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| Product | Description | |
|---|---|---|
| 1-aminocyclopropane-1-carboxylate deaminase | A pyridoxal 5'-phosphate enzyme. The enzyme, found in certain soil bacteria and fungi, catalyses the ring opening of 1-aminocyclopropane-1-carboxylate, the immediate precursor to ethylene, an important plant hormone that regulates fruit ripening and other processes. The enzyme releases an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. The enzyme has been used to make fruit ripening dependent on externally added ethylene, as it removes the substrate for endogenous ethylene formation. Group: Enzymes. Synonyms: 1-aminocyclopropane-1-carboxylate endolyase (deaminating); ACC deaminase; 1-aminocyclopropane carboxylic acid deaminase. Enzyme Commission Number: EC 3.5.99.7. CAS No. 69553-48-6. 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-4590; 1-aminocyclopropane-1-carboxylate deaminase; EC 3.5.99.7; 69553-48-6; 1-aminocyclopropane-1-carboxylate endolyase (deaminating); ACC deaminase; 1-aminocyclopropane carboxylic acid deaminase. Cat No: EXWM-4590. |  |
| 2-iminobutanoate/2-iminopropanoate deaminase | This enzyme, which has been found in all species and tissues examined, catalyses the hydrolytic deamination of imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases, such as EC 4.3.1.19, threonine ammonia-lyase and EC 4.3.1.17, L-serine ammonia-lyase. The reactions, which can occur spontaneously, are accelerated to minimize the cellular damage that could be caused by these reactive intermediates. Group: Enzymes. Synonyms: yjgF (gene name); ridA (gene name); enamine/imine deaminase (ambiguous). Enzyme Commission Number: EC 3.5.99.10. 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-4586; 2-iminobutanoate/2-iminopropanoate deaminase; EC 3.5.99.10; yjgF (gene name); ridA (gene name); enamine/imine deaminase (ambiguous). Cat No: EXWM-4586. | |
| 3-chloro-D-alanine dehydrochlorinase | A pyridoxal-phosphate protein. The enzyme cleaves a carbon-chlorine bond, releasing a chloride and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. The enzyme's activity can also result in β-replacement reactions, e.g. in the presence of hydrogen sulfide it can convert 3-chloro-D-alanine into D-cysteine and chloride. Group: Enzymes. Synonyms: β-chloro-D-alanine dehydrochlorinase; 3-chloro-D-alanine chloride-lyase (deaminating). Enzyme Commission Number: EC 4.5.1.2. CAS No. 78990-65-5. 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-5344; 3-chloro-D-alanine dehydrochlorinase; EC 4.5.1.2; 78990-65-5; β-chloro-D-alanine dehydrochlorinase; 3-chloro-D-alanine chloride-lyase (deaminating). Cat No: EXWM-5344. | |
| 4-Chloro-3-indolyl b-D-galactopyranoside | 4-Chloro-3-indolyl β-D-galactopyranoside is a prominent biochemical substrate ubiquitously employed in the biomedical sector, serving as a remarkable catalyst to discern the existence of β-galactosidase activity is an indispensable marker extensively utilized in the realm of molecular biology. Notably, its versatile application aids in the comprehensive investigation of gene expression patterns and enzyme functionality across diverse biological systems. Moreover, this compound, owing to its profound impact, garners immense prominence in assays necessitating a visual representation of β-galactosidase-mediated hydrolytic processes. CAS No. 135313-63-2. Molecular formula: C14H16ClNO6. Mole weight: 329.73. |  |
| 4-Methylumbelliferyl 2-Acetamido-2-deoxy-3-O-(tetra-O-acetyl-β-D-galactopyranosyl)-4,6-O-(p-methoxyphenylmethylene)-α-D-galactopyranoside | 4-Methylumbelliferyl 2-Acetamido-2-deoxy-3-O-(tetra-O-acetyl-β-D-galactopyranosyl)-4,6-O-(p-methoxyphenylmethylene)-α-D-galactopyranoside is a biomedical product used for studying enzymatic activities related to certain diseases. It serves as a fluorogenic substrate for measuring the hydrolytic activity of related enzymes, particularly those associated with lysosomal storage disorders or glycosidic bond cleavage. Molecular formula: C40H45NO18. Mole weight: 827.78. | |
