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| Product | Description | |
|---|---|---|
| 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 | Amidases, a member of nitrilase superfamily, catalyzes the hydrolysis of an amide, leading to the formation of carboxylic acid and ammonia. Amidases contain a conserved stretch of approximately 130 amino acids known as the AS sequence, and play a role in important metabolic processes [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 9012-56-0. Pack Sizes: 250 U; 1 KU. Product ID: HY-P2736. |  |
| 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. | |
| Amidases | synthesis of chiral carboxylic acids and amides. Group: Enzymes. Synonyms: Amidases; AMD. Form: 1. Enzyme Powder: 18 items*50mg / item, or other quantity2. Screening Kit: 18 items*1mg / item. Amidases; AMD; Screening Kit; library of enzyme; enzyme library. Cat No: ENLC-003. | |
| 2-oxoglutaramate amidase | The enzyme, which is highly specific for its substrate, participates in the nicotine degradation pathway of several Gram-positive bacteria. Group: Enzymes. Synonyms: ω-amidase (ambiguous). Enzyme Commission Number: EC 3.5.1.111. 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-4391; 2-oxoglutaramate amidase; EC 3.5.1.111; ω-amidase (ambiguous). Cat No: EXWM-4391. | |
| 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. | |
| carnitinamidase | Does not act on D-carnitinamide. Group: Enzymes. Synonyms: L-carnitinamidase; carnitine amidase; L-carnitine amidase. Enzyme Commission Number: EC 3.5.1.73. CAS No. 117444-04-9. 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-4464; carnitinamidase; EC 3.5.1.73; 117444-04-9; L-carnitinamidase; carnitine amidase; L-carnitine amidase. Cat No: EXWM-4464. | |
| D-benzoylarginine-4-nitroanilide amidase | This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. Group: Enzymes. Synonyms: benzoyl-D-arginine arylamidase; D-BAPA-ase. Enzyme Commission Number: EC 3.5.1.72. CAS No. 119345-26-5. 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-4463; D-benzoylarginine-4-nitroanilide amidase; EC 3.5.1.72; 119345-26-5; benzoyl-D-arginine arylamidase; D-BAPA-ase. Cat No: EXWM-4463. | |
| 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. | |
| mandelamide 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 mandelamide hydrolase. This enzyme is also called Pseudomonas mandelamide hydrolase. Group: Enzymes. Synonyms: Pseudomonas mandelamide hydrolase. Enzyme Commission Number: EC 3.5.1.86. 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-4477; mandelamide amidase; EC 3.5.1.86; Pseudomonas mandelamide hydrolase. Cat No: EXWM-4477. | |
| mycothiol S-conjugate amidase | The enzyme that is found in actinomycetes is involved in the detoxification of oxidizing agents and electrophilic antibiotics. The enzyme has low activity with 1-O-(2-acetamido-2-deoxy-α-D-glucopyranosyl)-1D-myo-inositol as substrate (cf. EC 3.5.1.103, N-acetyl-1-D-myo-inositol-2-amino-2-deoxy-α-D-glucopyranoside deacetylase). Group: Enzymes. Synonyms: MCA. Enzyme Commission Number: EC 3.5.1.115. 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-4395; mycothiol S-conjugate amidase; EC 3.5.1.115; MCA. Cat No: EXWM-4395. | |
| N-acetylmuramoyl-L-alanine amidase | This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. This enzyme participates in peptidoglycan biosynthesis. Autolysins and some phage lysins are examples of N-acetylmuramoyl-L-alanine amidases. Group: Enzymes. Synonyms: acetylmuramyl-L-alanine amidase; N-acetylmuramyl-L-alanine amidase; N-acylmuramyl-L-alanine amidase; acetylmuramoyl-alanine amidase; N-acetylmuramic acid L-alanine amidase; acetylmuramyl-alanine amidase; N-acetylmuramylalanine amidase; murein hydrolase; N-acetylmuramoyl-L-alanine amidase type I; N-acetylmuramoyl-L-alanine amidase type II. Enzyme Commission Number: EC 3.5.1.28. CAS No. 9013-25-6. 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-4417; N-acetylmuramoyl-L-alanine amidase; EC 3.5.1.28; 9013-25-6; acetylmuramyl-L-alanine amidase; N-acetylmuramyl-L-alanine amidase; N-acylmuramyl-L-alanine amidase; acetylmuramoyl-alanine amidase; N-acetylmuramic acid L-alanine amidase; acetylmuramyl-alanine amidase; N-acetylmuramylalanine amidase; murein hydrolase; N-acetylmuramoyl-L-alanine amidase type I; N-acetylmuramoyl-L-alanine amidase type II. Cat No: EXWM-4417. | |
| N-acetylmuramoyl-L-alanine amidase L2 | N-Acetylmuramoyl-l-alanine amidases are peptidoglycan hydrolases with the specificity to cleave the amide bond between the lactyl group of the muramic acid and the α-amino group of l-alanine, and are able to cause dissolution of the peptidoglycan structure and thus do not exhibit peptidase activity. Synonyms: NAMAA L2. |  |
