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| Product | Description | |
|---|---|---|
| 1,2-β-oligomannan phosphorylase | The enzyme, originally characterized from the thermophilic anaerobic bacterium Thermoanaerobacter sp. X514, catalyses a reversible reaction. In the synthetic direction it produces oligosaccharides with a degree of polymerization (DP) of 3, 4 and 5. The phosphorolysis reaction proceeds to completion, although activity is highest when the substrate has at least three residues. cf. EC 2.4.1.339, β-1,2-mannobiose phosphorylase. Group: Enzymes. Enzyme Commission Number: EC 2.4.1.340. 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-2579; 1,2-β-oligomannan phosphorylase; EC 2.4.1.340. Cat No: EXWM-2579. |  |
| α,α-trehalose synthase | Requires Mg2+ for maximal activity. The enzyme-catalysed reaction is reversible. In the reverse direction to that shown above, the enzyme is specific for α,α-trehalose as substrate, as it cannot use α- or β-paranitrophenyl glucosides, maltose, sucrose, lactose or cellobiose. While the enzymes from the thermophilic bacterium Rubrobacter xylanophilus and the hyperthermophilic archaeon Pyrococcus horikoshii can use ADP-, UDP- and GDP-α-D-glucose to the same extent, that from the hyperthermophilic archaeon Thermococcus litoralis has a marked preference for ADP-α-D-glucose and that from the hyperthermophilic archaeon Thermoproteus tenax has a marked preference for UDP-α-D-glucose. Group: Enzymes. Synonyms: trehalose synthase; trehalose synthetase; UDP-glucose:glucose 1-glucosyltransferase; TreT; PhGT; ADP-glucose:D-glucose 1-α-D-glucosyltransferase. Enzyme Commission Number: EC 2.4.1.245. 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-2474; α,α-trehalose synthase; EC 2.4.1.245; trehalose synthase; trehalose synthetase; UDP-glucose:glucose 1-glucosyltransferase; TreT; PhGT; ADP-glucose:D-glucose 1-α-D-glucosyltransferase. Cat No: EXWM-2474. | |
| β-1,2-mannobiose phosphorylase | The enzyme, originally characterized from the thermophilic anaerobic bacterium Thermoanaerobacter sp. X514, catalyses a reversible reaction. cf. EC 2.4.1.340, 1,2-β-oligomannan phosphorylase. Group: Enzymes. Enzyme Commission Number: EC 2.4.1.339. 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-2577; β-1,2-mannobiose phosphorylase; EC 2.4.1.339. Cat No: EXWM-2577. | |
| caldariellaquinol oxidase (H+-transporting) | A copper-containing cytochrome. The enzyme from thermophilic archaea is part of the terminal oxidase and catalyses the reduction of O2 to water, accompanied by the extrusion of protons across the cytoplasmic membrane. Group: Enzymes. Synonyms: SoxABCD quinol oxidase; SoxABCD complex; quinol oxidase SoxABCD; SoxM supercomplex; aa3-type quinol oxidase; aa3 quinol oxidase; cytochrome aa3; terminal quinol oxidase; terminal quinol:oxygen oxidoreductase; caldariella quinol:dioxygen oxidoreductase; cytochrome aa3-type oxidase caldariellaquinol:O2 oxidoreductase (H+-transporting). Enzyme Commission Number: EC 7.1.1.4 (Formerly EC 1.10.3.13). Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0479; caldariellaquinol oxidase (H+-transporting); EC 1.10.3.13; SoxABCD quinol oxidase; SoxABCD complex; quinol oxidase SoxABCD; SoxM supercomplex; aa3-type quinol oxidase; aa3 quinol oxidase; cytochrome aa3; terminal quinol oxidase; terminal quinol:oxygen oxidoreductase; caldariella quinol:dioxygen oxidoreductase; cytochrome aa3-type oxidase caldariellaquinol:O2 oxidoreductase (H+-transporting). Cat No: EXWM-0479. | |
| caldopentamine synthase | The enzyme, characterized from the thermophilic archaeon Hyperthermus butylicus, can also synthesize norspermine from norspermidine and thermospermine from spermidine (with lower activity). The long-chain polyamines stabilize double-stranded DNA at high temperatures. In contrast to EC 2.5.1.23, sym-norspermidine synthase and EC 2.5.1.126, norspermine synthase, this enzyme shows no activity with propane-1,3-diamine. Group: Enzymes. Synonyms: long-chain polyamine synthase (ambiguous). Enzyme Commission Number: EC 2.5.1.127. 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-2743; caldopentamine synthase; EC 2.5.1.127; long-chain polyamine synthase (ambiguous). Cat No: EXWM-2743. | |
| D-amino-acid transaminase | A pyridoxal-phosphate protein. The enzyme from thermophilic Bacillus species acts on many D-amino acids with D-alanine and D-2-aminobutyrate as the best amino donors. It can similarly use any of several 2-oxo acids as amino acceptor, with 2-oxoglutarate and 2-oxobutyrate among the best. The enzyme from some other sources has a broader specificity. Group: Enzymes. Synonyms: D-aspartate transaminase; D-alanine aminotransferase; D-aspartic aminotransferase;D-alanine-D-glutamate transaminase; D-alanine transaminase; D-amino acid aminotransferase. Enzyme Commission Number: EC 2.6.1.21. CAS No. 37277-85-3. ALT. 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-2861; D-amino-acid transaminase; EC 2.6.1.21; 37277-85-3; D-aspartate transaminase; D-alanine aminotransferase; D-aspartic aminotransferase;D-alanine-D-glutamate transaminase; D-alanine transaminase; D-amino acid aminotransferase. Cat No: EXWM-2861. | |
| Galactose, Low Endotoxin, Low Glucose (D-Galactose) | D-Galactose is a C-4 epimer of Glucose found in milk and sugar beets as well as being synthesized by the body. Galactose is made from lactose through hydrolysis reaction under acidic conditions. Galactose is a simple monosaccharide that serves as an energy source and as an essential component of glycolipids and glycoproteins. Galactose contributes to energy metabolism via its conversion to glucose by the enzymes that constitute the Leloir pathway. Defects in the genes encoding these proteins lead to the metabolic disorder galactosemia. Applications:Used as an alternate carbon source for wild-type yeastInduces transcription of sequences fused to the GAL10 promoterSuitable for use in two-hybrid protocols. Component of galactosyltransferase labeling bufferSupplement in MRS broth for the growth of thermophilic lactobacilliInduces the expression of uncoupling protein (UCP) in yeast transformantsOral therapy for nephrotic syndrome in focal and segmental glomerulosclerosis. Group: Biochemicals. Alternative Names: D-(+)-Galactose; Dextrogalactose; Lactoglucose; alpha-Galactose(D). Grades: Molecular Biology Grade. CAS No. 59-23-4. Pack Sizes: 100g, 500g, 1Kg, 5Kg, 10Kg. Molecular Formula: C6H12O6, Molecular Weight: 180.16. US Biological Life Sciences. |  Worldwide |
