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| Product | Description | |
|---|---|---|
| biuret amidohydrolase | Along with EC 3.5.2.15 (cyanuric acid amidohydrolase) and EC 3.5.1.54 (allophanate hydrolase), this enzyme forms part of thecyanuric-acid metabolism pathway, which degrades s-triazide herbicides, such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine], in bacteria.Urea-1-carboxylate rather than urea (as was thought previously) is the 2-nitrogen intermediate in cyanuric-acid metabolism in bacteria. The product, urea-1-carboxylate,can spontaneously decarboxylate under acidic conditions to form urea but, under physiological conditions, it can be converted into CO2 and ammonia by the action of EC 3.5.1.54. Group: Enzymes. Enzyme Commission Number: EC 3.5.1.84. CAS No. 95567-88-7. 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-4475; biuret amidohydrolase; EC 3.5.1.84; 95567-88-7. Cat No: EXWM-4475. |  |
| cyanuric acid amidohydrolase | Along with EC 3.5.1.54 (allophanate hydrolase) and EC 3.5.1.84 (biuret amidohydrolase), this enzyme forms part of the cyanuric-acid metabolism pathway, which degrades s-triazide herbicides, such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine], in bacteria. This is a key enzyme in the pathway, catalysing the ring cleavage of cyanuric acid. The enzyme is specific for cyanuric acid as substrate as neither the structurally related compounds ammeline (2,4-diamino-6-hydroxy-s-triazine) and ammelide (2-amino-4,6-dihydroxy-s-triazine) nor a number of pyrimidine compounds, such as uracil and cytosine, can act as substrates. Group: Enzymes. Synonyms: AtzD. Enzyme Commission Number: EC 3.5.2.15. CAS No. 132965-78-7. 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-4498; cyanuric acid amidohydrolase; EC 3.5.2.15; 132965-78-7; AtzD. Cat No: EXWM-4498. | |
| maleamate amidohydrolase | The reaction is involved in the aerobic catabolism of nicotinic acid. Group: Enzymes. Synonyms: NicF. Enzyme Commission Number: EC 3.5.1.107. 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-4386; maleamate amidohydrolase; EC 3.5.1.107; NicF. Cat No: EXWM-4386. | |
| N-acyl-aliphatic-L-amino acid amidohydrolase | Contains Zn2+. The enzyme is found in animals and is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate). It acts on mercapturic acids (S-conjugates of N-acetyl-L-cysteine) and neutral aliphatic N-acyl-α-amino acids. Some bacterial aminoacylases demonstrate substrate specificity of both EC 3.5.1.14 and EC 3.5.1.114. cf. EC 3.5.1.15, aspartoacylase and EC 3.5.1.114, N-acyl-aromatic-L-amino acid amidohydrolase. Group: Enzymes. Synonyms: aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α-N-acylaminoacid hydrolase; long acyl amidoa. Enzyme Commission Number: EC 3.5.1.14. CAS No. 9012-37-7. ACY1. 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-4403; N-acyl-aliphatic-L-amino acid amidohydrolase; EC 3.5.1.14; 9012-37-7; aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α-N-acylaminoacid hydrolase; long acyl amidoacylase; short acyl amidoacylase; ACY1 (gene name); N-acyl-L-amino-acid amidohydrolase. Cat No: EXWM-4403. | |
| N-acyl-aromatic-L-amino acid amidohydrolase | This enzyme is found in animals and is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate). It preferentially deacetylates Nα-acetylated aromatic amino acids and mercapturic acids (S-conjugates of N-acetyl-L-cysteine) that are usually not deacetylated by EC 3.5.1.14, N-acyl-aliphatic-L-amino acid amidohydrolase. The enzyme is significantly activated by Co2+ and Ni2+. Some bacterial aminoacylases demonstrate substrate specificity for both EC 3.5.1.14 and EC 3.5.1.114. cf. EC 3.5.1.14, N-acyl-aliphatic-L-amino acid amidohydrolase and EC 3.5.1.15, aspartoacylase. Group: Enzymes. Synonyms: aminoacylase 3; aminoacylase III; ACY3 (gene name). Enzyme Commission Number: EC 3.5.1.114. 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-4394; N-acyl-aromatic-L-amino acid amidohydrolase; EC 3.5.1.114; aminoacylase 3; aminoacylase III; ACY3 (gene name). Cat No: EXWM-4394. | |
| Native Microorganism Creatine Amidohydrolase | In enzymology, a creatinase (EC 3.5.3.3) is an enzyme that catalyzes the chemical reaction: creatine + H2O ?sarcosine + urea. Thus, the two substrates of this enzyme are creatine and H2O, whereas its two products are sarcosine and urea. The native enzyme was shown to be made up of two subunit monomers via SDS-polyacrylamide gel electrophoresis. Creatinase has been found to be most active at pH 8 and is most stable between ph 6-8 for 24 hrs. at 37 degrees. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. This enzyme participates in arginine and proline metabolism. 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: Creatine amidohydrolase; Creatinase; EC 3.5.3.3. Enzyme Commission Number: EC 3.5.3.3. CAS No. 37340-58-2. Mole weight: approx. 67 kDa (by gel filtration). Activity: 4.0 U/mg-solid or more. Appearance: White amorphous powder, lyophilized. Form: Freeze dried powder. Source: Microorganism. Creatine amidohydrolase; Creatinase; EC 3.5.3.3. Cat No: DIA-185. | |
| 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. | |
| peroxyureidoacrylate/ureidoacrylate amidohydrolase | The enzyme also shows activity towards ureidoacrylate. Part of the Rut pyrimidine catabolic pathway. Group: Enzymes. Synonyms: RutB. Enzyme Commission Number: EC 3.5.1.110. 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-4390; peroxyureidoacrylate/ureidoacrylate amidohydrolase; EC 3.5.1.110; RutB. Cat No: EXWM-4390. | |
| 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. | |
| ureidoglycolate amidohydrolase | This plant enzyme is involved in the degradation of ureidoglycolate, an intermediate of purine degradation. Not to be confused with EC 4.3.2.3, ureidoglycolate lyase, which releases urea rather than ammonia. Group: Enzymes. Synonyms: ureidoglycolate hydrolase; UAH (gene name). Enzyme Commission Number: EC 3.5.1.116. CAS No. 115629-07-7. 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-4396; ureidoglycolate amidohydrolase; EC 3.5.1.116; 115629-07-7; ureidoglycolate hydrolase; UAH (gene name). Cat No: EXWM-4396. | |