| 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 Penicillin Amidase | The biosynthesis of Penicillin amidase in E. coli by hydrophobic protein chromatography is an inducible reaction which is regulated by metabolized carbon source (e.g. polyols, carboxylic acid etc.). It is also influenced by catabolite repression. It catalyzes the formation of amide bonds through an acyl-enzyme intermediate. Penicillin amidase is a periplasmic 80k heterodimer with a and b chains (209 and 566 amino acids, respectively). it is widely distributed among microorganisms, including bacteria, yeast and filamentous fungi. among all the sources, the enzyme produced by e. coli is most well-characterized and common for industrial application. Applications: Penicillin...; benzylpenicillin acylase; novozym 217; semacylase; α-acylamino-β-lactam acylhydrolase; ampicillin acylase; EC 3.5.1.11; 9014-06-6. Enzyme Commission Number: EC 3.5.1.11. CAS No. 9014-6-6. Penicillin Amidase. Mole weight: Mr ~70 kDa. Activity: Type I, 5-10 units/mg protein; Type II, > 10 units/mg protein (E1%/280). Storage: 2-8°C. Form: Type II, ammonium sulfate suspension, Suspension in 0.1 M phosphate, pH 7.5 and 3 M ammonium sulfate. Source: Escherichia coli. penicillin amidase; penicillin acylase; benzylpenicillin acylase; novozym 217; semacylase; α-acylamino-β-lactam acylhydrolase; ampicillin acylase; EC 3.5.1.11; 9014-06-6. Cat No: NATE-0541. | |
| N-carbamoylputrescine 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 N-carbamoylputrescine amidohydrolase. Other names in common use include carbamoylputrescine hydrolase, and NCP. This enzyme participates in urea cycle and metabolism of amino groups. Group: Enzymes. Synonyms: carbamoylputrescine hydrolase; NCP. Enzyme Commission Number: EC 3.5.1.53. CAS No. 85030-69-9. 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-4442; N-carbamoylputrescine amidase; EC 3.5.1.53; 85030-69-9; carbamoylputrescine hydrolase; NCP. Cat No: EXWM-4442. | |
| N-carbamoylsarcosine 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 N-carbamoylsarcosine amidohydrolase. This enzyme is also called carbamoylsarcosine amidase. This enzyme participates in arginine and proline metabolism. Group: Enzymes. Synonyms: carbamoylsarcosine amidase. Enzyme Commission Number: EC 3.5.1.59. CAS No. 92767-52-7. 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-4448; N-carbamoylsarcosine amidase; EC 3.5.1.59; 92767-52-7; carbamoylsarcosine amidase. Cat No: EXWM-4448. | |
| nicotinamidase | 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 nicotinamide amidohydrolase. Other names in common use include nicotinamide deaminase, nicotinamide amidase, and YNDase. This enzyme participates in nicotinate and nicotinamide metabolism. Group: Enzymes. Synonyms: nicotinamide deaminase; nicotinamide amidase; YNDase. Enzyme Commission Number: EC 3.5.1.19. CAS No. 9033-32-3. 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-4408; nicotinamidase; EC 3.5.1.19; 9033-32-3; nicotinamide deaminase; nicotinamide amidase; YNDase. Cat No: EXWM-4408. | |
| nicotinamide-nucleotide amidase | Also acts more slowly on β-nicotinamide D-ribonucleoside. Group: Enzymes. Synonyms: NMN deamidase; nicotinamide mononucleotide deamidase; nicotinamide mononucleotide amidohydrolase. Enzyme Commission Number: EC 3.5.1.42. CAS No. 37355-58-1. 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-4431; nicotinamide-nucleotide amidase; EC 3.5.1.42; 37355-58-1; NMN deamidase; nicotinamide mononucleotide deamidase; nicotinamide mononucleotide amidohydrolase. Cat No: EXWM-4431. | |
| ω-amidase | Acts on glutaramate, succinamate and their 2-oxo derivatives. Group: Enzymes. Synonyms: α-keto acid-ω-amidase. Enzyme Commission Number: EC 3.5.1.3. CAS No. 9025-19-8. 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-4419; ω-amidase; EC 3.5.1.3; 9025-19-8; α-keto acid-ω-amidase. Cat No: EXWM-4419. | |
| penicillin 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 penicillin amidohydrolase. Other names in common use include penicillin acylase, benzylpenicillin acylase, novozym 217, semacylase, alpha-acylamino-beta-lactam acylhydrolase, and ampicillin acylase. This enzyme participates in penicillin and cephalosporin biosynthesis. Group: Enzymes. Synonyms: penicillin acylase; benzylpenicillin acylase; novozym 217; semacylase; α-acylamino-β-lactam acylhydrolase; ampicillin acylase. Enzyme Commission Number: EC 3.5.1.11. CAS No. 9014-6-6. Penicillin 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-4389; penicillin amidase; EC 3.5.1.11; 9014-06-6; penicillin acylase; benzylpenicillin acylase; novozym 217; semacylase; α-acylamino-β-lactam acylhydrolase; ampicillin acylase. Cat No: EXWM-4389. | |
| Penicillin amidase | Penicillin amidase is an enzyme used commercially for the production of semisynthetic penicillins. Synonyms: Amidase, penicillin; E.C. 3.5.1.11; Penicillin acylase; Benzylpenicillin acylase; Penicillin V acylase; Acylase, penicillin; Penicillin amidohydrolase; Penicillin G acylase. Grades: Activity wet form: 160U/g; Water content: 45%~60%. CAS No. 9014-6-6. | |
| Penicillin amidase, E. coli | Penicillin amidase (EC 3.5.1.11) (Penicillin acylase) is an enzyme that cleaves the acyl side chains of penicillins. Penicillin amidase can be used for the production of 6-aminopenicillanic acid. Penicillin amidase can also be used in the resolution of racemic mixtures, peptide synthesis, and synthesis of semi-synthetic β-lactam antibiotics [1] [2] [3]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: PGA. CAS No. 9014-6-6. Pack Sizes: 100 mg; 250 mg. Product ID: HY-P2834. | |
| peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase | Does not act on (GlcNAc)Asn, because it requires the presence of more than two amino-acid residues in the substrate [cf. EC 3.5.1.26, N4-(β-N-acetylglucosaminyl)-L-asparaginase]. The plant enzyme was previously erroneously listed as EC 3.2.2.18. Group: Enzymes. Synonyms: glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; Jack-bean glycopeptidase; PNGase A; PNGase F. Enzyme Commission Number: EC 3.5.1.52. CAS No. 83534-39-8. PNGase F. 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-4441; peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase; EC 3.5.1.52; 83534-39-8; glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; Jack-bean glycopeptidase; PNGase A; PNGase F. Cat No: EXWM-4441. | |
| peptidyl-glycinamidase | Inactivates vasopressin and oxytocin by splitting off glycinamide. Also cleaves ester substrates of trypsin and chymotrypsin. Although glycinamide is by far the preferred leaving group, other aminoacylamides may also be released, e.g. phenylalaninamide. The toad skin enzyme is inhibited by diisopropyl fluorophosphate. Group: Enzymes. Synonyms: carboxyamidase; peptidyl carboxy-amidase; peptidyl-aminoacylamidase; carboxamidopeptidase; peptidyl amino acid amide hydrolase. Enzyme Commission Number: EC 3.4.19.2. CAS No. 94047-14-0. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4087; peptidyl-glycinamidase; EC 3.4.19.2; 94047-14-0; carboxyamidase; peptidyl carboxy-amidase; peptidyl-aminoacylamidase; carboxamidopeptidase; peptidyl amino acid amide hydrolase. Cat No: EXWM-4087. | |
| phthalyl amidase | In the entry, "phthalyl" is used to mean "2-carboxybenzoyl". The enzyme from Xanthobacter agilis hydrolyses phthalylated amino acids, peptides, β-lactams, aromatic and aliphatic amines. The substituent on nitrogen may be an alkyl group, but may also be complex, giving an amino acid or peptide derivative. Substitutions on the phthalyl ring include 6-F, 6-NH2, 3-OH, and a nitrogen in the aromatic ring ortho to the carboxy group attached to the amine. No cofactors are required. Group: Enzymes. Enzyme Commission Number: EC 3.5.1.79. CAS No. 169150-79-2. 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-4470; phthalyl amidase; EC 3.5.1.79; 169150-79-2. Cat No: EXWM-4470. | |
| (R)-amidase | In addition (R)-piperidine-3-carboxamide is hydrolysed to (R)-piperidine-3-carboxylic acid and NH3, and (R)-N-tert-butylpiperazine-2-carboxamide is hydrolysed to (R)-piperazine-2-carboxylic acid and tert-butylamine with lower activity. The enzyme does not act on the other amide substrates which are hydrolysed by EC 3.5.1.4 (amidase). Group: Enzymes. Synonyms: R-stereospecific amidase; R-amidase. Enzyme Commission Number: EC 3.5.1.100. 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-4379; (R)-amidase; EC 3.5.1.100; R-stereospecific amidase; R-amidase. Cat No: EXWM-4379. | |
| (1R) -2, 2-Di methyl cyclopropane carboxamide | (1R) -2, 2-Di methyl cyclopropane carboxamide is involved in the screening system for active and enantioselective amidase based on its acyl transfer. Group: Biochemicals. Grades: Highly Purified. CAS No. 106462-18-4. Pack Sizes: 50mg, 100mg. Molecular Formula: C6H11NO, Molecular Weight: 113.16. US Biological Life Sciences. |  Worldwide |
| 6-Bn-cAMP | 6-Bn-cAMP is a selective stimulator of cAMP-dependent protein kinase which does not activate Epac. Compared to cAMP, it has superior stability against PDE, esterases, amidases and higher membrane permeability. Grades: ≥ 98% by HPLC. CAS No. 32115-08-5. Molecular formula: C17H17N5O6P · Na. Mole weight: 441.3. | |
| AACOCF | AACOCF, an anlogue of arachidonic acid, is a slow-binding inhibitor of cytosolic (85 kDa) phospholipase A2. It also inhibits fatty acid amide hydrolase (FAAH, anandamide amidase) in vitro. Synonyms: 1,1,1-Trifluoro-6Z,9Z,12Z,15Z-heneicosateraen-2-one; Arachidonyl trifluoromethyl ketone; Arachidonyltrifluoromethane. CAS No. 149301-79-1. Molecular formula: C21H31F3O. Mole weight: 356.47. | |
| acrosin | Occurs in spermatozoa; formed from proacrosin by limited proteolysis. Inhibited by naturally occurring trypsin inhibitors. In peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: acrosomal proteinase; acrozonase; α-acrosin; β-acrosin; upsilon-acrosin; acrosomal protease; acrosin amidase. Enzyme Commission Number: EC 3.4.21.10. CAS No. 9068-57-9. 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-4094; acrosin; EC 3.4.21.10; 9068-57-9; acrosomal proteinase; acrozonase; α-acrosin; β-acrosin; upsilon-acrosin; acrosomal protease; acrosin amidase. Cat No: EXWM-4094. | |
| AM3102 | AM-3102 is an Oleoyl ethanolamide (OEA) analog that stimulates PPARα transcriptional activity with an EC50 value of 100 nM and prolongs feeding latency. The biological effects of OEA are terminated by N-acylethanolamine-hydrolyzing acid amidase and fatty-acid amide hydrolase. AM3102 demonstrates weak affinity for the central cannabinoid (CB1) and peripheral cannabinoid (CB2) receptors with Ki values of 33 and 26 μM, respectively. Synonyms: KDS-5104; AM-3102; AM 3102; Methyl oleoylethanolamide. Grades: ≥98%. CAS No. 213182-22-0. Molecular formula: C21H41NO2. Mole weight: 339.6. | |
