; CphE; cyanophycin granule polypeptidase; extracellular CGPase. Enzyme Commission Number: EC 3.4.15.6. CAS No. 131554-16-0. 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-4056; cyanophycinase; EC 3.4.15.6; 131554-16-0; cyanophycin degrading enzyme; β-Asp-Arg hydrolysing enzyme; CGPase; CphB; CphE; cyanophycin granule polypeptidase; extracellular CGPase. Cat No: EXWM-4056. | |
| desampylase | The enzyme, characterized from the archaeon Haloferax volcanii, specifically cleaves the ubiquitin-like small modifier proteins SAMP1 and SAMP2 from protein conjugates, hydrolysing the isopeptide bond between a lysine residue of the target protein and the C-terminal glycine of the modifier protein. The enzyme contains Zn2+. cf. EC 3.4.19.12, ubiquitinyl hydrolase 1. In peptidase family M67. Group: Enzymes. Synonyms: SAMP-protein conjugate cleaving protease; HvJAMM1. Enzyme Commission Number: EC 3.4.24.88. 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-4372; desampylase; EC 3.4.24.88; SAMP-protein conjugate cleaving protease; HvJAMM1. Cat No: EXWM-4372. | |
| dichloromethane dehalogenase | Requires glutathione. Group: Enzymes. Synonyms: dichloromethane chloride-lyase (chloride-hydrolysing). Enzyme Commission Number: EC 4.5.1.3. CAS No. 97002-70-5. 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-5345; dichloromethane dehalogenase; EC 4.5.1.3; 97002-70-5; dichloromethane chloride-lyase (chloride-hydrolysing). Cat No: EXWM-5345. | |
| DNA topoisomerase | These enzymes bring about the conversion of one topological isomer of DNA into another, e.g., the relaxation of superhelical turns in DNA, the interconversion of simple and knotted rings of single-stranded DNA, and the intertwisting of single-stranded rings of complementary sequences, cf. EC 5.99.1.3 DNA topoisomerase (ATP-hydrolysing). Group: Enzymes. Synonyms: type I DNA topoisomerase; untwisting enzyme; relaxing enzyme; nicking-closing enzyme; swivelase; ω-protein; deoxyribonucleate topoisomerase; topoisomerase; type I DNA topoisomerase. Enzyme Commission Number: EC 5.99.1.2. CAS No. 80449-01-0. TOPO I. 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-5637; DNA topoisomerase; EC 5.99.1.2; 80449-01-0; type I DNA topoisomerase; untwisting enzyme; relaxing enzyme; nicking-closing enzyme; swivelase; ω-protein; deoxyribonucleate topoisomerase; topoisomerase; type I DNA topoisomerase. Cat No: EXWM-5637. | |
| DNA topoisomerase (ATP-hydrolysing) | The enzyme can introduce negative superhelical turns into double-stranded circular DNA. One unit has nicking-closing activity, and another catalyses super-twisting and hydrolysis of ATP (cf. EC 5.99.1.2 DNA topoisomerase). Group: Enzymes. Synonyms: type II DNA topoisomerase; DNA-gyrase; deoxyribonucleate topoisomerase; deoxyribonucleic topoisomerase; topoisomerase; DNA topoisomerase II. Enzyme Commission Number: EC 5.99.1.3. CAS No. 142805-56-9. TOPO II. 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-5638; DNA topoisomerase (ATP-hydrolysing); EC 5.99.1.3; 142805-56-9; type II DNA topoisomerase; DNA-gyrase; deoxyribonucleate topoisomerase; deoxyribonucleic topoisomerase; topoisomerase; DNA topoisomerase II. Cat No: EXWM-5638. | |
| double-stranded uracil-DNA glycosylase | No activity on DNA containing a T/G mispair or single-stranded DNA containing either a site-specific uracil or 3,N4-ethenocytosine residue, significant role for double-stranded uracil-DNA glycosylase in mutation avoidance in non-dividing E. coli. Uracil-DNA glycosylases are widespread enzymes that are found in all living organisms. Uracil-DNA glycosylase (EC 3.2.2.27) and EC 3.2.2.28 form a central part of the DNA-repair machinery since they initiate the DNA base-excision repair pathway by hydrolysing the N-glycosidic bond between uracil and the deoxyribose sugar thereby catalysing the removal of mis-incorporated uracil from DNA. Group: Enzymes. Synonyms: Mug; double-strand uracil-DNA glycosylase; Dug; dsUDG; double-stranded DNA specific UDG; dsDNA specific UDG; UdgB (ambiguous); G:T/U mismatch-specific DNA glycosylase; UDG (ambiguous). Enzyme Commission Number: EC 3.2.2.28. 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-3982; double-stranded uracil-DNA glycosylase; EC 3.2.2.28; Mug; double-strand uracil-DNA glycosylase; Dug; dsUDG; double-stranded DNA specific UDG; dsDNA specific UDG; UdgB (ambiguous); G:T/U mismatch-specific DNA glycosylase; UDG (ambiguous). Cat No: EXWM-3982. | |
| ginsenoside Rb1 β-glucosidase | Ginsenosidases catalyse the hydrolysis of glycosyl moieties attached to the C-3, C-6 or C-20 position of ginsenosides. They are specific with respect to the nature of the glycosidic linkage, the position and the order in which the linkages are cleaved. Ginsenoside Rb1 β-glucosidase specifically and sequentially hydrolyses the 20-[β-D-glucopyranosyl-(1?6)-β-D glucopyranosyloxy] residues attached to position 20 by first hydrolysing the (1?6)-glucosidic bond to generate ginsenoside Rd as an intermediate, followed by hydrolysis of the remaining 20-O-β-D-glucosidic bond. Group: Enzymes. Enzyme Commission Number: EC 3.2.1.192. 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-3876; ginsenoside Rb1 β-glucosidase; EC 3.2.1.192. Cat No: EXWM-3876. | |
| glutamate synthase (ferredoxin) | Binds a [3Fe-4S] cluster as well as FAD and FMN. The protein is composed of two domains, one hydrolysing L-glutamine to NH3 and L-glutamate (cf. EC 3.5.1.2, glutaminase), the other combining the produced NH3 with 2-oxoglutarate to produce a second molecule of L-glutamate. The NH3 is channeled through a 24 ? channel in the active protein. No hydrolysis of glutamine takes place without ferredoxin and 2-oxoglutarate being bound to the protein. Group: Enzymes. Synonyms: ferredoxin-dependent glutamate synthase; ferredoxin-glutamate synthase; glutamate synthase (ferredoxin-dependent). Enzyme Commission Number: EC 1.4.7.1. CAS No. 62213-56-3. 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-1487; glutamate synthase (ferredoxin); EC 1.4.7.1; 62213-56-3; ferredoxin-dependent glutamate synthase; ferredoxin-glutamate synthase; glutamate synthase (ferredoxin-dependent). Cat No: EXWM-1487. | |