| 6-oxocyclohex-1-ene-1-carbonyl-CoA hydratase | The enzyme, which participates in the anaerobic benzoyl-CoA degradation pathway in certain organisms, catalyses the addition of one molecule of water to the double bound of 6-oxocyclohex-1-ene-1-carbonyl-CoA followed by the hydrolytic C-C cleavage of the alicyclic ring. Group: Enzymes. Synonyms: 6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase; 6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase (decyclizing). Enzyme Commission Number: EC 3.7.1.21. 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-4729; 6-oxocyclohex-1-ene-1-carbonyl-CoA hydratase; EC 3.7.1.21; 6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase; 6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase (decyclizing). Cat No: EXWM-4729. | |
| acetoin dehydrogenase | Requires thiamine diphosphate. This enzyme, which belongs to the family of 2-oxo acid dehydrogenase complexes, catalyses the oxidative-hydrolytic cleavage of acetoin to acetaldehyde and acetyl-CoA in many bacterial strains, both aerobic and anaerobic. The enzyme is composed of multiple copies of three enzymic components: acetoin oxidoreductase (E1), dihydrolipoamide acetyltransferase (E2) and dihydrolipoyl dehydrogenase (E3). Group: Enzymes. Synonyms: acetoin dehydrogenase complex; acetoin dehydrogenase enzyme system; AoDH ES. Enzyme Commission Number: EC 2.3.1.190. 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-2133; acetoin dehydrogenase; EC 2.3.1.190; acetoin dehydrogenase complex; acetoin dehydrogenase enzyme system; AoDH ES. Cat No: EXWM-2133. | |
| AMP-CP | AMP-CP is a non-hydrolytic analogue of ADP and a starting structure in the synthesis of α/β hydrolysis-resistant tri- and polyphosphates. It is also an inhibitor of CD73. Uses: Enzyme inhibitors. Synonyms: Adenosine 5'-methylenediphosphate; MethADP; phosphomethylphosphonic acid adenosyl ester; AMP-CP; Adenosine, 5'-(trihydrogen methylenebis(phosphonate)); Adenosine 5'-(hydrogen (phosphonomethyl)phosphonate); ALPHA,BETA-METHYLENEADENOSINE 5'-DIPHOSPHATE; 104835-70-3; AMPCP; CHEBI:40730; 0T2A5439OE; [[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]methylphosphonic acid; alpha,beta-Methyleneadenosine 5'-diphosphate sodium salt; 5'-O-[hydroxy (phosphonomethyl) phosphoryl]adenosine; MethADP (Adenosine 5'-(alpha,beta-methylene)diphosphate). Grades: ≥ 95% by HPLC. CAS No. 104835-70-3. Molecular formula: C11H17N5O9P2 (free acid). Mole weight: 425.2(free acid). | |
| carbamoyl-serine ammonia-lyase | A pyridoxal-phosphate protein. The enzyme cleaves a carbon-oxygen bond, releasing CO2, ammonia, and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and a second ammonia molecule. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. Group: Enzymes. Synonyms: O-carbamoyl-L-serine deaminase; carbamoylserine deaminase; O-carbamoyl-L-serine ammonia-lyase (pyruvate-forming). Enzyme Commission Number: EC 4.3.1.13. CAS No. 52227-64-2. 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-5273; carbamoyl-serine ammonia-lyase; EC 4.3.1.13; 52227-64-2; O-carbamoyl-L-serine deaminase; carbamoylserine deaminase; O-carbamoyl-L-serine ammonia-lyase (pyruvate-forming). Cat No: EXWM-5273. | |
| Creatinase, microorganism | Creatine amidinohydrolase, microorganism is a hydrolytic enzyme that catalyzes the hydrolysis of creatine into creatinine and urea, playing a crucial role in the measurement of creatinine concentration. Creatine amidinohydrolase, microorganism can be used in the development of biosensors for measuring serum creatinine levels [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: Creatine amidinohydrolase, microorganism. CAS No. 37340-58-2. Pack Sizes: 1 KU; 5 KU. Product ID: HY-P2893B. |  |
| cystathionine β-lyase | A pyridoxal-phosphate protein. The enzyme cleaves a carbon-sulfur bond, releasing L-homocysteine and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. The enzyme from some sources also acts on L-cystine, forming pyruvate, ammonia and cysteine persulfide, and a number of related compounds. Possibly identical, in yeast, with EC 4.4.1.6 S-alkylcysteine lyase. Group: Enzymes. Synonyms: β-cystathionase; cystine lyase; cystathionine L-homocysteine-lyase (deaminating); L-cystathionine L-homocysteine-lyase (deaminating); CBL. Enzyme Commission Number: EC 4.4.1.8. CAS No. 9055-5-4. Cystathionine β-lyase. 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-5341; cystathionine β-lyase; EC 4.4.1.8; 9055-05-4; β-cystathionase; cystine lyase; cystathionine L-homocysteine-lyase (deaminating); L-cystathionine L-homocysteine-lyase (deaminating); CBL. Cat No: EXWM-5341. | |