| homoaconitate hydratase | Requires a [4Fe-4S] cluster for activity. The enzyme from the hyperthermophilic eubacterium Thermus thermophilus can catalyse the reaction shown above but cannot catalyse the previously described reaction, i.e. formation of (R)-homocitrate by hydration of cis-homoaconitate. The enzyme responsible for the conversion of cis-homoaconitate into (R)-homocitrate in T. thermophilus is unknown at present but the reaction can be catalysed in vitro using aconitate hydratase from pig (EC 4.2.1.3). Group: Enzymes. Synonyms: homoaconitase; cis-homoaconitase; HACN; Lys4; LysF; 2-hydroxybutane-1,2,4-tricarboxylate hydro-lyase (incorrect). Enzyme Commission Number: EC 4.2.1.36. CAS No. 9030-68-6. 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-5027; homoaconitate hydratase; EC 4.2.1.36; 9030-68-6; homoaconitase; cis-homoaconitase; HACN; Lys4; LysF; 2-hydroxybutane-1,2,4-tricarboxylate hydro-lyase (incorrect). Cat No: EXWM-5027. | |
| L-fucose isomerase | Requires a divalent metal ion (the enzyme from the bacterium Escherichia coli prefers Mn2+). The enzyme binds the closed form of the sugar and catalyses ring opening to generate a form of open-chain conformation that facilitates the isomerization reaction, which proceeds via an ene-diol mechanism. The enzyme from Escherichia coli can also convert D-arabinose to D-ribulose. The enzyme from the thermophilic bacterium Caldicellulosiruptor saccharolyticus also converts D-altrose to D-psicose and L-galactose to L-tagatose. Group: Enzymes. Enzyme Commission Number: EC 5.3.1.25. CAS No. 60063-83-4. 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-5464; L-fucose isomerase; EC 5.3.1.25; 60063-83-4. Cat No: EXWM-5464. | |
| lysine 6-dehydrogenase | The enzyme is highly specific for L-lysine as substrate, although S-(2-aminoethyl)-L-cysteine can act as a substrate, but more slowly. While the enzyme from Agrobacterium tumefaciens can use only NAD+, that from the thermophilic bacterium Geobacillus stearothermophilus can also use NADP+, but more slowly. Group: Enzymes. Synonyms: L-lysine ε-dehydrogenase; L-lysine 6-dehydrogenase; LysDH. Enzyme Commission Number: EC 1.4.1.18. CAS No. 89400-30-6. 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-1451; lysine 6-dehydrogenase; EC 1.4.1.18; 89400-30-6; L-lysine ε-dehydrogenase; L-lysine 6-dehydrogenase; LysDH. Cat No: EXWM-1451. | |
| [lysine-biosynthesis-protein LysW]-L-2-aminoadipate ligase | The enzymes from the thermophilic bacterium Thermus thermophilus and the thermophilic archaea Sulfolobus acidocaldarius and Sulfolobus tokodaii protect the amino group of L-2-aminoadipate by conjugation to the carrier protein LysW. This reaction is part of the lysine biosynthesis pathway in these organisms. Group: Enzymes. Synonyms: α-aminoadipate-lysW ligase lysX (gene name); LysX (ambiguous); AAA-LysW ligase. Enzyme Commission Number: EC 6.3.2.43. 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-5761; [lysine-biosynthesis-protein LysW]-L-2-aminoadipate ligase; EC 6.3.2.43; α-aminoadipate-lysW ligase lysX (gene name); LysX (ambiguous); AAA-LysW ligase. Cat No: EXWM-5761. | |
| N1-aminopropylagmatine ureohydrolase | The enzyme, which has been characterized from the hyperthermophilic archaeon Pyrococcus kodakarensis and the thermophilic Gram-negative bacterium Thermus thermophilus, is involved in the biosynthesis of spermidine. Group: Enzymes. Enzyme Commission Number: EC 3.5.3.24. 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-4526; N1-aminopropylagmatine ureohydrolase; EC 3.5.3.24. Cat No: EXWM-4526. | |
| N4-bis(aminopropyl)spermidine synthase | The enzyme, characterized from the thermophilic archaeon Thermococcus kodakarensis, synthesizes the branched-chain polyamine N4-bis(aminopropyl)spermidine, which is required for cell growth at high-temperature. When spermine is used as substrate, the enzyme forms N4-aminopropylspermine. Group: Enzymes. Enzyme Commission Number: EC 2.5.1.128. 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-2744; N4-bis(aminopropyl)spermidine synthase; EC 2.5.1.128. Cat No: EXWM-2744. | |
| norspermine synthase | The enzyme, characterized from the thermophilic archaeon Pyrobaculum aerophilum, can also synthesize norspermidine from propane-1,3-diamine and thermospermine from spermidine (with lower activity). The long-chain polyamines stabilize double-stranded DNA at high temperatures. In contrast to EC 2.5.1.127, caldopentamine synthase, this enzyme does not accept norspermine as a substrate. Group: Enzymes. Synonyms: long-chain polyamine synthase (ambiguous). Enzyme Commission Number: EC 2.5.1.126. 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-2742; norspermine synthase; EC 2.5.1.126; long-chain polyamine synthase (ambiguous). Cat No: EXWM-2742. | |
| nucleoside-triphosphate phosphatase | The enzyme is found in eukaryotes and thermophilic bacteria, but appears to be absent from mesophilic bacteria. Also hydrolyses nucleoside diphosphates, thiamine diphosphate and FAD. The enzyme from the plant Pisum sativum (garden pea) is regulated by calmodulin. Group: Enzymes. Synonyms: nucleoside-triphosphatase; nucleoside triphosphate phosphohydrolase; nucleoside-5-triphosphate phosphohydrolase; nucleoside 5-triphosphatase; unspecific diphosphate phosphohydrolase. Enzyme Commission Number: EC 3.6.1.15. CAS No. 9075-51-8. 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-4599; nucleoside-triphosphate phosphatase; EC 3.6.1.15; 9075-51-8; nucleoside-triphosphatase; nucleoside triphosphate phosphohydrolase; nucleoside-5-triphosphate phosphohydrolase; nucleoside 5-triphosphatase; unspecific diphosphate phosphohydrolase. Cat No: EXWM-4599. | |
| sucrose 6F-phosphate phosphorylase | The enzyme, isolated from the thermophilic bacterium Thermoanaerobacterium thermosaccharolyticum, catalyses the reversible phosphorolysis of sucrose 6F-phosphate. It also acts on sucrose with lower activity. Group: Enzymes. Synonyms: sucrose 6'-phosphate phosphorylase. Enzyme Commission Number: EC 2.4.1.329. 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-2566; sucrose 6F-phosphate phosphorylase; EC 2.4.1.329; sucrose 6'-phosphate phosphorylase. Cat No: EXWM-2566. | |