| glutamate-tRNAGln ligase | When this enzyme acts on tRNAGlu, it catalyses the same reaction as EC 6.1.1.17, glutamate-tRNA ligase. It has, however, diminished discrimination, so that it can also form glutamyl-tRNAGln. This relaxation of specificity has been found to result from the absence of a loop in the tRNA that specifically recognizes the third position of the anticodon. This accounts for the ability of this enzyme in, for example, Bacillus subtilis, to recognize both tRNA1Gln (UUG anticodon) and tRNAGlu (UUC anticodon) but not tRNA2Gln (CUG anticodon). The ability of this enzyme to recognize both tRNAGlu and one of the tRNAGln isoacceptors derives from their sharing a major identity element, a hypermodified derivative of U34 (5-methylaminomethyl-2-thiouridine). The glutamyl-tRNAGln is not used in protein synthesis until it is converted by EC 6.3.5.7, glutaminyl-tRNA synthase (glutamine-hydrolysing), into glutaminyl-tRNAGln. Group: Enzymes. Synonyms: nondiscriminating glutamyl-tRNA synthetase. Enzyme Commission Number: EC 6.1.1.24. CAS No. 9068-76-2. 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-5656; glutamate-tRNAGln ligase; EC 6.1.1.24; 9068-76-2; nondiscriminating glutamyl-tRNA synthetase. Cat No: EXWM-5656. | |
| glutaminyl-tRNA synthase (glutamine-hydrolysing) | In systems lacking discernible glutamine-tRNA ligase (EC 6.1.1.18), glutaminyl-tRNAGln is formed by a two-enzyme system. In the first step, a nondiscriminating ligase (EC 6.1.1.24, glutamate-tRNAGln ligase) mischarges tRNAGln with glutamate, forming glutamyl-tRNAGln. The glutamyl-tRNAGln is not used in protein synthesis until the present enzyme converts it into glutaminyl-tRNAGln (glutamyl-tRNAGlu is not a substrate for this reaction). Ammonia or asparagine can substitute for the preferred substrate glutamine. Group: Enzymes. Synonyms: Glu-AdT; Glu-tRNAGln amidotransferase; glutamyl-tRNAGln amidotransferase; Glu-tRNAGln:L-glutamine amido-ligase (ADP-forming). Enzyme Commission Number: EC 6.3.5.7. CAS No. 52232-48-1. 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-5810; glutaminyl-tRNA synthase (glutamine-hydrolysing); EC 6.3.5.7; 52232-48-1; Glu-AdT; Glu-tRNAGln amidotransferase; glutamyl-tRNAGln amidotransferase; Glu-tRNAGln:L-glutamine amido-ligase (ADP-forming). Cat No: EXWM-5810. | |
| GMP synthase (glutamine-hydrolysing) | Involved in the de novo biosynthesis of guanosine nucleotides. An N-terminal glutaminase domain binds L-glutamine and generates ammonia, which is transferred by a substrate-protective tunnel to the ATP-pyrophosphatase domain. The enzyme can catalyse the second reaction alone in the presence of ammonia. Group: Enzymes. Synonyms: GMP synthetase (glutamine-hydrolysing); guanylate synthetase (glutamine-hydrolyzing); guanosine monophosphate synthetase (glutamine-hydrolyzing); xanthosine 5'-phosphate amidotransferase; guanosine 5'-monophosphate synthetase. Enzyme Commission Number: EC 6.3.5.2. CAS No. 37318-71-1. 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-5805; GMP synthase (glutamine-hydrolysing); EC 6.3.5.2; 37318-71-1; GMP synthetase (glutamine-hydrolysing); guanylate synthetase (glutamine-hydrolyzing); guanosine monophosphate synthetase (glutamine-hydrolyzing); xanthosine 5'-phosphate amidotransferase; guanosine 5'-monophosphate synthetase. Cat No: EXWM-5805. | |
| heterotrimeric G-protein GTPase | This group comprises GTP-hydrolysing systems, where GTP and GDP alternate in binding. This group includes stimulatory and inhibitory G-proteins such as Gs, Gi, Go and Golf, targetting adenylate cyclase and/or K+ and Ca2+ channels; Gq stimulating phospholipase C; transducin activating cGMP phosphodiesterase; gustducin activating cAMP phosphodiesterase. Golf is instrumental in odour perception, transducin in vision and gustducin in taste recognition. At least 16 different α subunits (39-52 kDa), 5 β subunits (36 kDa) and 12 γ subunits (6-9 kDa) are known. Group: Enzymes. Enzyme Commission Number: EC 3.6.5.1. 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-4712; heterotrimeric G-protein GTPase; EC 3.6.5.1. Cat No: EXWM-4712. | |
| hydrogenobyrinic acid a,c-diamide synthase (glutamine-hydrolysing) | This step in the aerobic biosynthesis of cobalamin generates hydrogenobyrinic acid a,c-diamide, the substrate required by EC 6.6.1.2, cobaltochelatase, which adds cobalt to the macrocycle. Group: Enzymes. Synonyms: CobB. Enzyme Commission Number: EC 6.3.5.9. CAS No. 132053-22-6. 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-5811; hydrogenobyrinic acid a,c-diamide synthase (glutamine-hydrolysing); EC 6.3.5.9; 132053-22-6; CobB. Cat No: EXWM-5811. | |
| Hydrolysing for apple juice | Starch hydrolysis for apple juice processing. Applications: Apples & pears processing enzymes. Group: Enzymes. Synonyms: Hydrolysing for apple juice; Apples and Pears Processing Enzymes; Starch hydrolysis enzyme; Hydrolysing;apple juice; Pears Processing; Hydrolysing for apple juice; FJE-1419. Enzymes for apple juice. Appearance: powder or liquid. Hydrolysing for apple juice; Apples and Pears Processing Enzymes; Starch hydrolysis enzyme; Hydrolysing;apple juice; Pears Processing; Hydrolysing for apple juice; FJE-1419. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form) or subject to client requirement. Cat No: FJE-1419. | |