| cystathionine γ-lyase | A multifunctional pyridoxal-phosphate protein. The enzyme cleaves a carbon-sulfur bond, releasing L-cysteine and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form 2-oxobutanoate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. Also catalyses the conversion of L-homoserine to 2-oxobutanoate and ammonia, of L-cystine to thiocysteine, pyruvate and ammonia, and of L-cysteine to pyruvate, hydrogen sulfide and ammonia. Group: Enzymes. Synonyms: homoserine deaminase; homoserine dehydratase; cystine desulfhydrase; cysteine desulfhydrase; γ-cystathionase; cystathionase; homoserine deaminase-cystathionase; γ-CTL; cystalysin; cysteine lyase; L-cystathionine cysteine-. Enzyme Commission Number: EC 4.4.1.1. CAS No. 9012-96-8. CGL. 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-5312; cystathionine γ-lyase; EC 4.4.1.1; 9012-96-8; homoserine deaminase; homoserine dehydratase; cystine desulfhydrase; cysteine desulfhydrase; γ-cystathionase; cystathionase; homoserine deaminase-cystathionase; γ-CTL; cystalysin; cysteine lyase; L-cystathionine cysteine-lyase (deaminating); CGL. Cat No: EXWM-5312. | |
| cysteine-S-conjugate β-lyase | A pyridoxal-phosphate protein. The enzyme can act on a broad range of L-cysteine-S-conjugates, including aromatic conjugates such as 4-bromobenzene and 2,4-dinitrobenzene. The enzyme cleaves a carbon-sulfur bond, releasing a thiol and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. Group: Enzymes. Synonyms: cysteine conjugate β-lyase; glutamine transaminase K/cysteine conjugate β-lyase; L-cysteine-S-conjugate thiol-lyase (deaminating). Enzyme Commission Number: EC 4.4.1.13. CAS No. 68652-57-3. 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-5315; cysteine-S-conjugate β-lyase; EC 4.4.1.13; 68652-57-3; cysteine conjugate β-lyase; glutamine transaminase K/cysteine conjugate β-lyase; L-cysteine-S-conjugate thiol-lyase (deaminating). Cat No: EXWM-5315. | |
| D-serine ammonia-lyase | A pyridoxal-phosphate protein. The enzyme cleaves a carbon-oxygen bond, releasing a water molecule (hence the enzyme's original classification as EC 4.2.1.14, D-serine dehydratase) and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. Also acts, slowly, on D-threonine. Group: Enzymes. Synonyms: D-hydroxyaminoacid dehydratase; D-serine dehydrase; D-hydroxy amino acid dehydratase; D-serine hydrolase; D-serine dehydratase (deaminating); D-serine deaminase; D-serine hydro-lyase (deaminating). Enzyme Commission Number: EC 4.3.1.18. CAS No. 9015-88-7. 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-5278; D-serine ammonia-lyase; EC 4.3.1.18; 9015-88-7; D-hydroxyaminoacid dehydratase; D-serine dehydrase; D-hydroxy amino acid dehydratase; D-serine hydrolase; D-serine dehydratase (deaminating); D-serine deaminase; D-serine hydro-lyase (deaminating). Cat No: EXWM-5278. | |
| dye decolorizing peroxidase | Heme proteins with proximal histidine secreted by basidiomycetous fungi and eubacteria. They are similar to EC 1.11.1.16 versatile peroxidase (oxidation of Reactive Black 5, phenols, veratryl alcohol), but differ from the latter in their ability to efficiently oxidize a number of recalcitrant anthraquinone dyes, and inability to oxidize Mn(II). The model substrate Reactive Blue 5 is converted with high efficiency via a so far unique mechanism that combines oxidative and hydrolytic steps and leads to the formation of phthalic acid. Bacterial TfuDyP catalyses sulfoxidation. Group: Enzymes. Synonyms: DyP; DyP-type peroxidase. Enzyme Commission Number: EC 1.11.1.19. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0500; dye decolorizing peroxidase; EC 1.11.1.19; DyP; DyP-type peroxidase. Cat No: EXWM-0500. | |
| glucosaminate ammonia-lyase | Contains pyridoxal phosphate. The enzyme releases an unstable enamine product that tautomerizes to an imine form, which undergoes spontaneous hydrolytic deamination to form the final product. Group: Enzymes. Synonyms: glucosaminic dehydrase; D-glucosaminate dehydratase; D-glucosaminic acid dehydrase; aminodeoxygluconate dehydratase; 2-amino-2-deoxy-D-gluconate hydro-lyase (deaminating); aminodeoxygluconate ammonia-lyase; 2-amino-2-deoxy-D-gluconate ammonia-lyase; D-glucosaminate ammonia-lyase; D-glucosaminate ammonia-lyase (isomerizing; 2-dehydro-3-deoxy-D-gluconate-forming). Enzyme Commission Number: EC 4.3.1.9. CAS No. 37290-91-8. 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-5295; glucosaminate ammonia-lyase; EC 4.3.1.9; 37290-91-8; glucosaminic dehydrase; D-glucosaminate dehydratase; D-glucosaminic acid dehydrase; aminodeoxygluconate dehydratase; 2-amino-2-deoxy-D-gluconate hydro-lyase (deaminating); aminodeoxygluconate ammonia-lyase; 2-amino-2-deoxy-D-gluconate ammonia-lyase; D-glucosaminate ammonia-lyase; D-glucosaminate ammonia-lyase (isomerizing; 2-dehydro-3-deoxy-D-gluconate-forming). Cat No: EXWM-5295. | |