| sulfur oxygenase/reductase | This enzyme, which is found in thermophilic microorganisms, contains one mononuclear none-heme iron centre per subunit. Elemental sulfur is both the electron donor and one of the two known acceptors, the other being oxygen. Thiosulfate is also observed as a product, but is likely formed non-enzymically by a reaction between sulfite and sulfur. This enzyme differs from EC 1.13.11.18, sulfur dioxygenase and EC 1.12.98.4, sulfhydrogenase, in that both activities occur simultaneously. Group: Enzymes. Synonyms: SOR; sulfur oxygenase; sulfur oxygenase reductase. Enzyme Commission Number: EC 1.13.11.55. CAS No. 120598-92-7. 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-0574; sulfur oxygenase/reductase; EC 1.13.11.55; 120598-92-7; SOR; sulfur oxygenase; sulfur oxygenase reductase. Cat No: EXWM-0574. | |
| thermitase | A peptidase of family S8 (subtilisin family) from Thermoactinomyces vulgaris containing a single Cys, near the active site His, and inhibited by p-mercuribenzoate. The N-terminal extension of the polypeptide chain relative to subtilisin contributes to Ca2+-binding and the high thermostability. The amino acid composition and properties of the thermostable enzyme from Streptomyces rectus var. proteolyticus (formerly included in EC 3.4.21.14) are closely similar. Group: Enzymes. Synonyms: thermophilic Streptomyces serine proteinase; Thermoactinomyces vulgaris serine proteinase. Enzyme Commission Number: EC 3.4.21.66. CAS No. 69772-87-8. 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-4157; thermitase; EC 3.4.21.66; 69772-87-8; thermophilic Streptomyces serine proteinase; Thermoactinomyces vulgaris serine proteinase. Cat No: EXWM-4157. | |
| Thermitase from Bacillus cereus, Recombinant | Thermitase from Bacillus cereus is a protease that inactivates Rnases, Dnases and enzymes in reactions. Thermitase from bacillus cereus is a protease that inactivates rnases, dnases and enzymes in reactions. Applications: Thermitase is used for the isolation of rna and dna (plasmid and genomic). thermitase has been used in a study to assess the development and application of 15n-tracer substances for measuring the whole-body protein turnover rates. thermitase has also been used in a study to investigate a computational pr ocedure for transferring a binding site onto an existing protein scaffold. Group: Enzymes. Synonyms: Thermitase; thermophilic Streptomyces serine proteinase; Thermoactinomyces vulgaris serine proteinase. CAS No. 69772-87-8. Thermitase. Mole weight: mol wt 33 kDa. Activity: > 5.0 unit/mg protein. Storage: -20°C. Form: Supplied as a solution in 20mM Tris-HCl (pH 7.4), 1mM CaCl2 and 50% glycerol. Source: Bacillus cereus. Thermitase; thermophilic Streptomyces serine proteinase; Thermoactinomyces vulgaris serine proteinase. Cat No: NATE-0694. | |
| thermomycolin | A peptidase of family S8 (subtilisin family) from the thermophilic fungus Malbranchea pulchella var. sulfurea containing Cys, but not inhibited by p-mercuribenzoate. Very thermostable. Formerly included in EC 3.4.21.14. Group: Enzymes. Synonyms: thermomycolase. Enzyme Commission Number: EC 3.4.21.65. CAS No. 52233-31-5. 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-4156; thermomycolin; EC 3.4.21.65; 52233-31-5; thermomycolase. Cat No: EXWM-4156. | |
| thermopsin | From the thermophilic archaeon Sulfolobus acidocaldarius. Maximally active at pH 2 and 90 °C. Weakly inhibited by pepstatin but shows no sequence similarity to pepsin. Type example of peptidase family A5. Group: Enzymes. Enzyme Commission Number: EC 3.4.23.42. CAS No. 126125-05-1. 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-4279; thermopsin; EC 3.4.23.42; 126125-05-1. Cat No: EXWM-4279. | |
| tryptophan synthase (indole-salvaging) | Most mesophilic bacteria have a multimeric tryptophan synthase complex (EC 4.2.1.20) that forms L-tryptophan from L-serine and 1-C-(indol-3-yl)glycerol 3-phosphate via an indole intermediate. This intermediate, which is formed by the α subunits, is transferred in an internal tunnel to the β units, which convert it to tryptophan. In thermophilic organisms the high temperature enhances diffusion and causes the loss of indole. This enzyme, which does not combine with the α unit to form a complex, salvages the lost indole back to L-tryptophan. It has a much lower Km for indole than the β subunit of EC 4.2.1.20. Group: Enzymes. Synonyms: tryptophan synthase β2. Enzyme Commission Number: EC 4.2.1.122. 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-4963; tryptophan synthase (indole-salvaging); EC 4.2.1.122; tryptophan synthase β2. Cat No: EXWM-4963. | |
| 4-hydroxy-2-oxohexanoate aldolase | Requires Mn2+ for maximal activity. The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 4.1.3.39, 4-hydroxy-2-oxovalerate aldolase. The enzyme forms a bifunctional complex with EC 1.2.1.87, propanal dehydrogenase (CoA-propanoylating), with a tight channel connecting the two subunits. Group: Enzymes. Synonyms: BphI. Enzyme Commission Number: EC 4.1.3.43. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4920; 4-hydroxy-2-oxohexanoate aldolase; EC 4.1.3.43; BphI. Cat No: EXWM-4920. | |
| 4-hydroxy-2-oxovalerate aldolase | Requires Mn2+ for maximal activity. The enzyme from the bacterium Pseudomonas putida is also stimulated by NADH. In some bacterial species the enzyme forms a bifunctional complex with EC 1.2.1.10, acetaldehyde dehydrogenase (acetylating). The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 4.1.3.43, 4-hydroxy-2-oxohexanoate aldolase. Group: Enzymes. Synonyms: 4-hydroxy-2-ketovalerate aldolase; HOA; DmpG; 4-hydroxy-2-oxovalerate pyruvate-lyase; 4-hydroxy-2-oxopentanoate pyruvate-lyase; BphI; 4-hydroxy-2-oxopentanoate pyruvate-lyase (acetaldehyde-forming). Enzyme Commission Number: EC 4.1.3.39. CAS No. 37325-52-3. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4915; 4-hydroxy-2-oxovalerate aldolase; EC 4.1.3.39; 37325-52-3; 4-hydroxy-2-ketovalerate aldolase; HOA; DmpG; 4-hydroxy-2-oxovalerate pyruvate-lyase; 4-hydroxy-2-oxopentanoate pyruvate-lyase; BphI; 4-hydroxy-2-oxopentanoate pyruvate-lyase (acetaldehyde-forming). Cat No: EXWM-4915. | |
| 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. | |