| hydroxymethylbilane synthase | The enzyme works by stepwise addition of pyrrolylmethyl groups until a hexapyrrole is present at the active centre. The terminal tetrapyrrole is then hydrolysed to yield the product, leaving a cysteine-bound dipyrrole on which assembly continues. In the presence of a second enzyme, EC 4.2.1.75 uroporphyrinogen-III synthase, which is often called cosynthase, the product is cyclized to form uroporphyrinogen-III. If EC 4.2.1.75 is absent, the hydroxymethylbilane cyclizes spontaneously to form uroporphyrinogen I. Group: Enzymes. Synonyms: HMB-synthase; porphobilinogen deaminase; pre-uroporphyrinogen synthase; uroporphyrinogen I synthase; uroporphyrinogen I synthetase; uroporphyrinogen synthase; uroporphyrinogen synthetase; porphobilinogen ammonia-lyase (polymerizing); (4-[2-car. Enzyme Commission Number: EC 2.5.1.61. CAS No. 9074-91-3. 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-2799; hydroxymethylbilane synthase; EC 2.5.1.61; 9074-91-3; HMB-synthase; porphobilinogen deaminase; pre-uroporphyrinogen synthase; uroporphyrinogen I synthase; uroporphyrinogen I synthetase; uroporphyrinogen synthase; uroporphyrinogen synthetase; porphobilinogen ammonia-lyase (polymerizing); (4-[2-carboxyethyl]-3-[carboxymethyl]pyrrol-2-yl)methyltransferase (hydrolysing). Cat No: EXWM-2799. | |
| lovastatin nonaketide synthase | This fungal enzyme system comprises a multi-functional polyketide synthase (PKS) and an enoyl reductase. The PKS catalyses many of the chain building reactions of EC 2.3.1.85, fatty-acid synthase, as well as a reductive methylation and a Diels-Alder reaction, while the reductase is responsible for three enoyl reductions that are necessary for dihydromonacolin L acid production. Group: Enzymes. Synonyms: LNKS; LovB; LovC; acyl-CoA:malonyl-CoA C-acyltransferase (decarboxylating, oxoacyl- and enoyl-reducing, thioester-hydrolysing). Enzyme Commission Number: EC 2.3.1.161. CAS No. 235426-97-8. 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-2101; lovastatin nonaketide synthase; EC 2.3.1.161; 235426-97-8; LNKS; LovB; LovC; acyl-CoA:malonyl-CoA C-acyltransferase (decarboxylating, oxoacyl- and enoyl-reducing, thioester-hydrolysing). Cat No: EXWM-2101. | |
| Luciferase from E. coli, Recombinant | Luciferase is an enzyme that catalyzes production of light from luciferin in the presence of Mg2+-ATP and oxygen. The reaction of this enzyme with luciferin, ATP, and O2 results in the emission of light. Luciferase activity can be inhibited by general anesthetics including isoflurane and ketamine/medetomidine thereby affecting the sensitivity of bioluminescence imaging. Group: Enzymes. Synonyms: Photinus-luciferin 4-monooxygenase (ATP-hydrolysing); firefly luciferase; luciferase (firefly luciferin); Photinus luciferin 4-monooxygenase (adenosine triphosphate-hydrolyzing); firefly luciferin luciferase; Photinus pyralis luciferase; EC 1.13.12.7; 61970-00-1. Enzyme Commission Number: EC 1.13.12.7. Luciferase. Mole weight: ca. 60 kDa. Activity: > 1.0 x 10^9 relative light units (RLU)/mg lyophilizate Specific activity: 1.4 x 10^11 RLU/mg purified protein. Stability: stable at 25°C for at least 5 days (liquid form). Appearance: White lyophilizate. Storage: at -20°C. Source: E. coli. Species: E. coli. Photinus-luciferin 4-monooxygenase (ATP-hydrolysing); firefly luciferase; luciferase (firefly luciferin); Photinus luciferin 4-monooxygenase (adenosine triphosphate-hydrolyzing); firefly luciferin luciferase; Photinus pyralis luciferase; EC 1.13.12.7; 61970-00-1. Cat No: NATE-1253. | |
| Luciferase from Photinus pyralis (firefly), Recombinant | Firefly luciferase is an enzyme that catalyzes production of light from luciferin in the presence of Mg2+-ATP and oxygen. The reaction of this enzyme with luciferin, ATP, and O2 results in the emission of light. Luciferase activity can be inhibited by general anesthetics including isoflurane and ketamine/medetomidine thereby affecting the sensitivity of bioluminescence imaging. Applications: The reaction of this enzyme with luciferin, atp, and o2 results in the emission of light. luciferase can be used to detect trace amounts of atp. firefly luciferase is also one of the most commonly utilized reporter genes for the study of gene expression. the bioluminescent rea...pe I , > 5 ,000 ,000 units/mg protein; Type II, 15-30×106 light units/mg protein. Storage: -70°C. Form: Type I, Supplied as a solution in 50 mM Tris HCl pH 8.0, 1 mM dithiothreitol, 1 mM EDTA, and 10% (v/v) glycerol; Type II, Lyophilized powder approximately 20% protein; balance is primarily NaCl, HEPES buffer salts, and carbohydrate. Source: E. coli. Species: Photinus pyralis (firefly). Photinus-luciferin 4-monooxygenase (ATP-hydrolysing); firefly luciferase; luciferase (firefly luciferin); Photinus luciferin 4-monooxygenase (adenosine triphosphate-hydrolyzing); firefly luciferin luciferase; Photinus pyralis luciferase; EC 1.13.12.7; 61970-00-1. Cat No: NATE-0424. | |
| malate synthase | The enzyme catalyses the irreversible condensation of acetyl-CoA with glyoxylate to form (S)-malate. Among other functions, the enzyme participates in the glyoxylate cycle, a modified version of the TCA cycle that bypasses steps that lead to a loss of CO2. Group: Enzymes. Synonyms: L-malate glyoxylate-lyase (CoA-acetylating); glyoxylate transacetylase; glyoxylate transacetase; glyoxylic transacetase; malate condensing enzyme; malate synthetase; malic synthetase; malic-condensing enzyme; acetyl-CoA:glyoxylate C-acetyltransferase (thioester-hydrolysing, carboxymethyl-forming). Enzyme Commission Number: EC 2.3.3.9. CAS No. 9013-48-3. 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-2325; malate synthase; EC 2.3.3.9; 9013-48-3; L-malate glyoxylate-lyase (CoA-acetylating); glyoxylate transacetylase; glyoxylate transacetase; glyoxylic transacetase; malate condensing enzyme; malate synthetase; malic synthetase; malic-condensing enzyme; acetyl-CoA:glyoxylate C-acetyltransferase (thioester-hydrolysing, carboxymethyl-forming). Cat No: EXWM-2325. | |