| glutamate N-acetyltransferase | Also has some hydrolytic activity on acetyl-L-ornithine, but the rate is 1% of that of transferase activity. Group: Enzymes. Synonyms: ornithine transacetylase; α-N-acetyl-L-ornithine:L-glutamate N-acetyltransferase; acetylglutamate synthetase; acetylglutamate-acetylornithine transacetylase; acetylglutamic synthetase; acetylglutamic-acetylornithine transacetylase; acetylornithinase; acetylornithine glutamate acetyltransferase; glutamate acetyltransferase; N-acetyl-L-glutamate synthetase; N-acetylglutamate synthase; N-acetylglutamate synthetase; ornithine acetyltransferase; 2-N. Enzyme Commission Number: EC 2.3.1.35. CAS No. 37257-14-0. 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-2213; glutamate N-acetyltransferase; EC 2.3.1.35; 37257-14-0; ornithine transacetylase; α-N-acetyl-L-ornithine:L-glutamate N-acetyltransferase; acetylglutamate synthetase; acetylglutamate-acetylornithine transacetylase; acetylglutamic synthetase; acetylglutamic-acetylornithine transacetylase; acetylornithinase; acetylornithine glutamate acetyltransferase; glutamate acetyltransferase; N-acetyl-L-glutamate synthetase; N-acetylglutamate synthase; N-acetylglutamate synthetase; ornithine acetyltransferase; 2-N-acetyl-L-ornithine:L-glutamate N-acetyltransferase. Cat No: EXWM-2213. | |
| Guanine deaminase from Human, Recombinant | GDA is an enzyme responsible for the hydrolytic deamination of guanine. Studies in rat ortholog suggest this gene plays a role in microtubule assembly. Multiple transcript variants encoding different isoforms have been found for this gene. Recombinant human GDA protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. Group: Enzymes. Synonyms: Guanine deaminase; CYPIN; GUANASE; NEDASIN; guanine aminase; GAH; guanine aminohydrolase; GDA. Purity: > 90% determined by SDS-PAGE. GDA. Mole weight: 53 kDa (477 aa, 1-454 aa + His Tag). Activity: > 0.9 unit/ml. Appearance: Liquid. Storage: at -20°C. Form: 1 mg/ml solution 20 mM Tris-HCl buffer (pH 8.0), 10% glycerol and 1 mM DTT. Source: E. coli. Species: Human. Guanine deaminase; CYPIN; GUANASE; NEDASIN; guanine aminase; GAH; guanine aminohydrolase; GDA. Cat No: NATE-1285. | |
| homocysteine desulfhydrase | A pyridoxal-phosphate protein. The enzyme cleaves a carbon-sulfur bond, releasing hydrogen sulfide and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form 2-oxobutanoate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. Group: Enzymes. Synonyms: homocysteine desulfurase; L-homocysteine hydrogen-sulfide-lyase (deaminating). Enzyme Commission Number: EC 4.4.1.2. CAS No. 9024-41-3. 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-5321; homocysteine desulfhydrase; EC 4.4.1.2; 9024-41-3; homocysteine desulfurase; L-homocysteine hydrogen-sulfide-lyase (deaminating). Cat No: EXWM-5321. | |
| L-Asparaginase | Asparaginase is a hydrolytic enzyme that catalyzes the hydrolysis of asparagine to aspartic acid and is used for the treatment of acute lymphoblastic leukemia. Synonyms: L-ASNase; Asparaginase; L-Asparagine Amidohydrolase. Grades: ≥96% by RP-HPLC. CAS No. 9015-68-3. Molecular formula: C7H5NOS. Mole weight: 151.186. | |
| L-cysteate sulfo-lyase | A pyridoxal-phosphate protein. The enzyme cleaves a carbon-sulfur bond, releasing hydrogensulfite and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. D-Cysteine can also act as a substrate, but more slowly. It is converted into hydrogen sulfide, pyruvate, and ammonia. This inducible enzyme from the marine bacterium Silicibacter pomeroyi DSS-3 forms part of the cysteate-degradation pathway. Group: Enzymes. Synonyms: L-cysteate sulfo-lyase (deaminating); CuyA; L-cysteate bisulfite-lyase (deaminating; pyruvate-forming). Enzyme Commission Number: EC 4.4.1.25. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5327; L-cysteate sulfo-lyase; EC 4.4.1.25; L-cysteate sulfo-lyase (deaminating); CuyA; L-cysteate bisulfite-lyase (deaminating; pyruvate-forming). Cat No: EXWM-5327. | |