| 4-methyleneglutaminase | This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is 4-methylene-L-glutamine amidohydrolase. Other names in common use include 4-methyleneglutamine deamidase, and 4-methyleneglutamine amidohydrolase. This enzyme participates in c5-branched dibasic acid metabolism. Group: Enzymes. Synonyms: 4-methyleneglutamine deamidase; 4-methyleneglutamine amidohydrolase. Enzyme Commission Number: EC 3.5.1.67. CAS No. 86855-36-9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4457; 4-methyleneglutaminase; EC 3.5.1.67; 86855-36-9; 4-methyleneglutamine deamidase; 4-methyleneglutamine amidohydrolase. Cat No: EXWM-4457. | |
| 6-aminohexanoate-oligomer exohydrolase | The enzyme is involved in degradation of nylon-6 oligomers. It degrades linear oligomers of 6-aminohexanoate with a degree of polymerization of 2-20 by exo-type cleavage, removing residues sequentially from the N-terminus. Activity decreases with the increase of the polymerization number of the oligomer. cf. EC 3.5.1.117, 6-aminohexanoate-oligomer endohydrolase and EC 3.5.2.12, 6-aminohexanoate-cyclic-dimer hydrolase. Group: Enzymes. Synonyms: 6-aminohexanoate-dimer hydrolase; nylB (gene name); 6-aminohexanoic acid oligomer hydrolase (ambiguous); N-(6-aminohexanoyl)-6-aminohexanoate amidohydrolase; nylon-6 hydrolase (ambiguous). Enzyme Commission Number: EC 3.5.1.46. CAS No. 75216-15-8. 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-4434; 6-aminohexanoate-oligomer exohydrolase; EC 3.5.1.46; 75216-15-8; 6-aminohexanoate-dimer hydrolase; nylB (gene name); 6-aminohexanoic acid oligomer hydrolase (ambiguous); N-(6-aminohexanoyl)-6-aminohexanoate amidohydrolase; nylon-6 hydrolase (ambiguous). Cat No: EXWM-4434. | |
| acetylornithine deacetylase | Also hydrolyses N-acetylmethionine. Group: Enzymes. Synonyms: acetylornithinase; N-acetylornithinase; 2-N-acetyl-L-ornithine amidohydrolase. Enzyme Commission Number: EC 3.5.1.16. CAS No. 9025-12-1. 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-4405; acetylornithine deacetylase; EC 3.5.1.16; 9025-12-1; acetylornithinase; N-acetylornithinase; 2-N-acetyl-L-ornithine amidohydrolase. Cat No: EXWM-4405. | |
| acetylspermidine deacetylase | It was initially thought that N1-acetylspermidine was the substrate for this deacetylase reaction but this has since been disproved by Marchant et al. Group: Enzymes. Synonyms: N8-monoacetylspermidine deacetylase; N8-acetylspermidine deacetylase; N-acetylspermidine deacetylase; N1-acetylspermidine amidohydrolase (incorrect); 8-N-acetylspermidine amidohydrolase. Enzyme Commission Number: EC 3.5.1.48. CAS No. 67339-07-5. 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-4436; acetylspermidine deacetylase; EC 3.5.1.48; 67339-07-5; N8-monoacetylspermidine deacetylase; N8-acetylspermidine deacetylase; N-acetylspermidine deacetylase; N1-acetylspermidine amidohydrolase (incorrect); 8-N-acetylspermidine amidohydrolase. Cat No: EXWM-4436. | |
| aculeacin-A deacylase | This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. The systematic name of this enzyme class is aculeacin-A amidohydrolase. This enzyme is also called aculeacin A acylase. Group: Enzymes. Synonyms: aculeacin A acylase. Enzyme Commission Number: EC 3.5.1.70. CAS No. 121479-50-3. 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-4461; aculeacin-A deacylase; EC 3.5.1.70; 121479-50-3; aculeacin A acylase. Cat No: EXWM-4461. | |
| acylagmatine amidase | Also acts on acetylagmatine, propanoylagmatine and bleomycin B2. Group: Enzymes. Synonyms: acylagmatine amidohydrolase; acylagmatine deacylase. Enzyme Commission Number: EC 3.5.1.40. CAS No. 39419-74-4. 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-4429; acylagmatine amidase; EC 3.5.1.40; 39419-74-4; acylagmatine amidohydrolase; acylagmatine deacylase. Cat No: EXWM-4429. | |
| Acylase I from Aspergillus sp., Immobilized on Eupergit C | In enzymology, an aminoacylase (EC 3.5.1.14) is an enzyme that catalyzes the chemical reaction:N-acyl-L-amino acid + H2O<-> carboxylate + L-amino acid. Thus, the two substRates of this enzyme are N-acyl-L-amino acid and H2O, whereas its two products are carboxylate and L-amino acid. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. This enzyme participates in urea cycle and metabolism of amino groups. Moist pearls (dried substance ~30%, pearl diameter 50-100 μm), covalent fixation of the acylase. Group: Enzymes. Synonyms: aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α. Enzyme Commission Number: EC 3.5.1.14. CAS No. 9012-37-7. ACY1. Activity: > 50 U/g moist material. Storage: 2-8°C. Source: Aspergillus sp. aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α-N-acylaminoacid hydrolase; long acyl amidoacylase; short acyl amidoacylase; ACY1 (gene name); N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14; 9012-37-7. Cat No: NATE-0030. | |
| acyl-lysine deacylase | This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N6-acyl-L-lysine amidohydrolase. Other names in common use include epsilon-lysine acylase, and 6-N-acyl-L-lysine amidohydrolase. This enzyme participates in lysine degradation. Group: Enzymes. Synonyms: ε-lysine acylase; 6-N-acyl-L-lysine amidohydrolase. Enzyme Commission Number: EC 3.5.1.17. CAS No. 9025-11-0. 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-4406; acyl-lysine deacylase; EC 3.5.1.17; 9025-11-0; ε-lysine acylase; 6-N-acyl-L-lysine amidohydrolase. Cat No: EXWM-4406. | |
| Adenosine 3',5'-Bisphosphate Dicalcium Hydrate | Adenosine 3',5'-Bisphosphate Dicalcium Hydrate is a substrate for the amidohydrolase superfamily. Synonyms: Adenosine 3',5'-Diphosphate Dicalcium Hydrate; 3',5'-ADP Dicalcium Hydrate; 3',5'-Diphosphoadenosine Dicalcium Hydrate; 3'-Phosphoadenosine-5'-phosphate Dicalcium Hydrate; 3'-Phosphoryl-AMP Dicalcium Hydrate; A 3P5P; Adenosine 3',5'-bisphosphate Dicalcium Hydrate. Molecular formula: C10H27N5O18P2. Mole weight: 567.29. |  |