| N-acetylphosphatidylethanolamine-hydrolysing phospholipase D | This enzyme is involved in the biosynthesis of anandamide. It does not hydrolyse phosphatidylcholine and phosphatidylethanolamine. No transphosphatidation. The enzyme contains Zn2+ and is activated by Mg2+ or Ca2+. Group: Enzymes. Synonyms: NAPE-PLD; anandamide-generating phospholipase D; N-acyl phosphatidylethanolamine phospholipase D; NAPE-hydrolyzing phospholipase D. Enzyme Commission Number: EC 3.1.4.54. 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-3737; N-acetylphosphatidylethanolamine-hydrolysing phospholipase D; EC 3.1.4.54; NAPE-PLD; anandamide-generating phospholipase D; N-acyl phosphatidylethanolamine phospholipase D; NAPE-hydrolyzing phospholipase D. Cat No: EXWM-3737. | |
| NAD+ synthase (glutamine-hydrolysing) | NH3 can act instead of glutamine (cf. EC 6.3.1.5 NAD+ synthase). Group: Enzymes. Synonyms: NAD synthetase (glutamine-hydrolysing); nicotinamide adenine dinucleotide synthetase (glutamine); desamidonicotinamide adenine dinucleotide amidotransferase; DPN synthetase. Enzyme Commission Number: EC 6.3.5.1. CAS No. 37318-70-0. 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-5802; NAD+ synthase (glutamine-hydrolysing); EC 6.3.5.1; 37318-70-0; NAD synthetase (glutamine-hydrolysing); nicotinamide adenine dinucleotide synthetase (glutamine); desamidonicotinamide adenine dinucleotide amidotransferase; DPN synthetase. Cat No: EXWM-5802. | |
| Native Corynebacterium lilium Creatinine Deiminase | Hydrolase for creatinine determination that catalyzes the conversion of creatinine to N-methylhydantoin and ammonia. Rely on the proven diagnostic quality of this product. Applications: Use creatinine deaminase in diagnostic tests for the determination of creatinine in combination with n-carbamoylsarcosine amidase, n-methylhydantoinase (atp-hydrolysing) and sarcosine oxidase. Group: Enzymes. Synonyms: Creatinine hydrolase; creatinine desiminase. Creatinine Deiminase. Activity: 45.0-90.0 U/mg lyophilizate. Stability: At +2 to +8°C within specification range for 12 months. Store dry. Protect from light. Appearance: Beige lyophilizate. Source: Corynebacterium lilium. Creatinine hydrolase; Creatinine deaminase; EC 3.5.4.21; creatinine desiminase. Cat No: DIA-291. | |
| Native E. coli N-Carbamoylsarcosine Amidase | In enzymology, a N-carbamoylsarcosine amidase is an enzyme that catalyzes the chemical reaction: N-carbamoylsarcosine + H2O rightleftharpoons sarcosine + CO2 + NH3. Thus, the two substrates of this enzyme are N-carbamoylsarcosine and H2O, whereas its 3 products are sarcosine, CO2, and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. This enzyme participates in arginine and proline metabolism. Hydrolase that catalyzes the interconversion of n-carbamoylsarcosine to sarcosine. Applications: Use n-carbamoylsarcosine amidase in diagnostic tests for the determination of creatinine in combination with creatinine deaminase, n-methylhydantoinase (atp-hydrolysing) and sarcosine oxidase. Group: Enzymes. Synonyms: N-carbamoylsarcosine amidase; N-carbamoylsarcosine amidohydrolase; carbamoylsarcosine amidase. CAS No. 92767-52-7. N-Carbamoylsarcosine Amidase. Activity: 0.80-1.30 U/mg. Stability: At -15 to -25°C within specification range for 12 months. Store dry. Protect from light. Appearance: White lyophilizate. Source: E. coli. Species: E. coli. N-carbamoylsarcosine amidase; N-carbamoylsarcosine amidohydrolase; carbamoylsarcosine amidase. Cat No: NATE-0876. | |
| Native Human Topoisomerase II α | Topoisomerase II α (TopoIIα) is a gene product with conserved catalytic activities and it promotes the progression of DNA damage. The α isoform is present in proliferating cells. Applications: Topoisomerase ii α has been used in a study to assess aging pr ocesses in the human brain. topoisomerase ii α has also been used in a study to investigate its activity in hiv-1 replication. Group: Enzymes. Synonyms: type II DNA topoisomerase; DNA-gyrase; deoxyribonucleate topoisomerase; deoxyribonucleic topoisomerase; topoisomerase; DNA topoisomerase II; DNA topoisomerase (ATP-hydrolysing); EC 5.99.1.3; Topoisomerase II α; TOPO II. Enzyme Commission Number: EC 5.99.1.3. CAS No. 37318-49-3. TOPO II. Mole weight: mol wt 170 kDa. Storage: -70°C. Form: liquid; Solution in 10 mM Tris-HCl, pH 7.1, 0.25 M NaCl, 1 mM EDTA, 0.5 mM PMSF, 1 mM 2-mercaptoethanol, 10% glycerol. Source: Human. type II DNA topoisomerase; DNA-gyrase; deoxyribonucleate topoisomerase; deoxyribonucleic topoisomerase; topoisomerase; DNA topoisomerase II; DNA topoisomerase (ATP-hydrolysing); EC 5.99.1.3; Topoisomerase II α; TOPO II. Cat No: NATE-0710. | |
| Native Photinus pyralis (firefly) Luciferase | Firefly luciferase is an enzyme that catalyzes production of light from luciferin in the presence of Mg2+-ATP and oxygen. The reaction of this enzyme with luciferin, ATP, and O2 results in the emission of light. Luciferase activity can be inhibited by general anesthetics including isoflurane and ketamine/medetomidine thereby affecting the sensitivity of bioluminescence imaging. Applications: The reaction of this enzyme with luciferin, atp, and o2 results in the emission of light. luciferase can be used to detect trace amounts of atp. firefly luciferase is also one of the most commonly utilized reporter genes for the study of gene expression. the bioluminescent reaction ... been used in a study to identify the different characteristics of reporter genes in whole-cell bacterial sensors. luciferase from photinus pyralis has also been used in a study to develop a novel bioluminogenic assay for α-chymotrypsin. Group: Enzymes. Synonyms: Photinus-luciferin 4-monooxygenase (ATP-hydrolysing); firefly luciferase; luciferase (firefly luciferin); Photinus luciferin 4-monooxygenase (adenosine triphosphate-hydrolyzing); firefly luciferin luciferase; Photinus pyralis luciferase; EC 1.13.12.7; 61970-00-1. Enzyme Commission Number: EC 1.13.12.7. CAS No. 9014-00-0. Luciferase. Mole weight: mol wt 120 kDa (two subunits). Form: Lyophilized powder appr | |