| AM 374 | AM 374 is an fatty acid amide hydrolase (FAAH) inhibitor. AM 374 inhibits amidase activity with an IC 50 value of 13 nM. AM 374 can be used for the research of neurological disease [1] [2]. Uses: Scientific research. Group: Signaling pathways. CAS No. 86855-26-7. Pack Sizes: 10 mM * 1 mL; 5 mg; 10 mg; 25 mg; 50 mg. Product ID: HY-125967. | |
| ARN 14686 | ARN14686 is a NAAA (N-acylethanolamine acid amidase) activity-based protein profiling (ABPP) probe. ARN14686 can be used to detect NAAA by using click chemistry in cell lysates or intact cells, which binds covalently to the N-terminal cysteine of catalytically active NAAA to form a thioester adduct. ARN14686 inhibits the hydrolysis of the NAAA substrate PAMCA in HEK293 cells. The IC50s for human is 6 and the IC50s for rat recombinant enzymes is 13 nM. Synonyms: (S)-Undec-10-yn-1-yl (2-oxoazetidin-3-yl)carbamate. Grades: ≥98% by HPLC. CAS No. 1628345-10-7. Molecular formula: C15H24N2O3. Mole weight: 280.36. | |
| ARN726 | ARN726 is a systemically active and orally bioavailable N-acylethanolamine acid amidase (NAAA) inhibitor with IC50 value of 27 nM for human and 63 nM for rat NAAA. The selectivity for NAAA is better than fatty acid amide hydrolase (FAAH) with IC50s of 100 uM. It is also selective over acid cermidase with IC5Os of 12.5 uM. ARN726 can decrease lung myeloperoxidase activity and pleural exudate TNF-α levels in a mouse model of carrageenan-induced lung inflammation. Synonyms: ARN-0726; ARN 0726. Grades: ≥95%. CAS No. 1628343-77-0. Molecular formula: C14H24N2O3. Mole weight: 268.35. | |
| carboxylesterase | Wide specificity. The enzymes from microsomes also catalyse the reactions of EC 3.1.1.2 (arylesterase), EC 3.1.1.5 (lysophospholipase), EC 3.1.1.6 (acetylesterase), EC 3.1.1.23 (acylglycerol lipase), EC 3.1.1.28 (acylcarnitine hydrolase), EC 3.1.2.2 (palmitoyl-CoA hydrolase), EC 3.5.1.4 (amidase) and EC 3.5.1.13 (aryl-acylamidase). Also hydrolyses vitamin A esters. Group: Enzymes. Synonyms: ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyrate esterase; triacetin esterase; carboxyl ester h. Enzyme Commission Number: EC 3.1.1.1. CAS No. 9016-18-6. Esterase. 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-3434; carboxylesterase; EC 3.1.1.1; 9016-18-6; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyrate esterase; triacetin esterase; carboxyl ester hydrolase; butyrate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; esterase A; serine esterase; carboxylic acid esterase; cocaine esterase. Cat No: EXWM-3434. | |
| Carmofur | Carmofur (HCFU) is a rat recombinant acid ceramidase inhibitor with an IC 50 of 29 nM. Carmofur is also a protease inhibitor of SARS-CoV-2 main protease ( Mpro ), fatty acid amide hydrolase ( FAAH ) and N-acylethanolamine acid amidase ( NAAA ). Carmofur has anti-cancer, anti-inflammatory and anti-virus activities, and can be used for the study of COVID-19 and acute lung injury (ALI) [1] [2] [3]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: HCFU. CAS No. 61422-45-5. Pack Sizes: 10 mM * 1 mL; 25 mg; 50 mg; 100 mg; 500 mg. Product ID: HY-B0182. | |
| CHIR-090 | CHIR-090 is a very potent and tight-binding inhibitor of LpxC, which is a zinc-dependent amidase and present in almost all Gram-negative bacteria, and is a promising target for the development of novel antibiotic substances against multigrug-resistant Gram-negative bacteria. Its Ki value is 4.0 nM. It displays two-step time-dependent inhibition and kills a wide range of Gram-negative pathogens as effectively as ciprofloxacin or tobramycin. It has a different selectivity with the reported LpxC inhibitor L-161. It has excellent antibiotic activity against Pseudomonas aeruginosa and Escherichia coli by inhibiting LpxC orthologs at low nM concentrations. It is an excellent lead for the further development of new antibiotics targeting the lipid A pathway. Uses: Chir-090 displays two-step time-dependent inhibition and kills a wide range of gram-negative pathogens as effectively as ciprofloxacin or tobramycin. it has excellent antibiotic activity against pseudomonas aeruginosa and escherichia coli by inhibiting lpxc orthologs at low nm concentrations. Synonyms: CHIR-090; CHIR 090; CHIR090. N-[ (1S, 2R) -2-Hydroxy-1-[ (hydroxyamino) carbonyl]propyl]-4-[[4- (4-morpholinylmethyl) phenyl]ethynyl]benzamide. Grades: 98%. CAS No. 728865-23-4. Molecular formula: C24H27N3O5. Mole weight: 437.49. | |
| Clostripain | Clostripain (Clostridiopeptidase B) is a proteolytic enzyme isolated from Clostridium histolyticum with esterase, amidase and protease activities and is a highly specific carboxypeptide targeting arginine key protease [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: Clostridiopeptidase B. CAS No. 9028-00-6. Pack Sizes: 1 mg. Product ID: HY-P2895. | |