| aqualysin 1 | This enzyme from the extreme thermophile, Thermus aquaticus, is an alkaline serine peptidase. It has three subsites, S1, S2, and S3, in the substrate binding site. The preferred amino acids at the S1 site are Ala and Phe, at the S2 site are Ala and norleucine and at the S3 site are Phe and Ile. These specificities are similar to those of EC 3.4.21.64 (peptidase K) and EC 3.4.21.62 (subtilisin BPN'). The enzyme displays broad specificity for cleavage of insulin B-chain and hydrolyses elastin substrates such as succinyl-(Ala)n-p-nitroanilide (n = 1,2,3) and some peptide esters. Belongs in peptidase family S8A. Group: Enzymes. Synonyms: caldolysin. Enzyme Commission Number: EC 3.4.21.111. CAS No. 88747-68-6. 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-4106; aqualysin 1; EC 3.4.21.111; 88747-68-6; caldolysin. Cat No: EXWM-4106. | |
| 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. | |
| 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. | |
| BCL I | BCL I. Uses: Designed for use in research and industrial production. Additional or Alternative Names: RESTRICTION ENDONUCLEASES BCL I;FBA I;BCL I;BCL I RESTRICTION ENZYME;restriction endonuclease bcl I from*bacillus cald;RESTRICTION ENDONUCLEASE BCL I FROM*BACI LLUS CALDOL;BCL I 5'.T/GATCA.3' FROM THE THERMOPHILE BACILLUS CALDOLYTICUS SOLUTION IN 50%. Product Category: Heterocyclic Organic Compound. CAS No. 81295-11-6. Purity: 0.96. Product ID: ACM81295116. Alfa Chemistry ISO 9001:2015 Certified. Categories: BC Lions. |  |
| β-Glucosidase 1A from Thermus thermophilus, Recombinant | Beta-glucosidase is a glucosidase enzyme that acts upon β1->4 bonds linking two glucose or glucose-substituted molecules (i.e., the disaccharide cellobiose). It is one of the cellulases, enzymes involved in the decomposition of cellulose and related polysaccharides; more specifically, an exocellulase with specificity for a variety of beta-D-glycoside substrates. It catalyzes the hydrolysis of terminal non-reducing residues in beta-D-glucosides with release of glucose. Group: Enzymes. Synonyms: EC 3.2.1.21; gentiobiase; cellobiase; emulsin; elaterase; aryl-beta-glucosidase; beta-D-glucosidase; beta-glucoside glucohydrolase; arbutinase; . Enzyme Commission Number: EC 3.2.1.21. CAS No. 9001-22-3. Purity: >90% by SDS-PAGE. β-Glucosidase. Mole weight: 50.7 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Thermus thermophilus. EC 3.2.1.21; gentiobiase; cellobiase; emulsin; elaterase; aryl-beta-glucosidase; beta-D-glucosidase; beta-glucoside glucohydrolase; arbutinase; amygdalinase; p-nitrophenyl beta-glucosidase; primeverosidase; amygdalase; linamarase; salicilinase; beta-1,6-glucosidase; β-Glucosidase 1A. Cat No: NATE-1431. | |
| cholesterol 7-desaturase | The enzyme, characterized from several organisms including the worm Caenorhabditis elegans, the fly Drosophila melanogaster, and the ciliate Tetrahymena thermophila, is a Rieske oxygenase. In insects it participates in the the biosythesis of ecdysteroid hormones. The electrons are transferred from NAD(P)H via an electron transfer chain likely to include ferredoxin reductase and ferredoxin. The enzyme differs from regular desaturases, such as EC 1.14.19.20, 7-sterol 5(6)-desaturase, which are cytochrome b5-dependent and contain the three His-boxes that are typical to most desaturases. Group: Enzymes. Synonyms: nvd (gene name); daf-36 (gene name). Enzyme Commission Number: EC 1.14.19.21. 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-0984; cholesterol 7-desaturase; EC 1.14.19.21; nvd (gene name); daf-36 (gene name). Cat No: EXWM-0984. | |
| coccolysin | A 30 kDa endopeptidase found intracellularly in S. thermophilus and S. diacetilactis and in the medium of S. faecalis. In peptidase family M4 (thermolysin family). Formerly included in EC 3.4.24.4. Group: Enzymes. Synonyms: Streptococcus thermophilus intracellular proteinase; EM 19000. Enzyme Commission Number: EC 3.4.24.30. CAS No. 156859-08-4. 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-4312; coccolysin; EC 3.4.24.30; 156859-08-4; Streptococcus thermophilus intracellular proteinase; EM 19000. Cat No: EXWM-4312. | |
| DVS Beverage Starter Cultures | There are two main lactic acid bacteria used in making homemade and catering yogurt. Usually L. bulgaricus and S. thermophilus are added at a ratio of 1:1. Other types have additional strains of bacteria, which affect the taste and potential health benefits of the curd. Group: Others. Synonyms: DVS Beverage Starter Cultures. DVS Beverage Starter Cultures. Cat No: PRBT-010. | |
| Glutamate Dehydrogenase from Thermophilic Bacterium, recombinant | GDH is an oxidoreductase enzyme which relates carbon and nitrogen metabolism. It catalyzes the reduction of α-ketoglutarate and ammonia to L-glutamate and vice versa. This enzyme is a robust and ideal candidate for research use, and industrial applications in the diagnostics and food industries. Group: Enzymes. Synonyms: glutamate dehydrogenase; glutamic dehydrogenase; glutamate dehydrogenase (NAD+); glutamate oxidoreductase; glutamic acid dehydrogenase; L-glutamate dehydrogenase; NAD+-dependent glutamate dehydrogenase; NAD+-dependent glutamic dehyd. Enzyme Commission Number: EC 1.4.1.2. CAS No. 9001-46-1. GLDH. Mole weight: 270 kDa; Homohexameric ( 45 kDa per subunit). Activity: > 90 U/mg protein. Storage: at -20 °C. Form: Lyophilized powder. Source: E. coli. Species: Thermophilic Bacterium. glutamate dehydrogenase; glutamic dehydrogenase; glutamate dehydrogenase (NAD+); glutamate oxidoreductase; glutamic acid dehydrogenase; L-glutamate dehydrogenase; NAD+-dependent glutamate dehydrogenase; NAD+-dependent glutamic dehydrogenase; NAD+-glutamate dehydrogenase; NAD+-linked glutamate dehydrogenase; NAD+-linked glutamic dehydrogenase; NAD+-specific glutamic dehydrogenase; NAD+-specific glutamate dehydrogenase; NAD+:glutamate oxidoreductase; NADH-linked glutamate dehydrogenase; GLDH; EC 1.4.1.2. Cat No: NATE-1701. | |