| L-cysteine desulfidase | The enzyme from the archaeon Methanocaldococcus jannaschii contains a [4Fe-4S] cluster and is specific for L-cysteine (cf. EC 4.4.1.1, cystathionine γ-lyase). It cleaves a carbon-sulfur bond releasing sulfide and the unstable enamine product 2-aminoprop-2-enoate that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. The same reaction can also be catalysed by some pyridoxal-phosphate proteins (cf. EC 4.4.1.1, cystathionine γ-lyase). Group: Enzymes. Synonyms: L-cysteine desulfhydrase. Enzyme Commission Number: EC 4.4.1.28. 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-5330; L-cysteine desulfidase; EC 4.4.1.28; L-cysteine desulfhydrase. Cat No: EXWM-5330. | |
| methionine γ-lyase | A pyridoxal-phosphate protein. The enzyme cleaves a carbon-sulfur bond, releasing methanethiol and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form 2-oxobutanoate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. The enzyme is involved in L-methionine catabolism. Group: Enzymes. Synonyms: L-methioninase; methionine lyase; methioninase; methionine dethiomethylase; L-methionine γ-lyase; L-methionine methanethiol-lyase (deaminating). Enzyme Commission Number: EC 4.4.1.11. CAS No. 42616-25-1. L-Methionine γ-Lyase. 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-5314; methionine γ-lyase; EC 4.4.1.11; 42616-25-1; L-methioninase; methionine lyase; methioninase; methionine dethiomethylase; L-methionine γ-lyase; L-methionine methanethiol-lyase (deaminating). Cat No: EXWM-5314. | |
| Native Almonds β-Glucosidase | β-glucosidase is involved in the hydrolysis of β-glycosidic bonds connecting carbohydrate residues in β-D-glycosides. They convert cellobiose and cellooligosaccharides produced by the endo and exoglucanases to glucose. Applications: Β-glucosidase is also used in the synthesis of glucosides and fucosides with various potential applications in pharmaceutical, cosmetic and detergent industries, hydrolytic removal of aglycone moiety from flavonoid and isoflavonoid glycosides, flavor enhancement of fruit juices and wine, and biosynthesis of oligosaccharides. Group: Enzymes. Synonyms: β-glucosidase; gentiobiase; cellobiase; emulsin; elaterase; aryl-β-glucosidase; β-D-glucosidase; β-glucoside glucohydrolase; arbutinase; amygdalinase; p-nitrophenyl β-glucosidase; primeverosida. Enzyme Commission Number: EC 3.2.1.31. CAS No. 9001-22-3. β-Glucosidase. Mole weight: Mr ~135 kDa. Activity: 10-30 units/mg solid; > 2 units/mg solid. Storage: 2-8°C. Form: lyophilized powder. Source: Almonds. β-glucosidase; gentiobiase; cellobiase; emulsin; elaterase; aryl-β-glucosidase; β-D-glucosidase; β-glucoside glucohydrolase; arbutinase; amygdalinase; p-nitrophenyl β-glucosidase; primeverosidase; amygdalase; linamarase; salicilinase; β-1,6-glucosidase; EC 3.2.1.31; 9001-22-3. Cat No: NATE-0769. | |
| Native Aspergillus oryzae Nuclease S1 | Nuclease S1 isolated from Aspergillus oryzae exhibits endo-and exolytic hydrolytic activity for the phosphodiester bonds of single-stranded DNA and RNA yielding 5-phosphomononucleotide and 5-phosphooligonucleotide end-products. It is used to digest non-annealed polynucleotide tails and hairpin loops in RNA and DNA duplexes and can be used to convert superhelical DNA to the linear form. The nuclease s1 enzyme from aspergillus oryzae has the ability to degrade single-stranded oligonucleotides composed of either deoxynucleotides or ribonucleotides. Applications: Nuclease s1 from aspergillus oryzae has been used in a study to assess a bi ochemical method for mapping mutational...e S1 nuclease; EC 3.1.30.1; 37288-25-8. Enzyme Commission Number: EC 3.1.30.1. CAS No. 37288-25-8. Nuclease. Storage: -20°C. Form: Solution containing 30 mM sodium acetate, 50 mM NaCl, 1 mM ZnCl2, 50% glycerol, 2 mg/ml protein. Source: Aspergillus oryzae. endonuclease S1 (Aspergillus); single-stranded-nucleate endonuclease; deoxyribonuclease S1; deoxyribonuclease S1; nuclease S1; Neurospora crassa single-strand specific endonuclease; S1 nuclease; single-strand endodeoxyribonuclease; single-stranded DNA specific endonuclease; single-strand-specific endodeoxyribonuclease; single strand-specific DNase; Aspergillus oryzae S1 nuclease; EC 3.1.30.1; 37288-25-8. Cat No: NATE-0492. | |
