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| Product | Description | |
|---|---|---|
| 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. |  |
| 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. | |
| 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. | |
| 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. | |
| 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. | |
| 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. | |
| 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. | |
| 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. | |
| 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. | |
| 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. | |
| 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. | |
| 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-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 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 Porcine 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. Protein determined by biuret. Applications: Acylase i from porcine kidney has been used to study the acylase i-catalyzed deacetylation of various s-alkyl-n-acetyl-l-cysteines and their carb...ort acyl amidoacylase; ACY1 (gene name); N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14; 9012-37-7. Enzyme Commission Number: EC 3.5.1.14. CAS No. 9012-37-7. ACY1. Activity: > 2,000 units/mg protein; 500-1,500 units/mg protein. Storage: -20°C. Form: lyophilized powder. Source: Porcine kidney. Species: Porcine. 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-0031. | |
| N-benzyloxycarbonylglycine hydrolase | Also acts, more slowly, on N-benzyloxycarbonylalanine, but not on the corresponding derivatives of other amino acids or on N-benzyloxycarbonylpeptides. Requires Co2+ or Zn2+. cf. EC 3.5.1.64, Nα-benzyloxycarbonylleucine hydrolase. Group: Enzymes. Synonyms: benzyloxycarbonylglycine hydrolase; Nα-carbobenzoxyamino acid amidohydrolase; Nα-benzyloxycarbonyl amino acid urethane hydrolase; Nα-benzyloxycarbonyl amino acid urethane hydrolase I. Enzyme Commission Number: EC 3.5.1.58. CAS No. 91930-69-7. 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-4447; N-benzyloxycarbonylglycine hydrolase; EC 3.5.1.58; 91930-69-7; benzyloxycarbonylglycine hydrolase; Nα-carbobenzoxyamino acid amidohydrolase; Nα-benzyloxycarbonyl amino acid urethane hydrolase; Nα-benzyloxycarbonyl amino acid urethane hydrolase I. Cat No: EXWM-4447. | |
| N-carbamoyl-D-amino-acid hydrolase | This enzyme, along with EC 3.5.1.87 (N-carbamoyl-L-amino-acid hydrolase), EC 5.1.99.5 (hydantoin racemase) and hydantoinase, forms part of the reaction cascade known as the "hydantoinase process", which allows the total conversion of D,L-5-monosubstituted hydantoins into optically pure D- or L-amino acids. It has strict stereospecificity for N-carbamoyl-D-amino acids and does not act upon the corresponding L-amino acids or on the N-formyl amino acids, N-carbamoyl-sarcosine, -citrulline, -allantoin and -ureidopropanoate, which are substrates for other amidohydrolases. Group: Enzymes. Synonyms: D-N-carbamoylase; N-carbamoylase (ambiguous); N-carbamoyl-D-amino acid hydrolase. Enzyme Commission Number: EC 3.5.1.77. CAS No. 71768-08-6. 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-4468; N-carbamoyl-D-amino-acid hydrolase; EC 3.5.1.77; 71768-08-6; D-N-carbamoylase; N-carbamoylase (ambiguous); N-carbamoyl-D-amino acid hydrolase. Cat No: EXWM-4468. | |
| N-carbamoyl-L-amino-acid hydrolase | This enzyme, along with EC 3.5.1.77 (N-carbamoyl-D-amino-acid hydrolase), EC 5.1.99.5 (hydantoin racemase) and hydantoinase, forms part of the reaction cascade known as the "hydantoinase process", which allows the total conversion of D,L-5-monosubstituted hydantoins into optically pure D- or L-amino acids. The enzyme from Alcaligenes xylosoxidans has broad specificity for carbamoyl-L-amino acids, although it is inactive on the carbamoyl derivatives of glutamate, aspartate, arginine, tyrosine or tryptophan. The enzyme from Sinorhizobium meliloti requires a divalent cation for activity and can hydrolyse N-carbamoyl-L-tryptophan as well as N-carbamoyl L-amino acids with aliphatic substituents. The enzymeis inactive on derivatives of D-amino acids. In addition to N-carbamoyl L-amino acids, the enzyme can also hydrolyse formyl and acetyl derivatives to varying degrees. Group: Enzymes. Synonyms: N-carbamyl L-amino acid amidohydrolase; N-carbamoyl-L-amino acid amidohydrolase; L-N-car. Enzyme Commission Number: EC 3.5.1.87. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4478; N-carbamoyl-L-amino-acid hydrolase; EC 3.5.1.87; N-carbamyl L-amino acid amidohydrolase; N-carbamoyl-L-amino acid amidohydrolase; L-N-carbamoylase; N-carbamoylase (ambiguous). Cat No: EXWM-4478. | |
| PDP-EA | PDP-EA, an activator of fatty acid amide hydrolase (FAAH) from plant and mammalian species, is a FAAH activator, which is proposed to enhance amidohydrolase activity of FAAH by reducing negative feedback mechanisms. Synonyms: N-(2-Hydroxyethyl)-2-(3-pentadecylphenoxy)acetamide. Grades: ≥98% by HPLC. CAS No. 861891-72-7. Molecular formula: C25H43NO3. Mole weight: 405.61. | |
| succinyl-diaminopimelate desuccinylase | 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-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase. This enzyme is also called N-succinyl-L-alpha,epsilon-diaminopimelic acid deacylase. This enzyme participates in lysine biosynthesis. Group: Enzymes. Synonyms: N-succinyl-L-α,ε-diaminopimelic acid deacylase. Enzyme Commission Number: EC 3.5.1.18. CAS No. 9024-94-6. 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-4407; succinyl-diaminopimelate desuccinylase; EC 3.5.1.18; 9024-94-6; N-succinyl-L-α,ε-diaminopimelic acid deacylase. Cat No: EXWM-4407. | |
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