| Lactobacillus Acidophilus Freeze Dried Powder | Lactobacillus acidophilus (New Latin 'acid-loving milk-bacillus') is a species of gram positive bacteria in the genus Lactobacillus. L. acidophilus is a homofermentative, microaerophilic species, fermenting sugars into lactic acid, and grows readily at rather low pH values (below pH 5.0) and has an optimum growth temperature of around 37 °C (99 °F). L. acidophilus occurs naturally in the human and animal gastrointestinal tract and mouth. Some strains of L. acidophilus may be considered to have probiotic characteristics. These strains are commercially used in many dairy products, sometimes together with Streptococcus thermophilus and Lactobacillus delbrueckii subsp. bulgaricus in the production of acidophilus-type yogurt, or acidophiline. Group: Probiotics. Synonyms: Lactobacillus Acidophilus Freeze-Drying Powder; Lactobacillus Acidophilus. Activity: 10 billion CFU/g or more. Stability: 24 Months. Appearance: White To Light Yellow-Colored, Free-Flowing Powder. Storage: Recommend storage at refrigeration (4 °C) or frozen temperature (-18 °C) in original, sealed package until processed. Form: Powder. Anti Helicobacter Pylori Formula, Antiallergic Formula, Female Vaginal Health Formula, Weight Control Formula. Cat No: PRBT-012. | |
| Lactobacillus Delbrueckii Subsp. Bulgaricus | Lactobacillus delbrueckii subsp. bulgaricus is commonly used alongside Streptococcus thermophilus as a starter for making yogurt. Properties: 1. Lactobacillus Delbrueckii Subsp. Bulgaricus; 2. L. D. Bulgaricus Produces Acetaldehyde; 3. Lactobacillus Bulgaricus Temperature Range. It's a gram-positive rod that may appear long and filamentous. it's non-motile anddoes not form spores. Applications: O dietary supplements - capsules, powder, tablets, granule; o food - bars, powdered beverages. Group: Others. Synonyms: Lactobacillus Delbrueckii Subsp. Bulgaricus; Lactobacillus Delbrueckii. Purity: >90%. Activity: o 50 billion (5.00E+10) CFU/gm; o Overage provided. Stability: 24 Months. Appearance: White To Light Yellow-Colored, Free-Flowing Powder. Storage: Recommend storage at refrigeration (4 °C) or frozen temperature (-18 °C) in original, sealed package until processed. Lactobacillus Delbrueckii Subsp. Bulgaricus; Lactobacillus Delbrueckii. Cat No: PRBT-017. | |
| L-fuculose-1-phosphate aldolase from Thermus thermophilus HB8, Recombinant | In enzymology, a L-fuculose-phosphate aldolase (EC 4.1.2.17) is an enzyme that catalyzes the chemical reaction: L-fuculose-1-phosphate ? glycerone phosphate + (S)-lactaldehyde. Hence, this enzyme has one substrate, L-fuculose-1-phosphate, and two products, glycerone phosphate and (S)-lactaldehyde. This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. Group: Enzymes. Synonyms: L-fuculose-1-phosphate (S)-lactaldehyde-lyase (glycerone-phosphate-forming); L-fuculose 1-phosphate aldolase; fuculose aldolase; L-fuculose-1-phosphate lactaldehyde-lyase; L-fuculose-phosphate aldolase; EC 4.1.2.17. Enzyme Commission Number: EC 4.1.2.17. CAS No. 9024-54-8. Purity: min 95% by SDS-PAGE. L-fuculose-phosphate aldolase. Source: E. coli. Species: Thermus thermophilus HB8. L-fuculose-1-phosphate (S)-lactaldehyde-lyase (glycerone-phosphate-forming); L-fuculose 1-phosphate aldolase; fuculose aldolase; L-fuculose-1-phosphate lactaldehyde-lyase; L-fuculose-phosphate aldolase; EC 4.1.2.17. Cat No: NATE-1502. | |
| N1-aminopropylagmatine synthase | The enzyme is involved in the biosynthesis of spermidine from agmatine in some archaea and bacteria. The enzyme from the Gram-negative bacterium Thermus thermophilus accepts agmatine, spermidine and norspermidine with similar catalytic efficiency. The enzymes from the archaea Pyrococcus furiosus and Thermococcus kodakarensis prefer agmatine, but can utilize cadaverine, putrescine and propane-1,3-diamine with much lower catalytic efficiency. cf. EC 2.5.1.16, spermidine synthase, and EC 2.5.1.23, sym-norspermidine synthase. Group: Enzymes. Synonyms: agmatine/cadaverine aminopropyl transferase; ACAPT; PF0127 (gene name); triamine/agmatine aminopropyltransferase; SpeE; agmatine aminopropyltransferase. Enzyme Commission Number: EC 2.5.1.104. 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-2720; N1-aminopropylagmatine synthase; EC 2.5.1.104; agmatine/cadaverine aminopropyl transferase; ACAPT; PF0127 (gene name); triamine/agmatine aminopropyltransferase; SpeE; agmatine aminopropyltransferase. Cat No: EXWM-2720. | |
| NAD(P)H oxidase (H2O-forming) | A flavoprotein (FAD). NADPH is a better substrate than NADH. By removal of oxygen the enzyme is involved in aerobic tolerance in the thermophilic anaerobic archaeon Thermococcus profundus and in Giardia intestinalis, a microaerophilic single-celled parasite of the order Diplomonadida. Group: Enzymes. Enzyme Commission Number: EC 1.6.3.2. 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-1584; NAD(P)H oxidase (H2O-forming); EC 1.6.3.2. Cat No: EXWM-1584. | |
| Native Fructose-bisphosphate aldolase from Thermophillic bacteria | Fructose-bisphosphate aldolase (EC 4.1.2.13), often just aldolase, is an enzyme catalyzing a reversible reaction that splits the aldol, fructose 1,6-bisphosphate, into the triose phosphates dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (G3P). Aldolase can also produce DHAP from other (3S,4R)-ketose 1-phosphates such as fructose 1-phosphate and sedoheptulose 1,7-bisphosphate. Gluconeogenesis and the Calvin cycle, which are anabolic pathways, use the reverse reaction. Glycolysis, a catabolic pathway, uses the forward reaction. Aldolase is divided into two classes by mechanism. Applications: Carbon bond formation between dihydroxyacetone phosphate and linear aldehydes. Group: Enzymes. Synonyms: aldolase; fructose-1,6-bisphosphate triosephosphate-lyase; Fructose-bisphosphate aldolase; fructose diphosphate aldolase; D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase; EC 4.1.2.13; 9024-52-6. Enzyme Commission Number: EC 4.1.2.13. CAS No. 9024-52-6. Aldolase. Storage: Store at -20°C. Form: Frozen liquid. Source: Thermophillic bacteria. aldolase; fructose-1,6-bisphosphate triosephosphate-lyase; Fructose-bisphosphate aldolase; fructose diphosphate aldolase; D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase; EC 4.1.2.13; 9024-52-6. Cat No: NATE-1152. | |
| Native Lactate Dehydrogenase from Thermophillic bacteria | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: Diagnostic test and biosensors; nadh recycling. this enzyme is a potential candidate for biocatalysis, suitable for pharmaceutical development / manufacturing. Group: Enzymes. Synonyms: Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Storage: Store at -20°C. Form: Frozen Liquid. Source: Thermophillic bacteria. Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Cat No: DIA-400. | |
