Find where to buy products from suppliers in the USA, including: distributors, industrial manufacturers in America, bulk supplies and wholesalers of raw ingredients & finished goods.
Search for products or services, then visit the American suppliers website for prices, SDS or more information. You can also view suppliers in Australia, NZ or the UK.
| Product | Description | |
|---|---|---|
| 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. | |
| carboxypeptidase Taq | A 56-kDa enzyme from Thermus aquaticus. Most active at 80° C. Type example of peptidase family M32. Group: Enzymes. Enzyme Commission Number: EC 3.4.17.19. CAS No. 9031-98-5. 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-4071; carboxypeptidase Taq; EC 3.4.17.19; 9031-98-5. Cat No: EXWM-4071. | |
| DNA Polymerase for PAGE | DNA Polymerase for PAGE. Dna polymerase for page is purified from e. coliexpressing a cloned dna polymerase from thermus aquaticus. the enzyme consists of a single polypeptide with a molecular weight of approximately 94 kda. dna polymerase for page has 5?-3? dna polymerase activity and 5?-3? exonuclease activity. lt lacks 3?-5? exonuclease activity. this enzyme is supplied with unique buffer, and its pcr product is suitable for sds-page and agarose gel electrophoresis. Group: Cloning Enzymes. Purity: 2500U. Storage: Store at -20 ?. Cat No: CE-3004. | |
| 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. | |
| [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 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. | |
| 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. | |
| Native Thermus brockianus α-Galactosidase | Alpha-galactosidase is a glycoside hydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. It is encoded by the GLA gene. Two recombinant forms of alpha-galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN). Protein determined by biuret. Group: Enzymes. Synonyms: Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Enzyme Commission Number: EC 3.2.1.22. CAS No. 9025-35-8. GLA. Activity: 40-80 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension. Suspension in 2.8 M (NH4)2SO4 solution. Source: Thermus brockianus. Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Cat No: NATE-0290. | |
| Native Thermus flavus Malic Dehydrogenase | Malic dehydrogenase (MDH) exists as two isoforms within eukaryotic cells, one that is expressed in the mitochondria and functions in the TCA cycle and one in the cytoplasm that converts malate from the mitochondria back into oxaloacetate. Malic dehydrogenase from thermus flavus is stable and active at 90 oc. Applications: Malic dehydrogenase has been used in a study to assess electron transport chain activity in mit ochondria from human skeletal muscle. it has also been used in a study to investigate activities of enzymes and ammonia in serum of rats with fluoride hyperglycemia. Group: Enzymes. Synonyms: malic dehydrogenase; L-malate dehydrogenase; NAD-L-malate dehydrogenase; malic acid dehydrogenase; NAD-dependent malic dehydrogenase; NAD-malate dehydrogenase; NAD-malic deh. Enzyme Commission Number: EC 1.1.1.37. CAS No. 9001-64-3. MDH. Activity: > 50 units/mg solid. Storage: -20°C. Form: lyophilized powder; Contains dextran. Source: Thermus flavus. 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-specific malate dehydrogenase; NAD-linked malate dehydrogenase; MDH; L-malate-NAD+ oxidoreductase; EC 1.1.1.37; 9001-64-3. Cat No: NATE-0448. | |
| 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. | |
| Taq DNA Polymerase | Taq DNA Polymerase. Taq dna polymerase is purified from e. coli expressing a cloned dna polymerase from thermus aquaticus. the enzyme consists of a single polypeptide with a molecular weight of approximately 94 kda. taq dna polymerase has 5?-3? dna polymerase activity and 5?-3? exonuclease activity. it lacks 3?-5? exonuclease activity. taq dna polymerase is suitable for routine amplification. pcr products are unsuitable for page. extension rate is about 1-2 kb/min. template-independent a can be generated at the 3? end of the pcr product. amplification of genomic dna fragment up to 4 kb. Group: Cloning Enzymes. Purity: 500U; 2500U. Storage: Store at -20 ?. Cat No: CE-3003. | |
| Taq I | One unit of the enzyme is the amount required to hydrolyze 1 μg of Lambda DNA in 1 hour at 65°C in a total reaction volume of 50 μl. Applications: After 20-fold overdigestion with enzyme more than 95% of the dna fragments can be ligated and recut. Group: Restriction Enzymes. Purity: 2000U; 10000U. T↑CGA AGC↓T. Activity: 20000u.a./ml. Appearance: 10 X SE-buffer Y, BSA. Storage: -20°C. Form: Liquid. Source: An E.coli strain, that carries the cloned gene Taq I from Thermus aquaticus. Pack: 10 mM Tris-HCl (pH 7.5); 300 mM NaCl; 0,1 mM EDTA; 1 mM DTT; 200 μg/ml BSA; 50% glycerol. Cat No: ET-1182RE. | |
| Tru9 I | One unit of the enzyme is the amount required to hydrolyze 1 μg of Lambda DNA in 1 hour at 65°C in a total reaction volume of 50 μl. Applications: After 20-fold overdigestion with enzyme more than 95% of the dna fragments can be ligated and recut. Group: Restriction Enzymes. Purity: 500 U; 2500U. T↑TAA AAT↓T. Activity: 20000u.a./ml. Appearance: 10 X SE-buffer W. Storage: -20°C. Form: Liquid. Source: An E.coli strain that carries the cloned Tru9 I gene from Thermus ruber 9. Pack: 10 mM Tris-HCl-(pH 7.5); 50 mM NaCl; 0,1 mM EDTA; 1 mM DTT; 200 μg/ml BSA; 50% glycerol. Cat No: ET-1183RE. | |
| TseF I | One unit of the enzyme is the amount required to hydrolyze 1 μg of Lambda DNA in 1 hour at 65°C in a total reaction volume of 50 μl. Applications: After 10-fold overdigestion with enzyme more than 95% of the dna fragments can be ligated and recut. Group: Restriction Enzymes. Purity: 200U; 1000U. ↑GTSAC CASTG&darr. Activity: 5000u.a./ml. Appearance: 10 X SE-buffer B. Storage: -20°C. Form: Liquid. Source: An E.coli strain, that carries the cloned gene TseFI from Thermus species F35. Pack: 10 mM Tris-HCl (pH 7.6); 50 mM NaCl; 0,1 mM EDTA; 1 mM DTT; 200 μg/ml BSA; 50% glycerol. Cat No: ET-1184RE. | |
| 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. | |
| 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. | |
| 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. | |
| Native Thermus brockianus β-Galactosidase | β-galactosidase, also called beta-gal or β-gal, is a hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides. SubstRates of different β-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. The enzyme hydrolyses terminal, non-reducing b-d-galactose residues in b-d-galactosides. Group: Enzymes. Synonyms: Beta-Galactosidase; Galactosidase; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat. CAS No. 9031-11-2. β-gal. Source: Thermus brockianus. Beta-Galactosidase; Galactosidase; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat. Cat No: NATE-0298. | |
| Native Thermus flavus 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 flavus. 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-1614. | |
| 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. | |
| 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. | |
| 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. | |
Our database is helping our users find suppliers everyday.