| adenosylcobinamide hydrolase | Involved in the salvage pathway of cobinamide in archaea. Archaea convert adenosylcobinamide (AdoCbi) into adenosylcobinamide phosphate (AdoCbi-P) in two steps. First, the amidohydrolase activity of CbiZ cleaves off the aminopropanol moiety of AdoCbi yielding adenosylcobyric acid (AdoCby); second, AdoCby is converted into AdoCbi-P by the action of EC 6.3.1.10, adenosylcobinamide-phosphate synthase (CbiB). Group: Enzymes. Synonyms: CbiZ; AdoCbi amidohydrolase. Enzyme Commission Number: EC 3.5.1.90. CAS No. 905988-16-1. 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-4482; adenosylcobinamide hydrolase; EC 3.5.1.90; 905988-16-1; CbiZ; AdoCbi amidohydrolase. Cat No: EXWM-4482. | |
| alanine carboxypeptidase | From soil bacteria. The enzyme from Corynebacterium equi also hydrolyses N-benzoylglycine and N-benzoyl-L-aminobutyric acid. Group: Enzymes. Synonyms: N-benzoyl-L-alanine-amidohydrolase. Enzyme Commission Number: EC 3.4.17.6. CAS No. 37288-70-3. 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-4079; alanine carboxypeptidase; EC 3.4.17.6; 37288-70-3; N-benzoyl-L-alanine-amidohydrolase. Cat No: EXWM-4079. | |
| allantoate deiminase | This enzyme is part of the ureide pathway, which permits certain organisms to recycle the nitrogen in purine compounds. This enzyme, which liberates ammonia from allantoate, is present in plants and bacteria. In plants it is localized in the endoplasmic reticulum. Requires manganese. Group: Enzymes. Synonyms: allantoate amidohydrolase. Enzyme Commission Number: EC 3.5.3.9. CAS No. 37289-13-7. 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-4535; allantoate deiminase; EC 3.5.3.9; 37289-13-7; allantoate amidohydrolase. Cat No: EXWM-4535. | |
| allantoinase | This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. The systematic name of this enzyme class is (S)-allantoin amidohydrolase. This enzyme participates in purine metabolism. Group: Enzymes. Enzyme Commission Number: EC 3.5.2.5. CAS No. 9025-20-1. 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-4507; allantoinase; EC 3.5.2.5; 9025-20-1. Cat No: EXWM-4507. | |
| allophanate hydrolase | Along with EC 3.5.2.15 (cyanuric acid amidohydrolase) and EC 3.5.1.84 (biuret amidohydrolase), this enzyme forms part of thecyanuric-acid metabolism pathway, which degrades s-triazide herbicides, such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine], in bacteria. The yeast enzyme (but not that from green algae) also catalyses the reaction of EC 6.3.4.6, urea carboxylase, thus bringing about the hydrolysis of urea to CO2 and NH3 in the presence of ATP and bicarbonate. The enzyme from Pseudomonas sp. strain ADP has a narrow substrate specificity, being unable to use the structurally analogous compounds urea, hydroxyurea or methylcarbamate as substrate. Group: Enzymes. Synonyms: allophanate lyase; AtzF; TrzF. Enzyme Commission Number: EC 3.5.1.54. CAS No. 9076-72-6. 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-4443; allophanate hydrolase; EC 3.5.1.54; 9076-72-6; allophanate lyase; AtzF; TrzF. Cat No: EXWM-4443. | |
| amidase | This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is acylamide amidohydrolase. Other names in common use include acylamidase, acylase, amidohydrolase, deaminase, fatty acylamidase, and N-acetylaminohydrolase. This enzyme participates in 6 metabolic pathways: urea cycle and metabolism of amino groups, phenylalanine metabolism, tryptophan metabolism, cyanoamino acid metabolism, benzoate degradation via coa ligation, and styrene degradation. Group: Enzymes. Synonyms: acylamidase; acylase (misleading); amidohydrolase (ambiguous); deaminase (ambiguous); fatty acylamidase; N-acetylaminohydrolase (ambiguous). Enzyme Commission Number: EC 3.5.1.4. CAS No. 9012-56-0. Amidase. 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-4428; amidase; EC 3.5.1.4; 9012-56-0; acylamidase; acylase (misleading); amidohydrolase (ambiguous); deaminase (ambiguous); fatty acylamidase; N-acetylaminohydrolase (ambiguous). Cat No: EXWM-4428. | |
| Amidase from Pseudomonas aeruginosa, Recombinant | The amidase from Pseudomonas aeruginosa catalyzes the hydrolysis of a small range of short aliphatic amides. Each amidase monomer is formed by a globular four-layer αββα sandwich domain with an additional 81-residue long C-terminal segment. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. Applications: The importance of these hydrolases in biotechnology is growing rapidly, because their potential applications span through chemical and pharmaceutical industries as well as in bioremediation. immobilized amidase can be used efficiently for production of ac...onyms: acylamidase; acylase (misleading); amidohydrolase (ambiguous); deaminase (ambiguous); fatty acylamidase; N-acetylaminohydrolase (ambiguous); amidase; EC 3.5.1.4; acylamide amidohydrolase. Enzyme Commission Number: EC 3.5.1.4. CAS No. 9012-56-0. Amidase. Activity: >200 units/mg protein (biuret). Storage: Store at -20°C. Form: Solution in 50% glycerol containing 7 mM 2-mercaptoethanol and phosphate buffer salt. Source: E. coli. Species: Pseudomonas aeruginosa. acylamidase; acylase (misleading); amidohydrolase (ambiguous); deaminase (ambiguous); fatty acylamidase; N-acetylaminohydrolase (ambiguous); amidase; EC 3.5.1.4; acylamide amidohydrolase. Cat No: NATE-0809. | |
| AminoAcylase-1 from Human, Recombinant | Aminoacylase-1 is a cytosolic, homodimeric, zinc-binding enzyme that catalyzes the hydrolysis of acylated L-amino acids to L-amino acids and acyl group, and has been postulated to function in the catabolism and salvage of acylated amino acids. ACY1 has been assigned to chromosome 3p21.1, a region reduced to homozygosity in small-cell lung cancer (SCLC), and its expression has been reported to be reduced or undetectable in SCLC cell lines and tumors. The amino acid sequence of human aminoacylase-1 is highly homologous to the porcine counterpart, and ACY1 is the first member of a new family of zinc-binding enzymes. Acy1 recombinant human produced in e. coli is a single, non-... SDS-PAGE. ACY1. Mole weight: 48 kDa. Stability: Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles. Appearance: Sterile Filtered clear solution. Source: E. coli. Species: Human. N-acyl-L-amino-acid amidohydrolase; ACY-1, ACY1D; ACYLASE; ACY1; aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α-N-acylaminoacid hydrolase; long acyl amidoacylase; short | |