| N-methylhydantoinase (ATP-hydrolysing) | This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. This enzyme participates in arginine, creatinine, and proline metabolism. Group: Enzymes. Synonyms: N-methylhydantoin amidohydrolase; methylhydantoin amidase; N-methylhydantoin hydrolase; N-methylhydantoinase; N-methylimidazolidine-2,4-dione amidohydrolase (ATP-hydrolysing). Enzyme Commission Number: EC 3.5.2.14. CAS No. 100785-00-0. 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-4497; N-methylhydantoinase (ATP-hydrolysing); EC 3.5.2.14; 100785-00-0; N-methylhydantoin amidohydrolase; methylhydantoin amidase; N-methylhydantoin hydrolase; N-methylhydantoinase; N-methylimidazolidine-2,4-dione amidohydrolase (ATP-hydrolysing). Cat No: EXWM-4497. | |
| N-Methylhydantoinase (ATP-hydrolyzing) from Arthrobacter sp., Recombinant | In enzymology, a N-methylhydantoinase (ATP-hydrolysing) is an enzyme that catalyzes the chemical reaction: ATP + N-methylimidazolidine-2,4-dione + 2 H2O rightleftharpoons ADP + phosphate + N-carbamoylsarcosine. The 3 substrates of this enzyme are ATP, N-methylimidazolidine-2,4-dione, and H2O, whereas its 3 products are ADP, phosphate, and N-carbamoylsarcosine. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. This enzyme participates in arginine, creatinine, and proline metabolism. Hydrolase for creatinine determination that uses atp to catalyze the conversion of...amoylsarcosine amidase and sarcosine oxidase. Group: Enzymes. Synonyms: N-methylimidazolidine-2,4-dione amidohydrolase (ATP-hydrolysing); N-methylhydantoin amidohydrolase; methylhydantoin amidase; N-methylhydantoin hydrolase; N-methylhydantoinase. N-Methylhydantoinase. Activity: 0.6-1.0 U/ mg. Stability: At -15 to -25°C within specification range for 12 months. Store dry. Protect from light. Appearance: White lyophilizate. Source: E. coli. Species: Arthrobacter sp. N-methylimidazolidine-2,4-dione amidohydrolase (ATP-hydrolysing); N-methylhydantoin amidohydrolase; methylhydantoin amidase; N-methylhydantoin hydrolase; N-methylhydantoinase. Cat No: NATE-0904. | |
| phenylalanine racemase (ATP-hydrolysing) | The enzyme phenylalanine racemase is the enzyme that acts on amino acids and derivatives. It activates both the L & D stereo isomers of phenylalanine to form L-phenylalanyl adenylate and D-phenylalanyl adenylate, which are bound to the enzyme. These bound compounds are then transferred to the thiol group of the enzyme followed by conversion of its configuration, the D-isomer being the more favorable configuration of the two, with a 7 to 3 ratio between the two isomers. The racemisation reaction of phenylalanine is coupled with the highly favorable hydrolysis of adenosine triphosphate (ATP) to adenosine monophosphate (AMP) and pyrophosphate (PP), thermodynamically allowing it to proceed. This reaction is then drawn forward by further hydrolyzing PP to inorganic phosphate (Pi), via Le Chatelier's principle. Group: Enzymes. Synonyms: phenylalanine racemase; phenylalanine racemase (adenosine triphosphate-hydrolysing); gramicidin S synthetase I. Enzyme Commission Number: EC 5.1.1.11. CAS No. 37290-95-2. 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-5369; phenylalanine racemase (ATP-hydrolysing); EC 5.1.1.11; 37290-95-2; phenylalanine racemase; phenylalanine racemase (adenosine triphosphate-hydrolysing); gramicidin S synthetase I. Cat No: EXWM-5369. | |
| Phosphatase from Escherichia coli, Recombinant | A phosphatase is an enzyme that removes a phosphate group from its substrate by hydrolysing phosphoric acid monoesters into a phosphate ion and a molecule with a free hydroxyl group (see dephosphorylation). This action is directly opposite to that of phosphorylases and kinases, which attach phosphate groups to their substrates by using energetic molecules like ATP. A common phosphatase in many organisms is alkaline phosphatase. Another large group of proteins present in archaea, bacteria, and eukaryote exhibits deoxyribonucleotide and ribonucleotide phosphatase or pyrophosphatase activities that catalyse the decomposition of dNTP/NTP into dNDP/NDP and a free phosphate ... phosphatase is collectively called as protein phosphatase, which removes a phosphate group from the phosphorylated amino acid residue of the substrate protein. Protein phosphorylation is a common posttranslational modification of protein catalyzed by protein kinases, and protein phosphatases reverse the effect. Group: Enzymes. Synonyms: HAD2. Enzyme Commission Number: EC 3.1.3.-. Purity: >95 % as judged by SDS-PAGE. Phosphatase. Mole weight: 26827.7 Da. Activity: 1.905 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Escherichia coli str. K-12 substr. MG1655. Phosphatase; HAD2; EC 3.1.3.-. Cat No: NATE-1226. | |
| Photinus-luciferin 4-monooxygenase (ATP-hydrolysing) | Photinus (firefly) is a bioluminescent insect. The first step in the reaction is the formation of an acid anhydride between the carboxylic group and AMP, with the release of diphosphate. The enzyme may be assayed by measurement of light emission. Group: Enzymes. Synonyms: firefly luciferase; luciferase (firefly luciferin); Photinus luciferin 4-monooxygenase (adenosine triphosphate-hydrolyzing); firefly luciferin luciferase; Photinus pyralis luciferase. Enzyme Commission Number: EC 1.13.12.7. CAS No. 61970-00-1. Luciferase. 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-0620; Photinus-luciferin 4-monooxygenase (ATP-hydrolysing); EC 1.13.12.7; 61970-00-1; firefly luciferase; luciferase (firefly luciferin); Photinus luciferin 4-monooxygenase (adenosine triphosphate-hydrolyzing); firefly luciferin luciferase; Photinus pyralis luciferase. Cat No: EXWM-0620. | |