| Native β-hemolytic Streptococcus Streptokinase | Streptokinase (SK) is an enzyme secreted by several species of streptococci that can bind and activate human plasminogen. SK is used as an effective and inexpensive thrombolysis medication in some cases of myocardial infarction (heart attack) and pulmonary embolism. Streptokinase belongs to a group of medications known as fibrinolytics, and complexes of streptokinase with human plasminogen can hydrolytically activate other unbound plasminogen by activating through bond cleavage to produce plasmin. There are three domains to Streptokinase, denoted α (residues 1-150), β (residues 151-287), and γ (residues 288-414). Each domain binds plasminogen, altho...bral hemorrhage. streptokinase is also used in the treatment of complicated parapneumonic effusions and empyema where adverse reactions, allergic type, are rare. streptokinase has been used in a study to compare primary coronary intervention and thrombolytic therapy in my ocardial infarction patients. Group: Enzymes. Synonyms: Streptokinase; SK; EC 3.4.99.0; 9002-01-1. Enzyme Commission Number: EC 3.4.99.0. CAS No. 9002-1-1. SK. Activity: > 3,500 units/mg solid. Storage: -20°C. Form: Lyophilized powder containing ~50% total protein by biuret and sodium glutamate. Total protein composed of enzyme protein and human serum albumin. Source: β-hemolytic Streptococcus | |
| Native Microorganism Creatine Amidinohydrolase | Creatine Amidinohydrolase catalyzes the hydrolytic reaction converting creatine to sarcosine and urea. The enzyme is purified from a microorganism. The molecular weight of the enzyme is approximately 67,000. The enzyme is useful for the enzymatic assay of creatine and creatinine when coupled with other related enzymes. creatine + H2O ? sarcosine + urea. Applications: This enzyme is useful for enzymatic determination of creatinine when coupled with creatinine amidohydrolase, sarcosine dehydrogenase or sarcosine oxidase and formaldehyde dehydrogenase in clinical analysis. Group: Enzymes. Synonyms: Creatine Amidinohydrolase; Creatinase; EC 3.5.3.3. Enzyme Commission Number: EC 3.5.3.3. CAS No. 37340-58-2. Creatinase. Mole weight: approx. 67 kDa (by gel filtration). Activity: Grade? 4.0 U/mg-solid or more. Stability: Stable at -20°C for at least one year. Appearance: White amorphous powder, lyophilized. Form: Freeze dried powder. Source: Microorganism. Creatine amidohydrolase; Creatinase; EC 3.5.3.3. Cat No: DIA-185. | |
| Native Porcine Leucine Aminopeptidase | Leucine aminopeptidase (LAP) is a proteolytic enzyme which hydrolyzes the peptide bond adjacent to a free amino group. It is called leucine aminopeptidase because it rapidly catalyzes the hydrolysis of leucine containing peptides. However, it also catalyzes the hydrolytic release of other amino acids located at the N-terminal end of various peptides and proteins. The enzyme from porcine kidney has been extensively studied. It has a molecular weight of 255,000 and it consists of four subunits each having one atom of zinc. Group: Enzymes. Synonyms: Leucine Aminopeptidase; 9054-63-1; leucyl peptidase; peptidase S; cytosol aminopeptidase; cathepsin III; L-leucine aminopeptidase; leucinaminopeptidase; leucinamide aminopeptidase; FTBL proteins; proteinates FTBL; aminopeptidase II; aminopeptidase III; aminopeptidas. Enzyme Commission Number: EC 3.4.11.1. Purity: 90% (biuret). LAP. Activity: >100 U/mg protein. Storage: Stable when stored at 4°C. Do not freeze. Form: Ammonium Sulfate. Source: Porcine Kidney. Species: Porcine. Leucine Aminopeptidase; 9054-63-1; leucyl peptidase; peptidase S; cytosol aminopeptidase; cathepsin III; L-leucine aminopeptidase; leucinaminopeptidase; leucinamide aminopeptidase; FTBL proteins; proteinates FTBL; aminopeptidase II; aminopeptidase III; aminopeptidase I; EC 3.4.11.1; leucyl aminopeptidase; LAP. Cat No: NATE-1879. | |
| Native Pseudomonas sp. Creatinine amidohydrolase | Creatinine Amidohydrolase catalyzes the hydrolytic reaction converting creatinine to creatine. The enzyme is purified from a microorganism. The molecular size of the enzyme is approximately 175,000. The enzyme is useful for the enzy-matic assay of creatinine when coupled with other related enzymes. Creatinine + H2O ? Creatine. Creatininase from pseudomonas sp. is a homohexameric enzyme with a molecular mass of 28.4 kda per subunit. it is a cyclic amidohydrolase catalysing the reversible conversion of creatinine to creatine. each monomer contains a binuclear zinc centre near the c termini of the β-strands and the n termini of the main α-helices. these zinc ions indicate the location of the active site. Applications: This enzyme is useful for enzymatic determination of creatinine when coupled with creatine amidinohydrolase, sarcosine dehydrogenase or sarcosine oxidase and formaldehyde dehydrogenase in clinical analysis. Group: Enzymes. Synonyms: creatininase; creatinine hydrolase; creatinine . Enzyme Commission Number: EC 3.5.2.10. CAS No. 9025-13-2. Creatininase. Mole weight: 175 kDa. Activity: > 250U/mg protein. Storage: 2-8°C. Form: Lyophilized powder containing sucrose and BSA as stabilizers. Source: Pseudomonas sp. creatininase; creatinine hydrolase; creatinine amidohydrolase; EC 3.5.2.10; 9025-13-2. Cat No: DIA-130. | |