| AminoAcylase (Industry grade) | In enzymology, an aminoacylase (EC 3.5.1.14) is an enzyme that catalyzes the chemical reaction:N-acyl-L-amino acid + H2O<-> carboxylate + L-amino acid. Thus, the two substRates of this enzyme are N-acyl-L-amino acid and H2O, whereas its two products are carboxylate and L-amino acid. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. This enzyme participates in urea cycle and metabolism of amino groups. Group: Enzymes. Enzyme Commission Number: EC 3.5.1.14. CAS No. 9012-37-7. Purity: 0.98. ACY1. Storage: at -4-25°C, dry, dark conditions for 3 years. Form: Lyophilized powder. aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α-N-acylaminoacid hydrolase; long acyl amidoacylase; short acyl amidoacylase; ACY1 (gene name); N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14; 9012-37-7. Cat No: NATE-1620. | |
| Arachidonoyl amide | Arachidonamide (AEA) is a weak cannabinoid CB1 and CB2 agonist. Arachidonamide was hydrolyzed by FAAH more effectively than AEA but exhibited significantly weaker binding to the human CB1 receptor with a Ki of 9.6 μM. AEA also inhibits rat glial gap junction cell-cell communication by 90% at a concentration of 20 μM. Arachidonamide are found to be the best substrates for anandamide amidohydrolase (AAH) with relative rates of hydrolysis about twice that of anandamide. Synonyms: Arachidonamide; Arachidonic acid amide; 5Z,8Z,11Z,14Z-eicosatetraenamide. Grades: ≥98%. CAS No. 85146-53-8. Molecular formula: C20H33NO. Mole weight: 303.5. | |
| Asparaginase from E. coli, Recombinant | Asparaginase (EC 3.5.1.1, USAN) or Colaspase (BAN) is an enzyme that catalyzes the hydrolysis of asparagine to aspartic acid. Asparaginases are enzymes expressed and produced by microorganisms. Group: Enzymes. Synonyms: EC 3.5.1.1; Asparaginase; Colaspase; L-asparaginase; L-asparagine amidohydrolase. Enzyme Commission Number: EC 3.5.1.1. CAS No. 9015-68-3. Asparaginase. Mole weight: ~ 37,900. Activity: ~ 15 U/mg. Stability: > 4 years at 4°C. Storage: 4°C. Form: In 2.5 M lithium sulphate. Source: E. coli. EC 3.5.1.1; Asparaginase; Colaspase; L-asparaginase; L-asparagine amidohydrolase. Cat No: NATE-1932. | |
| aspartoacylase | Aspartoacylase (EC 3.5.1.15, aminoacylase II, N-acetylaspartate amidohydrolase, acetyl-aspartic deaminase, acylase II, ASPA) is a hydrolase enzyme responsible for catalyzing the deacylation of N-acetyl-l-aspartate (N-acetylaspartate,NAA) into aspartate and acetate. It is a zinc-dependent hydrolase that promotes the deprotonation of water to use as a nucleophile in a mechanism analogous to many other zinc-dependent hydrolases. It is most commonly found in the brain, where it controls the levels of N-actetyl-l-aspartate. Group: Enzymes. Synonyms: aminoacylase II; N-acetylaspartate amidohydrolase; acetyl-aspartic deaminase; acylase II. Enzyme Commission Number: EC 3.5.1.15. CAS No. 9031-86-1. 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-4404; aspartoacylase; EC 3.5.1.15; 9031-86-1; aminoacylase II; N-acetylaspartate amidohydrolase; acetyl-aspartic deaminase; acylase II. Cat No: EXWM-4404. | |
| β-ureidopropionase | The animal enzyme also acts on β-ureidoisobutyrate. Group: Enzymes. Synonyms: N-carbamoyl-β-alanine amidohydrolase. Enzyme Commission Number: EC 3.5.1.6. CAS No. 9027-27-4. 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-4449; β-ureidopropionase; EC 3.5.1.6; 9027-27-4; N-carbamoyl-β-alanine amidohydrolase. Cat No: EXWM-4449. | |
| biotinidase | Also acts on biotin esters. Group: Enzymes. Synonyms: amidohydrolase biotinidase. Enzyme Commission Number: EC 3.5.1.12. CAS No. 9025-15-4. 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-4400; biotinidase; EC 3.5.1.12; 9025-15-4; amidohydrolase biotinidase. Cat No: EXWM-4400. | |
| choloylglycine hydrolase | Also acts on the 3α,12α-dihydroxy-derivative, and on choloyl-taurine. Group: Enzymes. Synonyms: glycocholase; bile salt hydrolase; choloyltaurine hydrolase; 3α,7α,12α-trihydroxy-5β-cholan-24-oylglycine amidohydrolase. Enzyme Commission Number: EC 3.5.1.24. CAS No. 37289-07-9. Choloylglycine Hydrolase. 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-4414; choloylglycine hydrolase; EC 3.5.1.24; 37289-07-9; glycocholase; bile salt hydrolase; choloyltaurine hydrolase; 3α,7α,12α-trihydroxy-5β-cholan-24-oylglycine amidohydrolase. Cat No: EXWM-4414. | |
| Creatinase from E. coli, Recombinant | In enzymology, a creatinase (EC 3.5.3.3) is an enzyme that catalyzes the chemical reaction:creatine + H2O? sarcosine + urea. Thus, the two substrates of this enzyme are creatine and H2O, whereas its two products are sarcosine and urea. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. Creatinase accelerates the conversion reaction of creatine and water molecule to sarcosine and urea. It always acts in homodimer state and is induced by choline chloride. Group: Enzymes. Synonyms: Creatine amidohydrolase; Creatinase; EC 3.5.3.3. Enzyme Commission Number: EC 3.5.3.3. CAS No. 37340-58-2. Mole weight: ca. 80 kDa. Activity: > 15 U/mg. Appearance: White lyophilizate. Storage: at -20°C. Source: E. coli. Species: E. coli. Creatine amidohydrolase; Creatinase; EC 3.5.3.3. Cat No: NATE-1241. | |
| creatininase | Creatininase is a member of the urease-related amidohydrolases, the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. The systematic name of this enzyme class is creatinine amidohydrolase. This enzyme is also called creatinine hydrolase. This enzyme participates in arginine and proline metabolism. Group: Enzymes. Synonyms: creatinine hydrolase. Enzyme Commission Number: EC 3.5.2.10. CAS No. 9025-13-2. Creatininase. 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-4493; creatininase; EC 3.5.2.10; 9025-13-2; creatinine hydrolase. Cat No: EXWM-4493. | |