| Native Malate dehydrogenase (Decarboxylating) from Thermophillic bacteria | Malate dehydrogenase is an enzyme in the citric acid cycle that catalyzes the conversion of malate into oxaloacetate (using NAD+) and vice versa (this is a reversible reaction). Malate dehydrogenase is not to be confused with malic enzyme, which catalyzes the conversion of malate to pyruvate producing NADPH. Malate dehydrogenase is also involved in gluconeogenesis, the synthesis of glucose from smaller molecules. Pyruvate in the mitochondria is acted upon by pyruvate carboxylase to form oxaloacetate, a citric acid cycle intermediate. In order to get the oxaloacetate out of the mitochondria, malate dehydrogenase reduces it to malate, and it then traverses ...; malate NAD dehydrogenase; NAD-dependent malate dehydrogenase; NAD-sp; ECific malate dehydrogenase; NAD-linked malate dehydrogenase; MDH; L-malate-NAD+ oxidoreductase; S-malate: NAD+ oxidoreductase; EC 1.1.1.38; Malate Dehydrogenase. Enzyme Commission Number: EC 1.1.1.38. CAS No. 9080-52-8. MDH. Storage: Store at -20°C. Form: Frozen Liquid. Source: Thermophillic bacteria. malic dehydrogenase; L-malate dehydrogenase; NAD-L-malate dehydrogenase; malic acid dehydrogenase; NAD-dependent malic dehydrogenase; NAD-malate dehydrogenase; NAD-malic dehydrogenase; malate NAD dehydrogenase; NAD-dependent malate dehydrogenase; NAD-sp; ECific malate dehydrogenase; NAD- | |
| Native Malate dehydrogenase from Thermophillic bacteria | Malate dehydrogenase is an enzyme in the citric acid cycle that catalyzes the conversion of malate into oxaloacetate (using NAD+) and vice versa (this is a reversible reaction). Malate dehydrogenase is not to be confused with malic enzyme, which catalyzes the conversion of malate to pyruvate producing NADPH. Malate dehydrogenase is also involved in gluconeogenesis, the synthesis of glucose from smaller molecules. Pyruvate in the mitochondria is acted upon by pyruvate carboxylase to form oxaloacetate, a citric acid cycle intermediate. In order to get the oxaloacetate out of the mitochondria, malate dehydrogenase reduces it to malate, and it then traverses the inner...e dehydrogenase; NAD-sp; ECific malate dehydrogenase; NAD-linked malate dehydrogenase; MDH; L-malate-NAD+ oxidoreductase; S-malate: NAD+ oxidoreductase; EC 1.1.1.37; Malate Dehydrogenase. Enzyme Commission Number: EC 1.1.1.37. CAS No. 9001-64-3. MDH. Storage: Store at -20°C. Form: Frozen Liquid. Source: Thermophillic bacteria. malic dehydrogenase; L-malate dehydrogenase; NAD-L-malate dehydrogenase; malic acid dehydrogenase; NAD-dependent malic dehydrogenase; NAD-malate dehydrogenase; NAD-malic dehydrogenase; malate NAD dehydrogenase; NAD-dependent malate dehydrogenase; NAD-sp; ECific malate dehydrogenase; NAD-linked malate dehydrogenase; MDH; L-malate-NAD+ oxidored | |
| Native Phosphofructokinase from Thermophillic bacteria | Phosphofructokinase is a kinase enzyme that phosphorylates fructose 6-phosphate in glycolysis. The enzyme-catalysed transfer of a phosphoryl group from ATP is an important reaction in a wide variety of biological processes. One enzyme that utilizes this reaction is phosphofructokinase (PFK), which catalyses the phosphorylation of fructose-6-phosphate to fructose-1,6-bisphosphate, a key regulatory step in the glycolytic pathway. PFK exists as a homotetramer in bacteria and mammals (where each monomer possesses 2 similar domains) and as an octomer in yeast (where there are 4 alpha-(PFK1) and 4 beta-chains (PFK2), the latter, like the mammalian monomers, possessing 2 similar domains). This protein may use the morpheein model of allosteric regulation. Applications: Diagnostic tests. Group: Enzymes. Synonyms: PFKWII; EC 2.7.1.11; PFK; phosphofructokinase; 6-phosphofructokinase; Phosphofructokinase I; Phosphohexokinase. Enzyme Commission Number: EC 2.7.1.11. CAS No. 9001-80-3. PFK. Storage: Store at -20°C. Form: Frozen Liquid. Source: Thermophillic bacteria. PFKWII; EC 2.7.1.11; PFK; phosphofructokinase; 6-phosphofructokinase; Phosphofructokinase I; Phosphohexokinase. Cat No: DIA-403. | |
| Native Pyruvate decarboxylase from Thermophillic bacteria | Pyruvate decarboxylase (PDC) is a homotetrameric enzyme that catalyses the decarboxylation of pyruvic acid to acetaldehyde and carbon dioxide in the cytoplasm. Pyruvate decarboxylase depends on cofactors thiamine pyrophosphate (TPP) and magnesium. PDC contains a β-α-β structure, yielding parallel β-sheets. Applications: C-c bond formation: ligation of two aldehyde molecules enantioselectively to 2-hydroxy ketones; preparation of (r)-phenylacetylcarbinol (pac). Group: Enzymes. Synonyms: Pyruvate decarboxylase; EC 4.1.1.1; α-carboxylase (ambiguous); pyruvic decarboxylase; α-ketoacid carboxylase; 2-oxo-acid carboxy-lyase; 9001-04-1; 2-Oxo-acid carboxy-lyase; PDC. Enzyme Commission Number: EC 4.1.1.1. CAS No. 9001-4-1. PDC. Storage: Store at -20°C. Form: Frozen Liquid. Source: Thermophillic bacteria. Pyruvate decarboxylase; EC 4.1.1.1; α-carboxylase (ambiguous); pyruvic decarboxylase; α-ketoacid carboxylase; 2-oxo-acid carboxy-lyase; 9001-04-1; 2-Oxo-acid carboxy-lyase; PDC. Cat No: NATE-1159. | |
| Native Pyruvate Kinase from Thermophillic bacteria | Pyruvate kinase is an enzyme involved in glycolysis. It catalyzes the transfer of a phosphate group from phosphoenolpyruvate (PEP) to ADP, yielding one molecule of pyruvate and one molecule of ATP. Applications: Atp regeneration in biocatalysis. Group: Enzymes. Synonyms: Pyruvate kinase; EC 2.7.1.40; 9001-59-6; phosphoenolpyruvate kinase; phosphoenol transphosphorylase; pyruvate kinase (phosphorylating); fluorokinase; fluorokinase (phosphorylating); pyruvic kinase; pyruvate phosphotransferase; ATP:pyruvate 2-O-phosphotransferase. Enzyme Commission Number: EC 2.7.1.40. CAS No. 9001-59-6. Pyruvate Kinase. Storage: Store at -20°C. Form: Frozen Liquid. Source: Thermophillic bacteria. Pyruvate kinase; EC 2.7.1.40; 9001-59-6; phosphoenolpyruvate kinase; phosphoenol transphosphorylase; pyruvate kinase (phosphorylating); fluorokinase; fluorokinase (phosphorylating); pyruvic kinase; pyruvate phosphotransferase; ATP:pyruvate 2-O-phosphotransferase. Cat No: NATE-1158. | |