| poly(3-hydroxyoctanoate) depolymerase | The main product after prolonged incubation is the dimer. Besides hydrolysing polymers of 3-hydroxyoctanoic acid, the enzyme also hydrolyses other polymers derived from medium-chain-length (C6-C12) hydroxyalkanoic acids and copolymers of mixtures of these. It also hydrolyses p-nitrophenyl esters of fatty acids. Polymers of short-chain-length hydroxyalkanoic acids such as poly[(R)-3-hydroxybutanoic acid] and poly[(R)-3-hydroxypentanoic acid] are not hydrolysed. Group: Enzymes. Synonyms: PHO depolymerase; poly(3HO) depolymerase; poly[(R)-hydroxyalkanoic acid] depolymerase; poly(HA) depolymerase; poly(HAMCL) depolymerase; poly[(R)-3-hydroxyoctanoate] hydrolase. Enzyme Commission Number: EC 3.1.1.76. 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-3504; poly(3-hydroxyoctanoate) depolymerase; EC 3.1.1.76; PHO depolymerase; poly(3HO) depolymerase; poly[(R)-hydroxyalkanoic acid] depolymerase; poly(HA) depolymerase; poly(HAMCL) depolymerase; poly[(R)-3-hydroxyoctanoate] hydrolase. Cat No: EXWM-3504. | |
| protein-secreting ATPase | A non-phosphorylated, non-ABC (ATP-binding cassette) ATPase that is involved in protein transport. There are several families of enzymes included here, e.g. ATP-hydrolysing enzymes of the general secretory pathway (Sec or Type II), of the virulence-related secretory pathway (Type III) and of the conjugal DNA-protein transfer pathway (Type IV). Type II enzymes occur in bacteria, archaea and eucarya, whereas type III and type IV enzymes occur in bacteria where they form components of a multi-subunit complex. Group: Enzymes. Enzyme Commission Number: EC 3.6.3.50. 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-4689; protein-secreting ATPase; EC 3.6.3.50. Cat No: EXWM-4689. | |
| protein-synthesizing GTPase | This enzyme comprises a family of proteins involved in prokaryotic as well as eukaryotic protein synthesis. In the initiation factor complex, it is IF-2b (98 kDa) that binds GTP and subsequently hydrolyses it in prokaryotes. In eukaryotes, it is eIF-2 (150 kDa) that binds GTP. In the elongation phase, the GTP-hydrolysing proteins are the EF-Tu polypeptide of the prokaryotic transfer factor (43 kDa), the eukaryotic elongation factor EF-1α (53 kDa), the prokaryotic EF-G (77 kDa), the eukaryotic EF-2 (70-110 kDa) and the signal recognition particle that play a role in endoplasmic reticulum protein synthesis (325 kDa). EF-Tu and EF-1α catalyse binding of aminoacyl-tRNA to the ribosomal A-site, while EF-G and EF-2 catalyse the translocation of peptidyl-tRNA from the A-site to the P-site. GTPase activity is also involved in polypeptide release from the ribosome with the aid of the pRFs and eRFs. Group: Enzymes. Synonyms: elongation factor (EF); initiation factor (IF); peptide-release or termination factor. Enzyme Commission Number: EC 3.6.5.3. 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-4714; protein-synthesizing GTPase; EC 3.6.5.3; elongation factor (EF); initiation factor (IF); peptide-release or termination factor. Cat No: EXWM-4714. | |
| pyrethroid hydrolase | The enzyme is involved in degradation of pyrethroid pesticides. The enzymes from Sphingobium sp., Klebsiella sp. and Aspergillus niger hydrolyse cis-permethrin at approximately equal rate to trans-permethrin. The enzyme from mouse hydrolyses trans-permethrin at a rate about 22-fold higher than cis-permethrin. Group: Enzymes. Synonyms: pyrethroid-hydrolyzing carboxylesterase; pyrethroid-hydrolysing esterase; pyrethroid-hydrolyzing esterase; pyrethroid-selective esterase; pyrethroid-cleaving enzyme; permethrinase; PytH; EstP. Enzyme Commission Number: EC 3.1.1.88. 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-3517; pyrethroid hydrolase; EC 3.1.1.88; pyrethroid-hydrolyzing carboxylesterase; pyrethroid-hydrolysing esterase; pyrethroid-hydrolyzing esterase; pyrethroid-selective esterase; pyrethroid-cleaving enzyme; permethrinase; PytH; EstP. Cat No: EXWM-3517. | |
| pyridoxal 5'-phosphate synthase (glutamine hydrolysing) | The ammonia is provided by the glutaminase subunit and channeled to the active site of the lyase subunit by a 100 ? tunnel. The enzyme can also use ribulose 5-phosphate and dihydroxyacetone phosphate. The enzyme complex is found in aerobic bacteria, archaea, fungi and plants. Group: Enzymes. Synonyms: PdxST. Enzyme Commission Number: EC 4.3.3.6. 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-5307; pyridoxal 5'-phosphate synthase (glutamine hydrolysing); EC 4.3.3.6; PdxST. Cat No: EXWM-5307. | |
| trans-feruloyl-CoA synthase | Requires Mg2+. It has not yet been established whether AMP + diphosphate or ADP + phosphate are formed in this reaction. Group: Enzymes. Synonyms: trans-feruloyl-CoA synthetase; trans-ferulate:CoASH ligase (ATP-hydrolysing); ferulate:CoASH ligase (ATP-hydrolysing). Enzyme Commission Number: EC 6.2.1.34. 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-5692; trans-feruloyl-CoA synthase; EC 6.2.1.34; trans-feruloyl-CoA synthetase; trans-ferulate:CoASH ligase (ATP-hydrolysing); ferulate:CoASH ligase (ATP-hydrolysing). Cat No: EXWM-5692. | |
| UDP-N-acetylglucosamine 2-epimerase (hydrolysing) | The enzyme is found in mammalian liver, as well as in some pathogenic bacteria including Neisseria meningitidis and Staphylococcus aureus. It catalyses the first step of sialic acid (N-acetylneuraminic acid) biosynthesis. The initial product formed is the α anomer, which rapidly mutarotates to a mixture of anomers. The mammalian enzyme is bifunctional and also catalyses EC 2.7.1.60, N-acetylmannosamine kinase.cf. EC 5.1.3.14, UDP-N-acetylglucosamine 2-epimerase (non-hydrolysing). Group: Enzymes. Synonyms: UDP-N-acetylglucosamine 2-epimerase (ambiguous); GNE (gene name); siaA (gene name); neuC (gene name). Enzyme Commission Number: EC 3.2.1.183. 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-3867; UDP-N-acetylglucosamine 2-epimerase (hydrolysing); EC 3.2.1.183; UDP-N-acetylglucosamine 2-epimerase (ambiguous); GNE (gene name); siaA (gene name); neuC (gene name). Cat No: EXWM-3867. | |