| diphthine-ammonia ligase | This amidase catalyses the last step in the conversion of an L-histidine residue in the translation elongation factor EF2 to diphthamide. This factor is found in all archaebacteria and eukaryotes, but not in eubacteria, and is the target of bacterial toxins such as the diphtheria toxin and the Pseudomonas exotoxin A (see EC 2.4.2.36, NAD+-diphthamide ADP-ribosyltransferase). The substrate of the enzyme, diphthine, is produced by EC 2.1.1.98, diphthine synthase. Group: Enzymes. Synonyms: diphthamide synthase; diphthamide synthetase; DPH6 (gene name); ATPBD4 (gene name); diphthine:ammonia ligase (AMP-forming). Enzyme Commission Number: EC 6.3.1.14. CAS No. 114514-33-9. 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-5717; diphthine-ammonia ligase; EC 6.3.1.14; 114514-33-9; diphthamide synthase; diphthamide synthetase; DPH6 (gene name); ATPBD4 (gene name); diphthine:ammonia ligase (AMP-forming). Cat No: EXWM-5717. | |
| glutathionylspermidine synthase | Requires magnesium ions. Involved in the synthesis of trypanothione in trypanosomatids. The enzyme from Escherichia coli is bifunctional and also catalyses the glutathionylspermidine amidase (EC 3.5.1.78) reaction, resulting in a net hydrolysis of ATP. Group: Enzymes. Synonyms: glutathione:spermidine ligase (ADP-forming). Enzyme Commission Number: EC 6.3.1.8. CAS No. 9077-9-2. 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-5728; glutathionylspermidine synthase; EC 6.3.1.8; 9077-09-2; glutathione:spermidine ligase (ADP-forming). Cat No: EXWM-5728. | |
| isopenicillin-N N-acyltransferase | Proceeds by a two stage mechanism via 6-aminopenicillanic acid. Different from EC 3.5.1.11, penicillin amidase. Group: Enzymes. Synonyms: acyl-coenzyme A:isopenicillin N acyltransferase; isopenicillin N:acyl-CoA: acyltransferase. Enzyme Commission Number: EC 2.3.1.164. CAS No. 54576-90-8. 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-2104; isopenicillin-N N-acyltransferase; EC 2.3.1.164; 54576-90-8; acyl-coenzyme A:isopenicillin N acyltransferase; isopenicillin N:acyl-CoA: acyltransferase. Cat No: EXWM-2104. | |
| long-chain-fatty-acyl-glutamate deacylase | Does not act on acyl derivates of other amino acids. Optimum chain length of acyl residue is 12 to 16. Group: Enzymes. Synonyms: long-chain aminoacylase; long-chain-fatty-acyl-glutamate deacylase; long-chain acylglutamate amidase; N-acyl-D-glutamate deacylase. Enzyme Commission Number: EC 3.5.1.55. CAS No. 82249-69-2. 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-4444; long-chain-fatty-acyl-glutamate deacylase; EC 3.5.1.55; 82249-69-2; long-chain aminoacylase; long-chain-fatty-acyl-glutamate deacylase; long-chain acylglutamate amidase; N-acyl-D-glutamate deacylase. Cat No: EXWM-4444. | |
| 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. | |
| Lysostaphin | Lysostaphin is an antistaphylococcal agent. Lysostaphin has activities of three enzymes namely, glycylglycine endopeptidase, endo-β-N-acetyl glucosamidase and N-acteyl muramyl-L-alanine amidase [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 9011-93-2. Pack Sizes: 1 mg; 5 mg; 10 mg. Product ID: HY-P2329. | |
| MAFP | MAFP (Methyl Arachidonyl Fluorophosphonate) is an selective, active-site directed and irreversible inhibitor of cPLA2 and iPLA2. MAFP is also a potent irreversible inhibitor of anandamide amidase. Uses: Scientific research. Group: Signaling pathways. Alternative Names: Methyl Arachidonyl Fluorophosphonate. CAS No. 188404-10-6. Pack Sizes: 1 mg (26.99 mM * 100 μL in Methyl acetate). Product ID: HY-103334. | |
| 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-acetyl-1-D-myo-inositol-2-amino-2-deoxy-α-D-glucopyranoside deacetylase | This enzyme is considered the key enzyme and rate limiting step in the mycothiol biosynthesis pathway. In addition to acetylase activity, the enzyme possesses weak activity of EC 3.5.1.115, mycothiol S-conjugate amidase, and shares sequence similarity with that enzyme. The enzyme requires a divalent transition metal ion for activity, believed to be Zn2+. Group: Enzymes. Synonyms: MshB. Enzyme Commission Number: EC 3.5.1.103. 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-4382; N-acetyl-1-D-myo-inositol-2-amino-2-deoxy-α-D-glucopyranoside deacetylase; EC 3.5.1.103; MshB. Cat No: EXWM-4382. | |
| N-Acetyltaurine | N-Acetyltaurine is a sulfonate that can serve as a carbon source or a nitrogen source, and an energy source for microbial growth (such as the NAT strain). Additionally, N-Acetyltaurine is also a substrate for the amidase enzyme, porcine kidney N-acetyl-β-alanine deacetylase [EC 3.5.1.21] [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 19213-70-8. Pack Sizes: 10 mM * 1 mL; 5 mg; 10 mg; 25 mg; 50 mg; 100 mg. Product ID: HY-W587486. | |
| Native Almonds Glycopeptidase A | In enzymology, a peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase (EC 3.5.1.52) is an enzyme that catalyzes a chemical reaction that cleaves a N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. Group: Enzymes. Synonyms: EC 3.5.1.52; glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; glycopeptidase; Jack-bean glycopeptidase; PNGase A; PNGase F; glycopeptide N-glycosidase; 83534-39-8; peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase. Enzyme Commission Number: EC 3.5.1.52. CAS No. 83534-39-8. PNGase F. Activity: > 0.05 unit/mL. Storage: -20°C. Form: buffered aqueous glycerol solution; Solution in 50% glycerol containing 50 mM Citrate-phosphate buffer, pH 5.0, and BSA. Source: Almonds. EC 3.5.1.52; glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; glycopeptidase; Jack-bean glycopeptidase; PNGase A; PNGase F; glycopeptide N-glycosidase; 83534-39-8; peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase. Cat No: NATE-0600. | |