| Native Streptococcus thermophilus Glycerol 3-phosphate Oxidase | In enzymology, a glycerol-3-phosphate oxidase (EC 1.1.3.21) is an enzyme that catalyzes the chemical reaction:sn-glycerol 3-phosphate + O2<-> glycerone phosphate + H2O2. Thus, the two substrates of this enzyme are sn-glycerol 3-phosphate and O2, whereas its two products are glycerone phosphate and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. This enzyme participates in glycerophospholipid metabolism. It employs one cofactor, FAD. Applications: Gpo has been used for sensitive metabolite assays of starch and lipid synthesis, pyrophosphate, atp, adp, and most glycolytic i...3-phosphate Oxidase; 9046-28-0; sn-Glycerol 3-phosphate:oxygen 2-oxidoreductase; L-Glycerol 3-phosphate Oxidase; GPO. Enzyme Commission Number: EC 1.1.3.21. CAS No. 9046-28-0. Glycerol-3-phosphate oxidase. Activity: > 35 units/mg solid. Storage: -20°C. Form: lyophilized powder. Source: Streptococcus thermophilus. EC 1.1.3.21; glycerol phosphate oxidase; glycerol-1-phosphate oxidase; glycerol phosphate oxidase; L-α-glycerophosphate oxidase; α-glycerophosphate oxidase; L-α-glycerol-3-phosphate oxidase; Glycerol 3-phosphate Oxidase; 9046-28-0; sn-Glycerol 3-phosphate:oxygen 2-oxidoreductase; L-Glycerol 3-phosphate Oxidase; GPO. Cat No: NATE-0316. | |
| Native Thermus thermophilus Lipase | Triacylglycerol lipase is an enzyme with system name triacylglycerol acylhydrolase. This enzyme catalyses the following chemical reaction:triacylglycerol + H2O<-> diacylglycerol + a carboxylate. The product is a crude preparation containing a mixture of intracellular lipases and is supplied as a lyophilized powder. Group: Enzymes. Synonyms: Triacylglycerol acylhydrolase; Triacylglycerol lipase. Enzyme Commission Number: EC 3.1.1.3. CAS No. 9001-62-1. Lipase. Activity: >3.0 units/g. Stability: 2 years. Storage: 2-8°C. Form: Lyophilized powder. Source: Thermus thermophilus. EC 3.1.1.3; lipase; triglyceride lipase; tributyrase; butyrinase; glycerol ester hydrolase; tributyrinase; Tween hydrolase; steapsin; triacetinase; tributyrin esterase; Tweenase; amno N-AP; Takedo 1969-4-9; Meito MY 30; Tweenesterase; GA 56; capalase L; triglyceride hydrolase; triolein hydrolase; tween-hydrolyzing esterase; amano CE; cacordase; triglyceridase; triacylglycerol ester hydrolase; amano P; amano AP; PPL; glycerol-ester hydrolase; GEH; meito Sangyo OF lipase; hepatic lipase; lipazin; post-heparin plasma protamine-resistant lipase; salt-resistant post-heparin lipase; heparin releasable hepatic lipase; amano CES; amano B; tributyrase; triglyceride lipase; liver lipase; hepatic monoacylglycerol acyltransferase; 9001-62-1. Cat No: NATE-1613. | |
| Native Transketolase from Thermophillic bacteria | Transketolase is highly specific for ketol donor substrates and is stereospecific and enantioselective to hydroxyaldehyde substrates with an (R) configuration. It specifically catalyzes the irreversible transfer of one ketol unit from α-hydroxypyruvic acid to an aldehyde to produce a D-threo (3S,4R)ketose. Applications: This enzyme is a potential candidate for biocatalysis, suitable for pharmaceutical development / manufacturing. asymmetric c-c bond formation, ketol donor d-xylulose-5-phosphate may be substituted by hydroxypyruvate; preparation of ketose sugars such as fructose analogs, azasugars and fluorogenic substrates. Group: Enzymes. Synonyms: Transketolase; EC 2.2.1.1; 9014-48-6; glycolaldehydetransferase; Glycolaldehyde Transferase. Enzyme Commission Number: EC 2.2.1.1. CAS No. 9014-48-6. Transketolase. Storage: Store at -20°C. Form: Frozen Liquid. Source: Thermophillic bacteria. Transketolase; EC 2.2.1.1; 9014-48-6; glycolaldehydetransferase; Glycolaldehyde Transferase. Cat No: NATE-1162. | |
| Probiotics Blend for Antiallergic | Probiotics Blend of L. Reuteri, L. Salivarius, L. Paracasei, L. Acidophilus, L. Rhamnosus and S. Thermophilus. Group: Probiotics. Activity: 10 billion CFU/g or more. Stability: 24 Months. Appearance: White To Light Yellow-Colored, Free-Flowing Powder. Storage: Recommend storage at refrigeration (4 °C) or frozen temperature (-18 °C) in original, sealed package until processed. Form: Powder. Antiallergic Formula. Cat No: PBAF-006. | |
| propanal dehydrogenase (CoA-propanoylating) | The enzyme forms a bifunctional complex with EC 4.1.3.43, 4-hydroxy-2-oxohexanoate aldolase, with a tight channel connecting the two subunits. Also acts, more slowly, on glycolaldehyde and butanal. In Pseudomonas species the 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 1.2.1.10, acetaldehyde dehydrogenase (acetylating). NADP+ can replace NAD+ with a much slower rate. Group: Enzymes. Synonyms: BphJ. Enzyme Commission Number: EC 1.2.1.87. 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-1190; propanal dehydrogenase (CoA-propanoylating); EC 1.2.1.87; BphJ. Cat No: EXWM-1190. | |
| Recombinant Adenine phosphoribosyltransferase from Thermus thermophilus | Adenine phosphoribosyltransferase is widely spread in nature, it is produced in bacteria and eukaryotes, participates in the alternative de novo synthesis of purine nucleotides. Group: Enzymes. Synonyms: EC 2.4.2.7; APRT. Enzyme Commission Number: EC 2.4.2.7. CAS No. 9027-80-9. Purity: > 80 %. APRT. Mole weight: 19 kDa. Appearance: Colourless clear liquid. Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C. Source: E. coli. Species: Thermus thermophilus. EC 2.4.2.7; APRT; Adenine phosphoribosyltransferase. Cat No: NATE-1005. | |
| Recombinant Phosphoribosylpyrophosphate synthetase from Thermus thermophilus | Phosphoribosylpyrophosphate (PRPP) synthetase participates in the biosynthesis in bacteria of purine nucleotides, pyrimidine nucleotides, tryptophan, histidine, and the pyridine nucleotide coenzymes. Group: Enzymes. Synonyms: PRPP synthetase. CAS No. 9031-46-3. Purity: > 80 %. PRPP synthetase. Mole weight: 32 kDa. Appearance: Colourless clear liquid. Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C. Source: E. coli. Species: Thermus thermophilus. PRPP synthetase; Phosphoribosyl pyrophosphate synthetase. Cat No: NATE-1008. | |