| Creatininase from E. coli, Recombinant | 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. Group: Enzymes. Synonyms: EC 3.5.2.10, creatinine hydrolase; Creatininase; 9025-13-2. Enzyme Commission Number: EC 3.5.2.10. Mole weight: ca. 170 kDa. Activity: > 100 U/mg. Appearance: White lyophilizate. Storage: at -20°C. Source: E. coli. Species: E. coli. EC 3.5.2.10, creatinine hydrolase; Creatininase; 9025-13-2. Cat No: NATE-1242. | |
| Creatininase, Microorganism | Creatininase, Microorganism (Creatinine amidohydrolase; CAH), namely creatinine amidohydrolase, from Pseudomonas putida , is a homohexameric enzyme commonly used in biochemical research. Creatininase acts on carbon-nitrogen bonds other than peptide bonds, and can catalyze the hydrolysis of creatinine to creatine, which can then be metabolized by creatinase to urea and sarcosine [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: Creatinine amidohydrolase; CAH. CAS No. 9025-13-2. Pack Sizes: 1 KU. Product ID: HY-P2838. |  |
| D-galactarolactone isomerase | The enzyme, characterized from the bacterium Agrobacterium fabrum strain C58, belongs to the amidohydrolase superfamily. It participates in the degradation of D-galacturonate. Group: Enzymes. Synonyms: GLI. Enzyme Commission Number: EC 5.4.1.4. 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-5520; D-galactarolactone isomerase; EC 5.4.1.4; GLI. Cat No: EXWM-5520. | |
| D-glutaminase | This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is D-glutamine amidohydrolase. This enzyme participates in d-glutamine and d-glutamate metabolism and nitrogen metabolism. Group: Enzymes. Enzyme Commission Number: EC 3.5.1.35. CAS No. 37289-12-6. 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-4424; D-glutaminase; EC 3.5.1.35; 37289-12-6. Cat No: EXWM-4424. | |
| fatty acid amide hydrolase | Integral membrane protein, the enzyme is responsible for the catabolism of neuromodulatory fatty acid amides, including anandamide and oleamide, occurs in mammalia. Group: Enzymes. Synonyms: FAAH; oleamide hydrolase; anandamide amidohydrolase. Enzyme Commission Number: EC 3.5.1.99. 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-4491; fatty acid amide hydrolase; EC 3.5.1.99; FAAH; oleamide hydrolase; anandamide amidohydrolase. Cat No: EXWM-4491. | |
| formylaspartate deformylase | This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-formyl-L-aspartate amidohydrolase. This enzyme is also called formylaspartic formylase (formylase I, formylase II). This enzyme participates in histidine metabolism and glyoxylate and dicarboxylate metabolism. Group: Enzymes. Synonyms: formylaspartic formylase (formylase I, formylase II). Enzyme Commission Number: EC 3.5.1.8. CAS No. 9025-9-6. 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-4471; formylaspartate deformylase; EC 3.5.1.8; 9025-09-6; formylaspartic formylase (formylase I, formylase II). Cat No: EXWM-4471. | |
| formylmethionine deformylase | This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-formyl-L-methionine amidohydrolase. This enzyme participates in methionine metabolism and glyoxylate and dicarboxylate metabolism. Group: Enzymes. Enzyme Commission Number: EC 3.5.1.31. CAS No. 9032-86-4. 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-4421; formylmethionine deformylase; EC 3.5.1.31; 9032-86-4. Cat No: EXWM-4421. | |
| formyltetrahydrofolate deformylase | This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is 10-formyltetrahydrofolate amidohydrolase. This enzyme participates in glyoxylate and dicarboxylate metabolism and one carbon pool by folate. Group: Enzymes. Enzyme Commission Number: EC 3.5.1.10. CAS No. 9025-8-5. 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-4378; formyltetrahydrofolate deformylase; EC 3.5.1.10; 9025-08-5. Cat No: EXWM-4378. | |
| γ-glutamyl-γ-aminobutyrate hydrolase | Forms part of a putrescine-utilizing pathway in Escherichia coli, in which it has been hypothesized that putrescine is first glutamylated to form γ-glutamylputrescine, which is oxidized to 4-(γ-glutamylamino)butanal and then to 4-(γ-glutamylamino)butanoate. The enzyme can also catalyse the reactions of EC 3.5.1.35 (D-glutaminase) and EC 3.5.1.65 (theanine hydrolase). Group: Enzymes. Synonyms: γ-glutamyl-GABA hydrolase; PuuD; YcjL; 4-(γ-glutamylamino)butanoate amidohydrolase; 4-(L-γ-glutamylamino)butanoate amidohydrolase. Enzyme Commission Number: EC 3.5.1.94. 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-4486; γ-glutamyl-γ-aminobutyrate hydrolase; EC 3.5.1.94; γ-glutamyl-GABA hydrolase; PuuD; YcjL; 4-(γ-glutamylamino)butanoate amidohydrolase; 4-(L-γ-glutamylamino)butanoate amidohydrolase. Cat No: EXWM-4486. | |
| glutaminase | Glutaminase (EC 3.5.1.2, glutaminase I, L-glutaminase, glutamine aminohydrolase) is an amidohydrolase enzyme that generates glutamate from glutamine. Glutaminase has tissue-specific isoenzymes. Glutaminase has an important role in glial cells. Group: Enzymes. Synonyms: glutaminase I; L-glutaminase; glutamine aminohydrolase. Enzyme Commission Number: EC 3.5.1.2. CAS No. 9001-47-2. Glutaminase. 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-4409; glutaminase; EC 3.5.1.2; 9001-47-2; glutaminase I; L-glutaminase; glutamine aminohydrolase. Cat No: EXWM-4409. | |
| glutamin-(asparagin-)ase | The enzyme from the bacterium Achromobacter hydrolyses L-asparagine at 0.8 of the rate of L-glutamine; the D-isomers are also hydrolysed, but more slowly. cf. EC 3.5.1.2, glutaminase and EC 3.5.1.1, asparaginase. Group: Enzymes. Synonyms: glutaminase-asparaginase; ansB (gene name); L-asparagine/L-glutamine amidohydrolase; L-ASNase/L-GLNase. Enzyme Commission Number: EC 3.5.1.38. CAS No. 39335-03-0. 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-4426; glutamin-(asparagin-)ase; EC 3.5.1.38; 39335-03-0; glutaminase-asparaginase; ansB (gene name); L-asparagine/L-glutamine amidohydrolase; L-ASNase/L-GLNase. Cat No: EXWM-4426. | |