| Native Corynebacterium lilium Creatinine Deiminase | Hydrolase for creatinine determination that catalyzes the conversion of creatinine to N-methylhydantoin and ammonia. Rely on the proven diagnostic quality of this product. Applications: Use creatinine deaminase in diagnostic tests for the determination of creatinine in combination with n-carbamoylsarcosine amidase, n-methylhydantoinase (atp-hydrolysing) and sarcosine oxidase. Group: Enzymes. Synonyms: Creatinine hydrolase; creatinine desiminase. Creatinine Deiminase. Activity: 45.0-90.0 U/mg lyophilizate. Stability: At +2 to +8°C within specification range for 12 months. Store dry. Protect from light. Appearance: Beige lyophilizate. Source: Corynebacterium lilium. Creatinine hydrolase; Creatinine deaminase; EC 3.5.4.21; creatinine desiminase. Cat No: DIA-291. | |
| Native E.coli Sarcosine Oxidase | Oxidoreductase that catalyzes the demethylation of sarcosine to glycine. Use Sarcosine Oxidase in your preferred creatinine reagent mix and rely on the proven diagnostic quality of this product. Applications: Use sarcosine oxidase in diagnostic tests for the determination of creatinine. this can be done using one of two methods: (1) in combination with creatinase and creatininase. (2) in combination with creatinine deaminase, n-carbamoylsarcosine amidase and n-methylhydantoinase (atp-hydrolyzing). Group: Enzymes. Synonyms: Sarcosine Oxidase; SAO. CAS No. 9029-22-5. SAO. Mole weight: 40 kD. Activity: 22-40 U/mg lyophilizate; >45 U/mg protein. Stability: At -15 to -25°C within specification range for 12 months. Store dry. Protect from light. Appearance: Yellow lyophilizate. Source: E. coli. Sarcosine Oxidase; EC 1.5.3.1; SAO. Cat No: DIA-290. | |
| Native Elizabethkingia meningoseptica PNGase F | In enzymology, a peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase (EC 3.5.1.52) is an enzyme that catalyzes a chemical reaction that cleaves a N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. Applications: Used to deglycosylate protein. proteomics grade pngase f has been extensively purified and lyophilized from dilute potassium phosphate buffer to prod...eptidase; N-glycanase; glycopeptidase; Jack-bean glycopeptidase; PNGase A; PNGase F; glycopeptide N-glycosidase; peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase; EC 3.5.1.52; PNGase F; 83534-39-8. Enzyme Commission Number: EC 3.5.1.52. CAS No. 83534-39-8. Purity: > 95% (SDS-PAGE). PNGase F. Mole weight: ~36 kDa. Storage: 2-8°C. Source: Elizabethkingia meningoseptica. glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; glycopeptidase; Jack-bean glycopeptidase; PNGase A; PNGase F; glycopeptide N-glycosidase; peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase; EC 3.5.1.52; PNGase F; 83534-39-8. Cat No: NATE-0601. | |
| Native Elizabethkingia miricola PNGase F | In enzymology, a peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase (EC 3.5.1.52) is an enzyme that catalyzes a chemical reaction that cleaves a N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. Applications: Used to deglycosylate protein. Group: Enzymes. Synonyms: glycopeptide N-glycosida. Enzyme Commission Number: EC 3.5.1.52. CAS No. 83534-39-8. PNGase F. Mole weight: 36 kDa. Activity: > 20,000 units/mg protein and > 5,000 units/ml. Stability: The product remains active for at least 12 months when stored properly. Exposure for several days to ambient temperatures will not reduce activity. Do Not Freeze. Storage: 2-8°C. Form: Supplied as a solution in 20 mM Tris HCl, pH 7.5, 50 mM NaCl and 1 mM EDTA. Source: Elizabethkingia miricola. glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; glycopeptidase; Jack-bean glycopeptidase; PNGase A; PNGase F; glycopeptide N-glycosidase; peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase; EC 3.5.1.52; PNGase F; 83534-39-8. Cat No: NATE-0602. | |
| Native Flavobacterium meningosepticum PNGase F | In enzymology, a peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase (EC 3.5.1.52) is an enzyme that catalyzes a chemical reaction that cleaves a N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. Pngase f is purified from flavobacterium meningosepticum (3) and it is free of proteases and endo f activities. the following reagents are supplied with this produ...osaminyl)asparagine amidase; EC 3.5.1.52; PNGase F; 83534-39-8. Enzyme Commission Number: EC 3.5.1.52. CAS No. 83534-39-8. PNGase F. Mole weight: 36 kDa. Activity: 500,000 units/ml. Stability: Storage Conditions: 20 mM Tris-HCl, 50 mM NaCl, 5 mM Na2EDTA, 50% Glycerol, pH 7.5 25°C Heat Inactivation: 75°C for 10 min. Storage: Store at -20°C. Source: Flavobacterium meningosepticum. glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; glycopeptidase; Jack-bean glycopeptidase; PNGase A; PNGase F; glycopeptide N-glycosidase; peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase; EC 3.5.1.52; PNGase F; 83534-39-8. Cat No: NATE-0603. | |