| Native Streptococcus hemolyticus Streptokinase | Streptokinase (SK) is an enzyme secreted by several species of streptococci that can bind and activate human plasminogen. SK is used as an effective and inexpensive thrombolysis medication in some cases of myocardial infarction (heart attack) and pulmonary embolism. Streptokinase belongs to a group of medications known as fibrinolytics, and complexes of streptokinase with human plasminogen can hydrolytically activate other unbound plasminogen by activating through bond cleavage to produce plasmin. Streptokinase from β-hemolytic streptococcus (lancefield group c). Applications: Streptokinase is commonly used as a thrombolytic agent in the therapy of ischemic stroke. this therapy carries the important risk of intracerebral hemorrhage. streptokinase is also used in the treatment of complicated parapneumonic effusions and empyema where adverse reactions, allergic type, are rare. Group: Enzymes. Synonyms: St. Enzyme Commission Number: EC 3.4.99.0. CAS No. 9002-1-1. SK. Activity: > 3,500 units/mg solid. Appearance: Appearance (Color): Conforms to Requirements Off-White to Light Yellow to Light Beige. Form: Lyophilized powder containing ~50% total protein by biuret and sodium glutamate. Total protein composed of enzyme protein and human serum albumin. Source: Streptococcus hemolyticus. Streptokinase; SK; EC 3.4.99.0. Cat No: PHAM-261. | |
| Pup amidohydrolase | The enzyme has been characterized from the bacterium Mycobacterium tuberculosis. It catalyses the hydrolysis of the amido group of the C-terminal glutamine of prokaryotic ubiquitin-like protein (Pup), thus activating it for ligation to target proteins, a process catalysed by EC 6.3.1.19, prokaryotic ubiquitin-like protein ligase. The reaction requires ATP as cofactor but not its hydrolysis. The enzyme also catalyses the hydrolytic cleavage of the bond formed by the ligase, between an ε-amino group of a lysine residue of the target protein and the γ-carboxylate of the C-terminal glutamate of the prokaryotic ubiquitin-like protein. Group: Enzymes. Synonyms: dop (gene name); Pup deamidase; depupylase/deamidase; DPUP; depupylase. Enzyme Commission Number: EC 3.5.1.119. 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-4399; Pup amidohydrolase; EC 3.5.1.119; dop (gene name); Pup deamidase; depupylase/deamidase; DPUP; depupylase. Cat No: EXWM-4399. | |
| Recombinant Methionine aminopeptidase from E.coli | Methionine aminopeptidase (MetAP) catalyzes the hydrolytic cleavage of the N-terminal methionine from newly synthesized polypeptides. Group: Enzymes. Synonyms: MetAP; EC 3.4.11.18; 61229-81-0; methionine aminopeptidase; peptidase M; L-methionine aminopeptidase; MAP. Enzyme Commission Number: EC 3.4.11.18. CAS No. 61229-81-0. Purity: > 80 %. MAP. Mole weight: 29 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: E. coli. MetAP; EC 3.4.11.18; 61229-81-0; methionine aminopeptidase; peptidase M; L-methionine aminopeptidase; MAP. Cat No: NATE-1018. | |
| Ribonuclease H from Escherichia coli, Recombinant | Ribonuclease H (RNase H) is a family of non-sequence-specific endonucleases that catalyze the cleavage of RNA via a hydrolytic mechanism. Members of the RNase H family can be found in nearly all organisms, from bacteria to archaea to eukaryotes. RNase Hs ribonuclease activity cleaves the 3-O-P bond of RNA in a DNA/RNA duplex substrate to produce 3-hydroxyl and 5-phosphate terminated products. In DNA replication, RNase H is responsible for removing the RNA primer, allowing completion of the newly synthesized DNA. Applications: Ribonuclease h from escherichia coli has been used in a study to assess metallobi ochemistry of the magnesium ion. ribonuclease h has also been used in a study to investigate selective inhibitors of hiv-1 reverse transcriptase ass ociated rnase h activity. Group: Enzymes. Synonyms: Ribonuclease H; RNase H; EC 3.1.4.34; 9050-76-4. Enzyme Commission Number: EC 3.1.4.34. CAS No. 9050-76-4. Rnase. Activity: 1,000-4,000 units/mL. Storage: -20°C. Form: buffered aqueous glycerol solution; Solution in 50% glycerol containing 20 mM Tris-HCl, pH 7.5, 100 mM KCl, 10 mM MgCl2, 0.1 mM EDTA, 0.1 mM DTT and 0.05 mg BSA per ml. Source: E. coli. Species: Escherichia coli. Ribonuclease H; RNase H; EC 3.1.4.34; 9050-76-4. Pack: vial of ~30 units. Cat No: NATE-0657. | |