| Streptococcus Thermophilus Freeze Dried Powder | Streptococcus thermophilus also known as Streptococcus salivarius subsp. thermophilus is a gram-positive bacterium, and a fermentative facultative anaerobe, of the viridans group. It tests negative for cytochrome, oxidase, and catalase, and positive for alpha-hemolytic activity. It is non-motile and does not form endospores. Group: Probiotics. Synonyms: Streptococcus Thermophilus Probiotics Powder; Streptococcus Thermophilus. Activity: 10 billion CFU/g or more. Stability: 24 Months. Appearance: White To Light Yellow-Colored, Free-Flowing Powder. Storage: Recommend storage at refrigeration (4 °C) or frozen temperature (-18 °C) in original, sealed package until processed. Form: Powder. Antiallergic Formula. Cat No: PRBT-029. | |
| Streptococcus Thermophilus Probiotics Powder | Streptococcus Thermophilus Probiotics Powder have maintained a stable growth rate in children. Children who received S. thermophilus supplements had better growth during a 6-month period than children who did not receive the supplement. S. thermophilus breaks down the pyruvateinto lactic acid and acetaldehyde and the bacterium is healthy for the hostorganism that consumes it and combines this microbe with the rest of itsinternal flora. Gram-positivebacteria and a homofermentative facultative anaerobe. Applications: Streptococcusthermophilus isusually used in the production of milk, cheese, and other dairy products. Group: Others. Synonyms: Streptococcus Thermophilus Probiotics Powder; Streptococcus Thermophilus. Purity: >90%. Activity: o 300 billion (3.00E+11) CFU/gm o Overage provided. Stability: 24 Months. Appearance: White To Light Yellow-Colored, Free-Flowing Powder. Streptococcus Thermophilus Probiotics Powder; Streptococcus Thermophilus. Cat No: PRBT-029. | |
| Trehalose-phosphatase from Thermus thermophilus, Recombinant | In enzymology, a trehalose-phosphatase (EC 3.1.3.12) is an enzyme that catalyzes the chemical reaction: alpha,alpha-trehalose 6-phosphate + H2O <-> alpha,alpha-trehalose + phosphate. Thus, the two substrates of this enzyme are alpha,alpha'-trehalose 6-phosphate and H2O, whereas its two products are alpha,alpha-trehalose and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. Group: Enzymes. Synonyms: Trehalose 6-phosphatase; trehalose 6-phosphate phosphatase; trehalose-6-phosphate phosphohydrolase; TPP; T6PP. Enzyme Commission Number: EC 3.1.3.12. CAS No. 9025-72-3. Purity: >95 % as judged by SDS-PAGE. T6PP. Mole weight: 27788.9 Da. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Thermus thermophilus HB8. Trehalose 6-phosphatase; trehalose 6-phosphate phosphatase; trehalose-6-phosphate phosphohydrolase; TPP; T6PP. Cat No: NATE-1233. | |
| tryptophan synthase | A pyridoxal-phosphate protein. The α-subunit catalyses the conversion of 1-C-(indol-3-yl)glycerol 3-phosphate to indole and D-glyceraldehyde 3-phosphate (this reaction was included formerly under EC 4.1.2.8). The indole migrates to the β-subunit where, in the presence of pyridoxal 5'-phosphate, it is combined with L-serine to form L-tryptophan. In some organisms this enzyme is part of a multifunctional protein that also includes one or more of the enzymes EC 2.4.2.18 (anthranilate phosphoribosyltransferase), EC 4.1.1.48 (indole-3-glycerol-phosphate synthase), EC 4.1.3.27 (anthranilate synthase) and EC 5.3.1.24 (phosphoribosylanthranilate isomerase). In thermophilic organ...indoleglycerol-phosphate); L-serine hydro-lyase [adding 1-C-(indol-3-yl)glycerol 3-phosphate, L-tryptophan and glyceraldehyde-3-phosphate-forming]. Enzyme Commission Number: EC 4.2.1.20. CAS No. 9014-52-2. 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-5014; tryptophan synthase; EC 4.2.1.20; 9014-52-2; L-tryptophan synthetase; indoleglycerol phosphate aldolase; tryptophan desmolase; tryptophan synthetase; L-serine hydro-lyase (adding indoleglycerol-phosphate); L-serine hydro-lyase [adding 1-C-(indol-3-yl)glycerol 3-phosphate, L-tryptophan and glyceraldehyde-3-phosphate-forming]. Cat No: EXWM-5014. | |
| Tth111 I | One unit of the enzyme is the amount required to hydrolyze 1 μg of Lambda DNA (HindIII-digest) in 1 hour at 65°C in a total reaction volume of 50 μl. Applications: After 2-fold overdigestion with enzyme 10% of the dna fragments can be ligated. Group: Restriction Enzymes. Purity: 400U; 2000U. GACN↑NNGTC CTGNN↓NCAG. Activity: 5000u.a./ml. Appearance: 10 X SE-buffer Y. Storage: -20°C. Form: Liquid. Source: An E.coli strain, that carries the cloned gene Tth111I from Thermus Thermophilus 111. Pack: 10 mM Tris-HCl (pH 7.5); 500 mM NaCl; 0,1 mM EDTA; 1 mM DTT; 50% glycerol. Cat No: ET-1185RE. | |
| UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase | A pyridoxal 5'-phosphate protein. This enzyme participates in the biosynthetic pathway for UDP-α-D-ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-α-D-mannuronic acid), an important precursor of B-band lipopolysaccharide. The enzymes from Pseudomonas aeruginosa serotype O5 and Thermus thermophilus form a complex with the previous enzyme in the pathway, EC 1.1.1.335 (UDP-N-acetyl-2-amino-2-deoxyglucuronate oxidase). Group: Enzymes. Synonyms: WbpE; WlbC. Enzyme Commission Number: EC 2.6.1.98. 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-2939; UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase; EC 2.6.1.98; WbpE; WlbC. Cat No: EXWM-2939. | |
| UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase | This enzyme participates in the biosynthetic pathway for UDP-α-D-ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-α-D-mannuronic acid), an important precursor of B-band lipopolysaccharide. The enzymes from Pseudomonas aeruginosa serotype O5 and Thermus thermophilus form a complex with the the enzyme catalysing the next step the pathway (EC 2.6.1.98, UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase). The enzyme also possesses an EC 1.1.99.2 (L-2-hydroxyglutarate dehydrogenase) activity, and utilizes the 2-oxoglutarate produced by EC 2.6.1.98 to regenerate the tightly bound NAD+. The enzymes from Bordetella pertussis and Chromobacterium violaceum do not bind NAD+ as tightly and do not require 2-oxoglutarate to function. Group: Enzymes. Synonyms: WlbA; WbpB. Enzyme Commission Number: EC 1.1.1.335. 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-0249; UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase; EC 1.1.1.335; WlbA; WbpB. Cat No: EXWM-0249. | |
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