| N-formylglutamate deformylase | The animal enzyme also acts on β-citryl-L-glutamate and β-citryl-L-glutamine. Group: Enzymes. Synonyms: β-citryl-L-glutamate hydrolase; formylglutamate deformylase; N-formylglutamate hydrolase; β-citrylglutamate amidase; β-citryl-L-glutamate amidohydrolase; β-citryl-L-glutamate amidase; β-citryl-L-glutamate-hydrolyzing enzyme. Enzyme Commission Number: EC 3.5.1.68. CAS No. 97286-12-9. 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-4458; N-formylglutamate deformylase; EC 3.5.1.68; 97286-12-9; β-citryl-L-glutamate hydrolase; formylglutamate deformylase; N-formylglutamate hydrolase; β-citrylglutamate amidase; β-citryl-L-glutamate amidohydrolase; β-citryl-L-glutamate amidase; β-citryl-L-glutamate-hydrolyzing enzyme. Cat No: EXWM-4458. | |
| Nitrilase (Crude Enzyme) | Nitrilase enzymes catalyse the hydrolysis of nitriles to carboxylic acids and ammonia, without the formation of "free" amide intermediates. Nitrilases are involved in natural product biosynthesis and post translational modifications in plants, animals, fungi and certain prokaryotes. Nitrilases can also be used as catalysts in preparative organic chemistry. Among others, nitrilases have been used for the resolution of racemic mixtures. Nitrilase should not be confused with nitrile hydratase (nitrile hydro-lyase; EC 4. 2. 1. 84) which hydrolyses nitriles to amides. Nitrile hydratases are almost invariably co-expressed with an amidase, which converts the amide to the carboxylic acid, consequently it can sometimes be difficult to distinguish nitrilase activity from nitrile hydratase plus amidase activity. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Synthesis; industry. Group: Enzymes. Synonyms: acetonitrilase; benzonitrilase. Enzyme Commission Number: EC 3.5.5.1. CAS No. 9024-90-2. Nitrilase. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. acetonitrilase; benzonitrilase. Pack: 100ml. Cat No: NATE-1842. | |
| N-(long-chain-acyl)ethanolamine deacylase | Does not act on N-acylsphingosine or N,O-diacylethanolamine. Group: Enzymes. Synonyms: N-acylethanolamine amidohydrolase; acylethanolamine amidase. Enzyme Commission Number: EC 3.5.1.60. CAS No. 99283-61-1. 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-4450; N-(long-chain-acyl)ethanolamine deacylase; EC 3.5.1.60; 99283-61-1; N-acylethanolamine amidohydrolase; acylethanolamine amidase. Cat No: EXWM-4450. | |
| N-methylhydantoinase (ATP-hydrolysing) | This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. This enzyme participates in arginine, creatinine, and proline metabolism. Group: Enzymes. Synonyms: N-methylhydantoin amidohydrolase; methylhydantoin amidase; N-methylhydantoin hydrolase; N-methylhydantoinase; N-methylimidazolidine-2,4-dione amidohydrolase (ATP-hydrolysing). Enzyme Commission Number: EC 3.5.2.14. CAS No. 100785-00-0. 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-4497; N-methylhydantoinase (ATP-hydrolysing); EC 3.5.2.14; 100785-00-0; N-methylhydantoin amidohydrolase; methylhydantoin amidase; N-methylhydantoin hydrolase; N-methylhydantoinase; N-methylimidazolidine-2,4-dione amidohydrolase (ATP-hydrolysing). Cat No: EXWM-4497. | |
| N-Methylhydantoinase (ATP-hydrolyzing) from Arthrobacter sp., Recombinant | In enzymology, a N-methylhydantoinase (ATP-hydrolysing) is an enzyme that catalyzes the chemical reaction: ATP + N-methylimidazolidine-2,4-dione + 2 H2O rightleftharpoons ADP + phosphate + N-carbamoylsarcosine. The 3 substrates of this enzyme are ATP, N-methylimidazolidine-2,4-dione, and H2O, whereas its 3 products are ADP, phosphate, and N-carbamoylsarcosine. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. This enzyme participates in arginine, creatinine, and proline metabolism. Hydrolase for creatinine determination that uses atp to catalyze the conversion of...amoylsarcosine amidase and sarcosine oxidase. Group: Enzymes. Synonyms: N-methylimidazolidine-2,4-dione amidohydrolase (ATP-hydrolysing); N-methylhydantoin amidohydrolase; methylhydantoin amidase; N-methylhydantoin hydrolase; N-methylhydantoinase. N-Methylhydantoinase. Activity: 0.6-1.0 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: Arthrobacter sp. N-methylimidazolidine-2,4-dione amidohydrolase (ATP-hydrolysing); N-methylhydantoin amidohydrolase; methylhydantoin amidase; N-methylhydantoin hydrolase; N-methylhydantoinase. Cat No: NATE-0904. | |
| PNGase A from Oryza sativa (rice), Recombinant | PNGase A cleaves N-linked glycans from high mannose, hybrid, and short complex oligosaccharides such as those found in plant and insect cells. PNGase A differs from PNGase F in that it cleaves N-linked glycans with or without α(1,3)-linked core fucose residues.PNGase A is a recombinant amidase, which cleaves between the innermost GlcNAc and asparagine residues of high mannose, hybrid, and short complex oligosaccharides such as those found in plant and insect cells from N-linked glycoproteins and glycopeptides. PNGase A differs from PNGase F in that it cleaves N-linked glycans with or without α(1,3)-linked core fucose residues. Group: Enzymes. Synonyms: N-Glycosidase A; PNGase A; Glycopeptidase A; N-linked-glycopeptide-(N-acetyl-β-D-glucosaminyl)-L-asparagine amidohydrolase; PNGase. Enzyme Commission Number: EC 3.5.1.52. Purity: > 95% pure as determined by SDS-PAGE. PNGase F. Mole weight: 63.8 kDa. Activity: 5,000 units/ml. Storage: 4°C. Form: Storage Conditions: 50 mM NaCl, 20 mM Tris-HCl, 5 mM EDTA, (pH 7.5 @ 25°C). Source: Pichia pastoris. Species: Oryza sativa (rice). N-Glycosidase A; PNGase A; Glycopeptidase A; N-linked-glycopeptide-(N-acetyl-β-D-glucosaminyl)-L-asparagine amidohydrolase; PNGase. Cat No: NATE-1941. | |