| glutathionylspermidine amidase | Spermidine is numbered so that atom N-1 is in the amino group of the aminopropyl part of the molecule. The enzyme from Escherichia coli is bifunctional and also catalyses the glutathionylspermidine synthase (EC 6.3.1.8) reaction, resulting in a net hydrolysis of ATP. Group: Enzymes. Synonyms: glutathionylspermidine amidohydrolase (spermidine-forming). Enzyme Commission Number: EC 3.5.1.78. CAS No. 171040-71-4. 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-4469; glutathionylspermidine amidase; EC 3.5.1.78; 171040-71-4; glutathionylspermidine amidohydrolase (spermidine-forming). Cat No: EXWM-4469. | |
| imidazolonepropionase | This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. The systematic name of this enzyme class is 3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate amidohydrolase. Other names in common use include 4(5)-imidazolone-5(4)-propionic acid hydrolase, and imidazolone propionic acid hydrolase. This enzyme participates in histidine metabolism. Group: Enzymes. Synonyms: 4(5)-imidazolone-5(4)-propionic acid hydrolase; imidazolone propionic acid hydrolase. Enzyme Commission Number: EC 3.5.2.7. CAS No. 9024-91-3. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4509; imidazolonepropionase; EC 3.5.2.7; 9024-91-3; 4(5)-imidazolone-5(4)-propionic acid hydrolase; imidazolone propionic acid hydrolase. Cat No: EXWM-4509. | |
| L-Aminoacylase (Crude Enzyme) | This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Synthesis; medicine. Group: Enzymes. Synonyms: aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α-N-acylaminoacid hydrolase; long acyl amidoacylase; short acyl amidoacylase; ACY1 (gene name); N-acyl-L-amino-acid amidohydrolase. Enzyme Commission Number: EC 3.5.1.14. CAS No. 9012-37-7. ACY1. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α-N-acylaminoacid hydrolase; long acyl amidoacylase; short acyl amidoacylase; ACY1 (gene name); N-acyl-L-amino-acid amidohydrolase. Pack: 100ml. Cat No: NATE-1835. | |
| 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-Asparaginase from Guinea pig, Recombinant | Asparaginase (EC 3.5.1.1, USAN) or Colaspase (BAN) is an enzyme that catalyzes the hydrolysis of asparagine to aspartic acid. Asparaginases are enzymes expressed and produced by microorganisms. Group: Enzymes. Synonyms: EC 3.5.1.1; Asparaginase; Colaspase; L-asparaginase; L-asparagine amidohydrolase. Enzyme Commission Number: EC 3.5.1.1. CAS No. 9015-68-3. Purity: >99% (SDS-PAGE). Asparaginase. Mole weight: ~63 kDa. Activity: > 1,400 IU/mg. Storage: at -80°C. Form: 25 mM Tris pH7.5, 500 mM NaCl, 2 mM DTT, 1 mM EDTA. Source: E. coli. Species: Guinea pig. EC 3.5.1.1; Asparaginase; Colaspase; L-asparaginase; L-asparagine amidohydrolase. Cat No: NATE-1577. | |
| L-proline amide hydrolase | L-proline amide hydrolase (EC 3.5.1.101) is an enzyme with systematic name (S)-piperidine-2-carboxamide amidohydrolase. Group: Enzymes. Synonyms: S-stereoselective piperazine-2-tert-butylcarboxamide hydrolase; LaaA; L-amino acid amidase. Enzyme Commission Number: EC 3.5.1.101. 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-4380; L-proline amide hydrolase; EC 3.5.1.101; S-stereoselective piperazine-2-tert-butylcarboxamide hydrolase; LaaA; L-amino acid amidase. Cat No: EXWM-4380. | |
| maleimide hydrolase | Succinimide and glutarimide, and sulfur-containing cyclic imides, such as rhodanine, can also act as substrates for the enzyme from Blastobacter sp. A17p-4. The reverse, cyclization, reaction is also catalysed, but much more slowly. It has lower activity towards cyclic ureides, which are the substrates of EC 3.5.2.2, dihydropyrimidinase. Group: Enzymes. Synonyms: imidase; cyclic imide hydrolase; cyclic-imide amidohydrolase (decyclicizing) [misprint]; cyclic-imide amidohydrolase (decyclizing). Enzyme Commission Number: EC 3.5.2.16. CAS No. 9030-74-4. 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-4499; maleimide hydrolase; EC 3.5.2.16; 9030-74-4; imidase; cyclic imide hydrolase; cyclic-imide amidohydrolase (decyclicizing) [misprint]; cyclic-imide amidohydrolase (decyclizing). Cat No: EXWM-4499. | |
| N4-(β-N-acetylglucosaminyl)-L-asparaginase | Acts only on asparagine-oligosaccharides containing one amino acid, i.e., the asparagine has free α-amino and α-carboxyl groups [cf. EC 3.5.1.52, peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase]. Group: Enzymes. Synonyms: aspartylglucosylamine deaspartylase; aspartylglucosylaminase; aspartylglucosaminidase; aspartylglycosylamine amidohydrolase; N-aspartyl-β-glucosaminidase; glucosylamidase; β-aspartylglucosylamine amidohydrolase; 4-N-(β-N-acetyl-D-glucosaminyl)-L-asparagine amidohydrolase. Enzyme Commission Number: EC 3.5.1.26. CAS No. 9075-24-5. 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-4416; N4-(β-N-acetylglucosaminyl)-L-asparaginase; EC 3.5.1.26; 9075-24-5; aspartylglucosylamine deaspartylase; aspartylglucosylaminase; aspartylglucosaminidase; aspartylglycosylamine amidohydrolase; N-aspartyl-β-glucosaminidase; glucosylamidase; β-aspartylglucosylamine amidohydrolase; 4-N-(β-N-acetyl-D-glucosaminyl)-L-asparagine amidohydrolase. Cat No: EXWM-4416. | |
| N-acetyldiaminopimelate deacetylase | This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N6-acetyl-LL-2,6-diaminoheptanedioate amidohydrolase. Other names in common use include N-acetyl-L-diaminopimelic acid deacylase, N-acetyl-LL-diaminopimelate deacylase, and 6-N-acetyl-LL-2,6-diaminoheptanedioate amidohydrolase. This enzyme participates in lysine biosynthesis. Group: Enzymes. Synonyms: N-acetyl-L-diaminopimelic acid deacylase; N-acetyl-LL-diaminopimelate deacylase; 6-N-acetyl-LL-2,6-diaminoheptanedioate amidohydrolase. Enzyme Commission Number: EC 3.5.1.47. CAS No. 99193-93-8. 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-4435; N-acetyldiaminopimelate deacetylase; EC 3.5.1.47; 99193-93-8; N-acetyl-L-diaminopimelic acid deacylase; N-acetyl-LL-diaminopimelate deacylase; 6-N-acetyl-LL-2,6-diaminoheptanedioate amidohydrolase. Cat No: EXWM-4435. | |