| S-alkylcysteine lyase | A pyridoxal-phosphate protein. The enzyme cleaves a carbon-sulfur bond, releasing an alkyl thiol and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. Possibly identical, in yeast, with EC 4.4.1.8 cystathionine β-lyase. Group: Enzymes. Synonyms: S-alkylcysteinase; alkylcysteine lyase; S-alkyl-L-cysteine sulfoxide lyase; S-alkyl-L-cysteine lyase; S-alkyl-L-cysteinase; alkyl cysteine lyase; S-alkyl-L-cysteine alkylthiol-lyase (deaminating). Enzyme Commission Number: EC 4.4.1.6. CAS No. 62213-27-8. 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-5340; S-alkylcysteine lyase; EC 4.4.1.6; 62213-27-8; S-alkylcysteinase; alkylcysteine lyase; S-alkyl-L-cysteine sulfoxide lyase; S-alkyl-L-cysteine lyase; S-alkyl-L-cysteinase; alkyl cysteine lyase; S-alkyl-L-cysteine alkylthiol-lyase (deaminating). Cat No: EXWM-5340. | |
| Streptokinase from Streptococcus sp., Recombinant | Streptokinase (SK) is an enzyme secreted by several species of streptococci that can bind and activate human plasminogen. SK is used as an effective and inexpensive thrombolysis medication in some cases of myocardial infarction (heart attack) and pulmonary embolism. Streptokinase belongs to a group of medications known as fibrinolytics, and complexes of streptokinase with human plasminogen can hydrolytically activate other unbound plasminogen by activating through bond cleavage to produce plasmin. There are three domains to Streptokinase, denoted α (residues 1-150), β (residues 151-287), and γ (residues 288-414). Each domain binds plasminogen, although none can activate plasminogen independently. Group: Enzymes. Synonyms: SK; EC 3.4.99.0; 9002-01-1. Purity: Greater than 97.0% as determined by:(a) Analysis by RP-HPLC.(b) Analysis by SDS-PAGE. SK. Stability: Lyophilized Streptokinase although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Streptokinase should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles. Form: Sterile Filtered White lyophilized (freeze-dried) powder. Source: E.Coli. Streptokinase; SK; EC 3.4.99.0; 9002-01-1. Cat No: NATE-1630. | |
| tryptophanase | A pyridoxal-phosphate protein, requiring K+. The enzyme cleaves a carbon-carbon bond, releasing indole and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. Also catalyses 2,3-elimination and β-replacement reactions of some indole-substituted tryptophan analogues of L-cysteine, L-serine and other 3-substituted amino acids. Group: Enzymes. Synonyms: L-tryptophanase; L-tryptophan indole-lyase (deaminating); TNase. Enzyme Commission Number: EC 4.1.99.1. CAS No. 9024-00-4. TNase. 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-4925; tryptophanase; EC 4.1.99.1; 9024-00-4; L-tryptophanase; L-tryptophan indole-lyase (deaminating); TNase. Cat No: EXWM-4925. | |
| tyrosine phenol-lyase | A pyridoxal-phosphate protein. The enzyme cleaves a carbon-carbon bond, releasing phenol and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. The enzyme also slowly catalyses similar reactions with D-tyrosine, S-methyl-L-cysteine, L-cysteine, L-serine and D-serine. Group: Enzymes. Synonyms: β-tyrosinase; L-tyrosine phenol-lyase (deaminating). Enzyme Commission Number: EC 4.1.99.2. CAS No. 9059-31-8. 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-4933; tyrosine phenol-lyase; EC 4.1.99.2; 9059-31-8; β-tyrosinase; L-tyrosine phenol-lyase (deaminating). Cat No: EXWM-4933. | |
| 4-Methylumbelliferyl 3,4,6-Tri-O-acetyl-β-D-galactopyranoside | 4-Methylumbelliferyl 3,4,6-Tri-O-acetyl-β-D-galactopyranoside, a common biomedical research substrate, detects β-galactosidase activity by enzymatic hydrolysis. The resultant 4-methylumbelliferone yields a fluorescent signature, useful in detecting lysosomal storage disease. Tay-Sachs and Sandhoff diseases, blighting β-galactosidase activity, prompt investigations reliant on the novel hydrolytic mechanism. Grades: 85%. Molecular formula: C22H24O11. Mole weight: 464.42. | |
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