| PNGase F from Elizabethkingia meningoseptica, Recombinant | In enzymology, a peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase (EC 3.5.1.52) is an enzyme that catalyzes a chemical reaction that cleaves a N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. Applications: Highly purified material can be used for preparative deglycosylation or for analytical applications in gel, in solution, or on blot membranes. ...n 50% (v/v) glycerol and 50% (v/v) 20 mM Potassium Phosphate, pH 7.5. Type III, buffered aqueous solution, Supplied as a solution in 20 mM Tris HCl, pH 7.5, 50 mM NaCl and 1 mM EDTA. Source: E. coli. Species: Elizabethkingia meningoseptica. glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; glycopeptidase; Jack-bean glycopeptidase; PNGase A; PNGase F; glycopeptide N-glycosidase; peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase; EC 3.5.1.52; PNGase F; 83534-39-8. Pack: PNGase F was used for deglycosylation of P-glycoprotein in a study to investigate the dual impact of statins on p-glycoprotein and its effect on dox | |
| PNGase F from Elizabethkingia miricola, Recombinant | In enzymology, a peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase (EC 3.5.1.52) is an enzyme that catalyzes a chemical reaction that cleaves a N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. Applications: Pngase f can be use to cleave n-glycans attached to proteins and antibodies. Group: Enzymes. Synonyms: glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; glycop. CAS No. 83534-39-8. Purity: >95% by SDS-PAGE gel. PNGase F. Stability: PNGase F retains >60% activity after left at room temperature for over 72 hours. Long term storage at - 20°C or below. Storage: Long term storage at -20°C or below. Form: 20 mM Tris pH8, 50% glycerol. Source: E. coli. Species: Elizabethkingia miricola. glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; glycopeptidase; Jack-bean glycopeptidase; PNGase A; PNGase F; glycopeptide N-glycosidase; peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase; EC 3.5.1.52; PNGase F; 83534-39-8. Cat No: NATE-1286. | |
| PNGase F from Flavobacterium meningosepticum, Recombinant | In enzymology, a peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase (EC 3.5.1.52) is an enzyme that catalyzes a chemical reaction that cleaves a N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. Pngase f, peptide n-glycosidase f, is a recombinantly expressed endoglycosidase from flavobacterium meningosepticum that cleaves the β-aspartylglucosami...cetyl-β-glucosaminyl)asparagine amidase; EC 3.5.1.52; PNGase F; 83534-39-8. CAS No. 83534-39-8. Purity: >95% by SDS-PAGE. PNGase F. Mole weight: 34,800 daltons (Apparent). Activity: >10 U/mg. Stability: 1 year. Storage: 2-8°C. Avoid multiple freeze/thaw cycles. Form: 20 mM Tris - pH 7.5, 50 mM NaCl, 0.5 mM EDTA. Source: E. coli. Species: Flavobacterium meningosepticum. glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; glycopeptidase; Jack-bean glycopeptidase; PNGase A; PNGase F; glycopeptide N-glycosidase; peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase; EC 3.5.1.52; PNGase F; 83534-39-8. Cat No: NATE-1287. | |
| Sapacitabine | Sapacitabine is an orally bioavailable pyrimidine analogue prodrug with potential antineoplastic activity. Sapacitabine is hydrolyzed by amidases to the deoxycytosine analogue CNDAC (2'-Cyano-2'-deoxyarabinofuranosylcytosine), which is then phosphorylated into the active triphosphate form. As an analogue of deoxycytidine triphosphate, CNDAC triphosphate incorporates into DNA strands during replication, resulting in single-stranded DNA breaks during polymerization due to beta-elimination during the fidelity checkpoint process; cell cycle arrest in the G2 phase and apoptosis ensue. Synonyms: CS682; CYC682; CYC-682; Sapacitabine. CAS No. 151823-14-2. Molecular formula: C26H42N4O5. Mole weight: 490.645. | |
| trypanothione synthase | The enzyme, characterized from several trypanosomatids (e.g. Trypanosoma cruzi) catalyses two subsequent reactions, leading to production of trypanothione from glutathione and spermidine. Some trypanosomatids (e.g. Crithidia species and some Leishmania species) also contain an enzyme that only carries out the first reaction (cf. EC 6.3.1.8, glutathionylspermidine synthase). The enzyme is bifunctional, and also catalyses the hydrolysis of glutathionylspermidine and trypanothione (cf. EC 3.5.1.78, glutathionylspermidine amidase). Group: Enzymes. Synonyms: glutathionylspermidine:glutathione ligase (ADP-forming). Enzyme Commission Number: EC 6.3.1.9. CAS No. 130246-69-4. 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-5729; trypanothione synthase; EC 6.3.1.9; 130246-69-4; glutathionylspermidine:glutathione ligase (ADP-forming). Cat No: EXWM-5729. | |
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