| N-acetylglucosamine-6-phosphate deacetylase | This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-acetyl-D-glucosamine-6-phosphate amidohydrolase. Other names in common use include acetylglucosamine phosphate deacetylase, acetylaminodeoxyglucosephosphate acetylhydrolase, and 2-acetamido-2-deoxy-D-glucose-6-phosphate amidohydrolase. This enzyme participates in aminosugars metabolism. Group: Enzymes. Synonyms: acetylglucosamine phosphate deacetylase; acetylaminodeoxyglucosephosphate acetylhydrolase; 2-acetamido-2-deoxy-D-glucose-6-phosphate amidohydrolase. Enzyme Commission Number: EC 3.5.1.25. CAS No. 9027-50-3. N-acetylglucosamine 6-phosphate deacetylase. 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-4415; N-acetylglucosamine-6-phosphate deacetylase; EC 3.5.1.25; 9027-50-3; acetylglucosamine phosphate deacetylase; acetylaminodeoxyglucosephosphate acetylhydrolase; 2-acetamido-2-deoxy-D-glucose-6-phosphate amidohydrolase. Cat No: EXWM-4415. | |
| N-acetylglucosamine 6-phosphate deacetylase from Bacillus subtilis, Recombinant | In enzymology, a N-acetylglucosamine-6-phosphate deacetylase (EC 3.5.1.25) is an enzyme that catalyzes the chemical reaction: N-acetyl-D-glucosamine 6-phosphate + H2O ? D-glucosamine 6-phosphate + acetate. Thus, the two substrates of this enzyme are N-acetyl-D-glucosamine 6-phosphate and H2O, whereas its two products are D-glucosamine 6-phosphate and acetate. Group: Enzymes. Synonyms: N-acetyl-D-glucosamine-6-phosphate amidohydrolase; acetylglucosamine phosphate deacetylase; acetylaminodeoxyglucosephosphate acetylhydrolase; 2-acetamido-2-deoxy-D-glucose-6-phosphate amidohydrolase; EC 3.5.1.25. Enzyme Commission Number: EC 3.5.1.25. CAS No. 9027-50-3. Purity: >90% as judged by SDS-PAGE. N-acetylglucosamine 6-phosphate deacetylase. Mole weight: 44.6 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: Bacillus subtilis. N-acetyl-D-glucosamine-6-phosphate amidohydrolase; acetylglucosamine phosphate deacetylase; acetylaminodeoxyglucosephosphate acetylhydrolase; 2-acetamido-2-deoxy-D-glucose-6-phosphate amidohydrolase; EC 3.5.1.25. Cat No: NATE-1541. | |
| N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli, Recombinant | In enzymology, a N-acetylglucosamine-6-phosphate deacetylase (EC 3.5.1.25) is an enzyme that catalyzes the chemical reaction: N-acetyl-D-glucosamine 6-phosphate + H2O ? D-glucosamine 6-phosphate + acetate. Thus, the two substrates of this enzyme are N-acetyl-D-glucosamine 6-phosphate and H2O, whereas its two products are D-glucosamine 6-phosphate and acetate. Group: Enzymes. Synonyms: N-acetyl-D-glucosamine-6-phosphate amidohydrolase; acetylglucosamine phosphate deacetylase; acetylaminodeoxyglucosephosphate acetylhydrolase; 2-acetamido-2-deoxy-D-glucose-6-phosphate amidohydrolase; EC 3.5.1.25. Enzyme Commission Number: EC 3.5.1.25. CAS No. 9027-50-3. Purity: >90% as judged by SDS-PAGE. N-acetylglucosamine 6-phosphate deacetylase. Mole weight: 43.0 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: Escherichia coli. N-acetyl-D-glucosamine-6-phosphate amidohydrolase; acetylglucosamine phosphate deacetylase; acetylaminodeoxyglucosephosphate acetylhydrolase; 2-acetamido-2-deoxy-D-glucose-6-phosphate amidohydrolase; EC 3.5.1.25. Cat No: NATE-1540. | |
| N-acetylglucosamine deacetylase | This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-acetyl-D-glucosamine amidohydrolase. Other names in common use include acetylaminodeoxyglucose acetylhydrolase, and N-acetyl-D-glucosaminyl N-deacetylase. This enzyme participates in aminosugars metabolism. Group: Enzymes. Synonyms: acetylaminodeoxyglucose acetylhydrolase; N-acetyl-D-glucosaminyl N-deacetylase. Enzyme Commission Number: EC 3.5.1.33. CAS No. 9012-32-2. 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-4423; N-acetylglucosamine deacetylase; EC 3.5.1.33; 9012-32-2; acetylaminodeoxyglucose acetylhydrolase; N-acetyl-D-glucosaminyl N-deacetylase. Cat No: EXWM-4423. | |
| N-Acyl-D-Amino-Acid Deacylase (Crude Enzyme) | This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Synthesis. Group: Enzymes. Synonyms: D-Aaase; D-Agase; D-Aminoacylase; D-Anase; N-Acyl-D-amino acid amidohydrolase; N-acyl-D-amino-acid deacylase; N-Acyl-D-aspartate amidohydrolase. Enzyme Commission Number: EC 3.5.1.81. CAS No. 65979-42-2. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. D-Aaase; D-Agase; D-Aminoacylase; D-Anase; N-Acyl-D-amino acid amidohydrolase; N-acyl-D-amino-acid deacylase; N-Acyl-D-aspartate amidohydrolase. Pack: 100ml. Cat No: NATE-1837. | |
| Native Aspergillus genus Acylase I | In enzymology, an aminoacylase (EC 3.5.1.14) is an enzyme that catalyzes the chemical reaction:N-acyl-L-amino acid + H2O<-> carboxylate + L-amino acid. Thus, the two substRates of this enzyme are N-acyl-L-amino acid and H2O, whereas its two products are carboxylate and L-amino acid. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. This enzyme participates in urea cycle and metabolism of amino groups. Group: Enzymes. Synonyms: aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α-N-acylaminoacid hydrolase; long acyl amidoacylase; short acyl amidoacylase; ACY1 (gene name); N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14; 9012-37-7. CAS No. 9012-37-7. ACY1. Storage: 0-10°C. Source: Aspergillus genus. aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α-N-acylaminoacid hydrolase; long acyl amidoacylase; short acyl amidoacylase; ACY1 (gene name); N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14; 9012-37-7. Cat No: NATE-1593. | |
| Native Aspergillus melleus Acylase I | In enzymology, an aminoacylase (EC 3.5.1.14) is an enzyme that catalyzes the chemical reaction:N-acyl-L-amino acid + H2O<-> carboxylate + L-amino acid. Thus, the two substRates of this enzyme are N-acyl-L-amino acid and H2O, whereas its two products are carboxylate and L-amino acid. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. This enzyme participates in urea cycle and metabolism of amino groups. Enzyme activity: the optimum temperature is 40-45 oc, the optimum ph is 8.0 (stable form ph 6-10). the enzyme is activated by cocl2 in the range of 10-4 to 10-3 m. Group: Enzymes. Synonyms: aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; . Enzyme Commission Number: EC 3.5.1.14. CAS No. 9012-37-7. ACY1. Activity: >0.5 units/mg. Storage: 2-8°C. Form: powder. Source: Aspergillus melleus. aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α-N-acylaminoacid hydrolase; long acyl amidoacylase; short acyl amidoacylase; ACY1 (gene name); N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14; 9012-37-7. Cat No: NATE-0029. | |