| UDP-N-acetylglucosamine 2-epimerase (non-hydrolysing) | This bacterial enzyme catalyses the reversible interconversion of UDP-GlcNAc and UDP-ManNAc. The latter is used in a variety of bacterial polysaccharide biosyntheses.cf. EC 3.2.1.183, UDP-N-acetylglucosamine 2-epimerase (hydrolysing). Group: Enzymes. Synonyms: UDP-N-acetylglucosamine 2'-epimerase (ambiguous); uridine diphosphoacetylglucosamine 2'-epimerase (ambiguous); uridine diphospho-N-acetylglucosamine 2'-epimerase (ambiguous); uridine diphosphate-N-acetylglucosamine-2'-epimerase (ambiguous); rffE (gene name); mnaA (gene name); UDP-N-acetyl-D-glucosamine 2-epimerase. Enzyme Commission Number: EC 5.1.3.14. CAS No. 9037-71-2. 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-5399; UDP-N-acetylglucosamine 2-epimerase (non-hydrolysing); EC 5.1.3.14; 9037-71-2; UDP-N-acetylglucosamine 2'-epimerase (ambiguous); uridine diphosphoacetylglucosamine 2'-epimerase (ambiguous); uridine diphospho-N-acetylglucosamine 2'-epimerase (ambiguous); uridine diphosphate-N-acetylglucosamine-2'-epimerase (ambiguous); rffE (gene name); mnaA (gene name); UDP-N-acetyl-D-glucosamine 2-epimerase. Cat No: EXWM-5399. | |
| UDP-N,N'-diacetylbacillosamine 2-epimerase (hydrolysing) | Requires Mg2+. Involved in biosynthesis of legionaminic acid, a nonulosonate derivative that is incorporated by some bacteria into assorted virulence-associated cell surface glycoconjugates. The initial product formed by the enzyme from Legionella pneumophila, which incorporates legionaminic acid into the O-antigen moiety of its lipopolysaccharide, is 2,4-diacetamido-2,4,6-trideoxy-α-D-mannopyranose, which rapidly mutarotates to a mixture of anomers. The enzyme from Campylobacter jejuni, which incorporates legionaminic acid into flagellin, prefers GDP-N,N'-diacetylbacillosamine. Group: Enzymes. Synonyms: UDP-Bac2Ac4Ac 2-epimerase; NeuC. Enzyme Commission Number: EC 3.2.1.184. 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-3868; UDP-N,N'-diacetylbacillosamine 2-epimerase (hydrolysing); EC 3.2.1.184; UDP-Bac2Ac4Ac 2-epimerase; NeuC. Cat No: EXWM-3868. | |
| uracil-DNA glycosylase | Uracil-DNA glycosylases are widespread enzymes that are found in all living organisms. EC 3.2.2.27 and double-stranded uracil-DNA glycosylase (EC 3.2.2.28) form a central part of the DNA-repair machinery since they initiate the DNA base-excision repair pathway by hydrolysing the N-glycosidic bond between uracil and the deoxyribose sugar thereby catalysing the removal of mis-incorporated uracil from DNA. Group: Enzymes. Synonyms: UdgB (ambiguous); uracil-DNA N-glycosylase; UDG (ambiguous); uracil DNA glycohydrolase. Enzyme Commission Number: EC 3.2.2.27. 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-3981; uracil-DNA glycosylase; EC 3.2.2.27; UdgB (ambiguous); uracil-DNA N-glycosylase; UDG (ambiguous); uracil DNA glycohydrolase. Cat No: EXWM-3981. | |
| urea carboxylase | A biotinyl-protein. The yeast enzyme (but not that from green algae) also catalyses the reaction of EC 3.5.1.54 allophanate hydrolase, thus bringing about the hydrolysis of urea to CO2 and NH3. Previously also listed as EC 3.5.1.45. The enzyme from the prokaryotic bacterium Oleomonas sagaranensis can also use acetamide and formamide as substrates. Group: Enzymes. Synonyms: urease (ATP-hydrolysing); urea carboxylase (hydrolysing); ATP-urea amidolyase; urea amidolyase; UALase; UCA. Enzyme Commission Number: EC 6.3.4.6. CAS No. 9058-98-4. 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-5798; urea carboxylase; EC 6.3.4.6; 9058-98-4; urease (ATP-hydrolysing); urea carboxylase (hydrolysing); ATP-urea amidolyase; urea amidolyase; UALase; UCA. Cat No: EXWM-5798. | |
| vesicle-fusing ATPase | A large family of ATP-hydrolysing enzymes involved in the heterotypic fusion of membrane vesicles with target membranes and the homotypic fusion of various membrane compartments. They belong to the AAA-type (ATPase associated with a variety of cell activities) ATPase superfamily. They include peroxin, which apparently is involved in Zellweger's syndrome. Group: Enzymes. Enzyme Commission Number: EC 3.6.4.6. 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-4708; vesicle-fusing ATPase; EC 3.6.4.6. Cat No: EXWM-4708. | |
| 1,3-Dimethylimidazolium dimethyl phosphate | 1,3-Dimethylimidazolium dimethyl phosphate is an imidazolium-based phosphoric ionic liquid that can be prepared by reacting 1-methylimidazole with trimethyl phosphate. It can also be used to produce bioethanol from sugarcane bagasse by enzymatic hydrolysis. Uses: Cas: 654058-04-5, mf: c7h15n2o4p, mw: 222.18. Group: Electrolytesbattery materials. Alternative Names: [MMIM][DMP]. CAS No. 654058-04-5. Product ID: 1,3-dimethylimidazol-1-ium; dimethyl phosphate. Molecular formula: 222.18. Mole weight: C7H15N2O4P. CN1C=C[N+](=C1)C.COP(=O)([O-])OC. 1S/C5H9N2.C2H7O4P/c1-6-3-4-7(2)5-6; 1-5-7(3, 4)6-2/h3-5H, 1-2H3; 1-2H3, (H, 3, 4)/q+1; /p-1. GSGLHYXFTXGIAQ-UHFFFAOYSA-M. ≥98.0%(HPLC). |  |
| (13E)-labda-7,13-dien-15-ol synthase | The enzyme from the lycophyte Selaginella moellendorffii is bifunctional, initially forming (13E)-labda-7,13-dien-15-yl diphosphate, which is hydrolysed to the alcohol. Group: Enzymes. Synonyms: labda-7,13E-dien-15-ol synthase. Enzyme Commission Number: EC 3.1.7.10. 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-3761; (13E)-labda-7,13-dien-15-ol synthase; EC 3.1.7.10; labda-7,13E-dien-15-ol synthase. Cat No: EXWM-3761. | |