| Native Clostridium perfringens (C. welchII) Choloylglycine Hydrolase | Choloylglycine hydrolase (EC 3.5.1.24) is an N-terminal nucleophilic (Ntn) hydrolase that catalyzes the hydrolysis of amide bonds, libeRates the glycine/taurine moiety from the steroid core and eventually yields unconjugated bile acids. Agents that oxidize thiol groups (e.g., p-mercuribenzoate, iodoacetamide, Hg2+, Cu2+, and Cd2+) have been shown to strongly inhibit bile salt hydrolase (BSH) activity in Clostridium perfringens. Applications: The enzyme from creative enzymes has been used in the analysis of bile samples in various studies. Group: Enzymes. Synonyms: EC 3.5.1.24; glycocholase; bile salt hydrolase; choloyltaurine hydrolase; 3α,7α,12α-trihydroxy-5β-cholan-24-oylglycine amidohydrolase; 37289-07-9. Enzyme Commission Number: EC 3.5.1.24. CAS No. 37289-07-9. Choloylglycine Hydrolase. Activity: > 100 units/mg protein. Storage: -20°C. Form: lyophilized powder. Partially purified lyophilized powder containing buffer salts and stabilizer. Source: Clostridium perfringens (C. welchII). EC 3.5.1.24; glycocholase; bile salt hydrolase; choloyltaurine hydrolase; 3α,7α,12α-trihydroxy-5β-cholan-24-oylglycine amidohydrolase; 37289-07-9. Cat No: NATE-0129. | |
| Native E. coli N-Carbamoylsarcosine Amidase | In enzymology, a N-carbamoylsarcosine amidase is an enzyme that catalyzes the chemical reaction: N-carbamoylsarcosine + H2O rightleftharpoons sarcosine + CO2 + NH3. Thus, the two substrates of this enzyme are N-carbamoylsarcosine and H2O, whereas its 3 products are sarcosine, CO2, and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. This enzyme participates in arginine and proline metabolism. Hydrolase that catalyzes the interconversion of n-carbamoylsarcosine to sarcosine. Applications: Use n-carbamoylsarcosine amidase in diagnostic tests for the determination of creatinine in combination with creatinine deaminase, n-methylhydantoinase (atp-hydrolysing) and sarcosine oxidase. Group: Enzymes. Synonyms: N-carbamoylsarcosine amidase; N-carbamoylsarcosine amidohydrolase; carbamoylsarcosine amidase. CAS No. 92767-52-7. N-Carbamoylsarcosine Amidase. Activity: 0.80-1.30 U/mg. Stability: At -15 to -25°C within specification range for 12 months. Store dry. Protect from light. Appearance: White lyophilizate. Source: E. coli. Species: E. coli. N-carbamoylsarcosine amidase; N-carbamoylsarcosine amidohydrolase; carbamoylsarcosine amidase. Cat No: NATE-0876. | |
| Native Escherichia coli Asparaginase | Asparaginase (EC 3.5.1.1, USAN) or Colaspase (BAN) is an enzyme that catalyzes the hydrolysis of asparagine to aspartic acid. Asparaginases are enzymes expressed and produced by microorganisms. Applications: Asparaginase is used in enzymatic assays and to convert asparagine to aspartic acid. asparaginase is used to reduce the formation of acrylamide in starchy food products. it is also used as a chemotherapy agent for acute lymphoblastic leukemia. product is from escherichia coli and is provided as a lyophilized powder containing sodium chloride. Group: Enzymes. Synonyms: EC 3.5.1.1; Asparaginase; Colaspase; L-asparaginase; L-asparagine amidohydrolase. Enzyme Commission Number: EC 3.5.1.1. CAS No. 9015-68-3. Asparaginase. Storage: 2-8°C. Form: lyophilized powder. Source: Escherichia coli. EC 3.5.1.1; Asparaginase; Colaspase; L-asparaginase; L-asparagine amidohydrolase. Cat No: PHAM-226. | |
| Native Escherichia coli Glutaminase | Glutaminase catalyzes the conversion of glutamine to glutamate. Glutaminase is an amidohydrolase enzyme that generates glutamate from glutamine. Glutaminase has tissue-specific isoenzymes. Glutaminase has an important role in glial cells. Glutaminase catalyzes the following reaction:Glutamine + H2O ? Glutamate + NH3. Group: Enzymes. Synonyms: EC 3.5.1.2; glutaminase I; L-glutaminase; glutamine aminohydrolase; Glutaminase; 9001-47-2. Enzyme Commission Number: EC 3.5.1.2. CAS No. 9001-47-2. Glutaminase. Activity: Type I, 500-1,500 units/mg protein; Type II, 50-200 units/mg protein. Storage: -20°C. Form: Type I, Lyophilized powder containing stabilizer and potassium succinate; Type II, Lyophilized powder containing potassium succinate and EDTA. Source: Escherichia coli. EC 3.5.1.2; glutaminase I; L-glutaminase; glutamine aminohydrolase; Glutaminase; 9001-47-2. Cat No: NATE-0307. | |
| Native H. pylori Urease | Ureases (EC 3.5.1.5), functionally, belong to the superfamily of amidohydrolases and phosphotriesterases. It is an enzyme that catalyzes the hydrolysis of urea into carbon dioxide and ammonia. The reaction occurs as follows: (NH2)2CO + H2O ? CO2 + 2NH3. Applications: Specific methodologies have not been tested using this product. Group: Enzymes. Synonyms: EC 3.5.1.5; Urease. Enzyme Commission Number: EC 3.5.1.5. CAS No. 9002-13-5. Purity: Sephadex G200 Purified. SDS-PAGE analysis with 30KD and 66KD. Urease. Form: Antigen Grade, Liquid. Source: H. pylori. EC 3.5.1.5; Urease. Cat No: PHAM-179. | |
| Native Jack bean Urease | Ureases (EC 3.5.1.5), functionally, belong to the superfamily of amidohydrolases and phosphotriesterases. It is an enzyme that catalyzes the hydrolysis of urea into carbon dioxide and ammonia. The reaction occurs as follows: (NH2)2CO + H2O ? CO2 + 2NH3. Applications: This enzyme is useful for enzymatic determination of urea in clinical analysis. Group: Enzymes. Synonyms: EC 3.5.1.5; Urease. Enzyme Commission Number: EC 3.5.1.5. CAS No. 9002-13-5. Activity: 100U/mg-solid or more. Appearance: White amorphous powder, lyophilized. Form: Freeze dried powder. Source: Jack bean. EC 3.5.1.5; Urease. Cat No: PHAM-180. | |
| 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. | |
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