| 1,4-lactonase | The enzyme is specific for 1,4-lactones with 4-8 carbon atoms. It does not hydrolyse simple aliphatic esters, acetylcholine, sugar lactones or substituted aliphatic lactones, e.g. 3-hydroxy-4-butyrolactone; requires Ca2+. Group: Enzymes. Synonyms: γ-lactonase. Enzyme Commission Number: EC 3.1.1.25. CAS No. 37278-38-9. 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-3450; 1,4-lactonase; EC 3.1.1.25; 37278-38-9; γ-lactonase. Cat No: EXWM-3450. | |
| 1-Chloro-1-deoxy-scyllo-inositol | 1-Chloro-1-deoxy-scyllo-inositol, a promising therapeutic candidate for the treatment of metabolic conditions like obesity and diabetes, exerts its action by suppressing the enzymatic activity of α-glucosidase, the key enzyme involved in the hydrolysis of carbohydrates into glucose, which subsequently limits the intestinal absorption of glucose, ultimately resulting in a reduced blood glucose level. Molecular formula: C6H11ClO5. Mole weight: 198.60. | |
| 1-methyladenosine nucleosidase | This enzyme belongs to the family of hydrolases, specifically those glycosylases that hydrolyse N-glycosyl compounds. The systematic name of this enzyme class is 1-methyladenosine ribohydrolase. This enzyme is also called 1-methyladenosine hydrolase. Group: Enzymes. Synonyms: 1-methyladenosine hydrolase. Enzyme Commission Number: EC 3.2.2.13. CAS No. 37367-71-8. 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-3967; 1-methyladenosine nucleosidase; EC 3.2.2.13; 37367-71-8; 1-methyladenosine hydrolase. Cat No: EXWM-3967. | |
| 20-O-multi-glycoside ginsenosidase | The 20-O-multi-glycoside ginsenosidase catalyses the hydrolysis of the 20-O-α-(1?6)-glycosidic bond and the 20-O-β-(1?6)-glycosidic bond of protopanaxadiol-type ginsenosides. The enzyme usually leaves a single glucosyl residue attached at position 20, although it can cleave the remaining glucosyl residue with a lower efficiency. Starting with a ginsenoside that is glycosylated at positions 3 and 20, such as ginsenosides Rb1, Rb2, Rb3 and Rc, the most common product is ginsenoside Rd, with a low amount of ginsenoside Rg3 also formed. Group: Enzymes. Synonyms: ginsenosidase type II (erroneous). Enzyme Commission Number: EC 3.2.1.195. 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-3879; 20-O-multi-glycoside ginsenosidase; EC 3.2.1.195; ginsenosidase type II (erroneous). Cat No: EXWM-3879. | |
| 2,3,4,6,3,4,6-Hepta-O-benzoylsucrose | 2,3,4,6,3,4,6-Hepta-O-benzoylsucrose is an efficacious glycosidase inhibitor, ubiquitously utilized in the realm of targeting metabolic maladies including diabetes. Its principal mechanism is the potent and precise suppression of enzymes tasked with the paramount function of complex sugar hydrolysis. Synonyms: 2,3,4,6-Tetra-O-benzoyl-a-D-glucopyranosyl-(1-2)-3,4,6-tri-O-benzoyl-b-D-fructopyranoside. CAS No. 309261-83-4. Molecular formula: C61H50O18. Mole weight: 1071.04. | |
| 2',3'-cyclic-nucleotide 2'-phosphodiesterase | Also hydrolyses 3'-nucleoside monophosphates and bis-4-nitrophenyl phosphate, but not 3'-deoxynucleotides. Similar reactions are carried out by EC 3.1.27.3 (ribonuclease T1) and EC 3.1.27.5 (pancreatic ribonuclease). Group: Enzymes. Synonyms: ribonucleoside 2',3'-cyclic phosphate diesterase; 2',3 -cyclic AMP phosphodiesterase; 2',3'-cyclic nucleotidase; cyclic 2',3'-nucleotide 2'-phosphodiesterase; cyclic 2',3'-nucleotide phosphodiesterase; 2',3'-cyclic nucleoside monophosphate phosphodiesterase; 2',3'-cyclic AMP 2'-phosphohydrolase; cyclic phosphodiesterase:3'-nucleotidase; 2',3'-cyclic n. Enzyme Commission Number: EC 3.1.4.16. CAS No. 9037-18-7. 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-3715; 2',3'-cyclic-nucleotide 2'-phosphodiesterase; EC 3.1.4.16; 9037-18-7; ribonucleoside 2',3'-cyclic phosphate diesterase; 2',3 -cyclic AMP phosphodiesterase; 2',3'-cyclic nucleotidase; cyclic 2',3'-nucleotide 2'-phosphodiesterase; cyclic 2',3'-nucleotide phosphodiesterase; 2',3'-cyclic nucleoside monophosphate phosphodiesterase; 2',3'-cyclic AMP 2'-phosphohydrolase; cyclic phosphodiesterase:3'-nucleotidase; 2',3'-cyclic nucleotide phosphohydrolase; 2':3'-cyclic phosphodiesterase; 2':3'-cyclic nucleotide phosphodiesterase:3'-nucleotidase. Cat No: EXWM-3715. | |
| 2',3'-cyclic-nucleotide 3'-phosphodiesterase | The brain enzyme acts on 2',3'-cyclic AMP more rapidly than on the UMP or CMP derivatives. An enzyme from liver acts on 2',3'-cyclic CMP more rapidly than on the purine derivatives; it also hydrolyses the corresponding 3',5'-cyclic phosphates, but more slowly. This latter enzyme has been called cyclic-CMP phosphodiesterase. Group: Enzymes. Synonyms: cyclic-CMP phosphodiesterase; 2',3'-cyclic AMP phosphodiesterase; cyclic 2',3'-nucleotide 3'-phosphodiesterase; cyclic 2',3'-nucleotide phosphodiesterase; 2',3'-cyclic nucleoside monophosphate phosphodiesterase; 2',3'-cyclic nucleotide 3'-phosphohydrolase; CNPase; 2',3'-cyclic nucleotide phosphohydrolase; 2':3'-cyclic nucleotide 3'-phosphod. Enzyme Commission Number: EC 3.1.4.37. CAS No. 60098-35-3. 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-3720; 2',3'-cyclic-nucleotide 3'-phosphodiesterase; EC 3.1.4.37; 60098-35-3; cyclic-CMP phosphodiesterase; 2',3'-cyclic AMP phosphodiesterase; cyclic 2',3'-nucleotide 3'-phosphodiesterase; cyclic 2',3'-nucleotide phosphodiesterase; 2',3'-cyclic nucleoside monophosphate phosphodiesterase; 2',3'-cyclic nucleotide 3'-phosphohydrolase; CNPase; 2',3'-cyclic nucleotide phosphohydrolase; 2':3'-cyclic nucleotide 3'-phosphodiesterase; 2':3'-CNMP-3'-ase. Cat No: EXWM-3720. | |
| 2,5-dioxopiperazine hydrolase | Highly specific; does not hydrolyse other dioxopiperazines, glycylglycine, proteins or barbiturates. Group: Enzymes. Synonyms: cyclo(Gly-Gly) hydrolase; cyclo(glycylglycine) hydrolase. Enzyme Commission Number: EC 3.5.2.13. CAS No. 97599-45-6. 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-4496; 2,5-dioxopiperazine hydrolase; EC 3.5.2.13; 97599-45-6; cyclo(Gly-Gly) hydrolase; cyclo(glycylglycine) hydrolase. Cat No: EXWM-4496. | |
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