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| Product | Description | |
|---|---|---|
| (1?4)-α-D-glucan 1-α-D-glucosylmutase | The enzyme from Arthrobacter sp., Sulfolobus acidocaldarius acts on (1?4)-α-D-glucans containing three or more (1?4)-α-linked D-glucose units. Not active towards maltose. Group: Enzymes. Synonyms: malto-oligosyltrehalose synthase; maltodextrin α-D-glucosyltransferase. Enzyme Commission Number: EC 5.4.99.15. CAS No. 170780-49-1. 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-5554; (1?4)-α-D-glucan 1-α-D-glucosylmutase; EC 5.4.99.15; 170780-49-1; malto-oligosyltrehalose synthase; maltodextrin α-D-glucosyltransferase. Cat No: EXWM-5554. |  |
| 2,6-dihydroxypseudooxynicotine hydrolase | The enzyme, characterized from the soil bacterium Arthrobacter nicotinovorans, participates in nicotine degradation. Group: Enzymes. Enzyme Commission Number: EC 3.7.1.19. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4726; 2,6-dihydroxypseudooxynicotine hydrolase; EC 3.7.1.19. Cat No: EXWM-4726. | |
| 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase | Does not contain a metal centre or organic cofactor. Fission of two C-C bonds: 2,4-dioxygenolytic cleavage with concomitant release of carbon monoxide. The enzyme from Arthrobacter sp. can also act on 3-hydroxy-4-oxoquinoline, forming N-formylanthranilate and CO (cf. EC 1.13.11.47, 3-hydroxy-4-oxoquinoline 2,4-dioxygenase), but more slowly. Group: Enzymes. Synonyms: (1H)-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase. Enzyme Commission Number: EC 1.13.11.48. CAS No. 160995-63-1. 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-0566; 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase; EC 1.13.11.48; 160995-63-1; (1H)-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase. Cat No: EXWM-0566. | |
| 4-methylaminobutanoate oxidase (formaldehyde-forming) | A flavoprotein (FAD). In the enzyme from the soil bacterium Arthrobacter nicotinovorans the cofactor is covalently bound. Participates in the nicotine degradation pathway of this organism. Group: Enzymes. Synonyms: mabO (gene name). Enzyme Commission Number: EC 1.5.3.19. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1546; 4-methylaminobutanoate oxidase (formaldehyde-forming); EC 1.5.3.19; mabO (gene name). Cat No: EXWM-1546. | |
| 6-hydroxypseudooxynicotine dehydrogenase | Contains a cytidylyl molybdenum cofactor. The enzyme, which participates in the nicotine degradation pathway, has been characterized from the soil bacterium Arthrobacter nicotinovorans. Group: Enzymes. Enzyme Commission Number: EC 1.5.99.14. 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-1568; 6-hydroxypseudooxynicotine dehydrogenase; EC 1.5.99.14. Cat No: EXWM-1568. | |
| α(2?3,6,8,9) Neuraminidase from Arthrobacter ureafaciens, Recombinant | Neuraminidase is the common name for Acetyl-neuraminyl hydrolase (Sialidase). α2-3,6,8,9 Neuraminidase catalyzes the hydrolysis of all linear and branched non-reducing terminal sialic acid residues from glycoproteins and oligosaccharides. The enzyme releases α2-3 and α2-6 linkages at a slightly higher rate than α2-8 and α2-9 linkages. Group: Enzymes. Synonyms: neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6; α2-3,6,8,9 Neuraminidase A; α2-3,6,8,9 Neuraminidase; α(2?3,6,8,9) Neuraminidase. Enzyme Commission Number: EC 3.2.1.18. CAS No. 9001-67-6. Neuraminidase. Mole weight: 100,000 daltons. Activity: ~316,000 units/mg. Storage: at -20°C. Form: Supplied in: 50 mM NaCl, 20 mM Tris-HCl (pH 7.5 @ 25°C) and 1 mM EDTA. Source: E. coli. Species: Arthrobacter ureafaciens. neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6; α2-3,6,8,9 Neuraminidase A; α2-3,6,8,9 Neuraminidase; α(2?3,6,8,9) Neuraminidase. Cat No: NATE-0758. | |
| Alu I | One unit of the enzyme is the amount required to hydrolyze 1 μg of Lambda DNA in 1 hour at 37°C in a total reaction volume of 50 μl. Applications: After 5-fold overdigestion with enzyme approximately 90% of the dna fragments can be ligated and recut. Group: Restriction Enzymes. Purity: 200U; 1000U. AG↑CT TC↓GA. Activity: 2000-5000u.a./ml. Appearance: 10 X SE-buffer Y. Storage: -20°C. Form: Liquid. Source: An. E.coli strain that carries the cloned Alu I gene from Arthrobacter luteus. Pack: 10 mM Tris-HCl (pH 7.6); 100 mM NaCl; 0.1 mM EDTA; 200 μg/ml BSA; 1 mM DTT, 50% glycerol. Cat No: RE-1018EN. | |
| Dimethylglycine oxidase from Arthrobacter globifomis, Recombinant | Dimethylglycine oxidase (DMGO) is a covalent flavoenzyme from Arthrobacter globiformis that catalyzes the oxidative demethylation of dimethylglycine to yield sarcosine, formaldehyde, and hydrogen peroxide. The N-terminal region binds FAD covalently so it is yellowish. Dimethylglycine oxidase recombinant originated from arthrobacter globifomis fused to his tag at n-terminal produced in e. coli is a single, non-glycosylated, polypeptide chain containing 850 amino acids and having a molecular mass of 92.1 kda. the dmgo is purified by proprietary chromatographic techniques. Group: Enzymes. Synonyms: DMGO; Dimethylglycine Oxidase. CAS No. 74870-79-4. Purity: Greater than 95.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. DMGO. Mole weight: 92.1 kDa. Stability: Dimethylglycine Oxidase Recombinant although stable at 4°C for 30 days, should be stored desiccated below -20°C for periods greater than 30 days. Please prevent freeze-thaw cycles. Appearance: Sterile filtered liquid formulation 1 mg/ml. Source: E. coli. Species: Arthrobacter globifomis. DMGO; Dimethylglycine Oxidase. Cat No: NATE-0826. | |
| Endo-β-N-acetylglucosaminidase from Arthrobacter protophormia, Recombinant | An Endoglycosidase is an enzyme that releases oligosaccharides from glycoproteins or glycolipids. It may also cleave polysaccharide chains between residues that are not the terminal residue, although releasing oligosaccharides from conjugated protein and lipid molecules is more common. It breaks the glycosidic bonds between two sugar monomer in the polymer. It is different from exoglycosidase that it does not do so at the terminal residue. Hence, it is used to release long carbohydrates from conjugated molecules. If an exoglycosidase were used, every monomer in the polymer would have to be removed, one by one from the chain, taking a long time. An endoglycosidase cleaves, giving a polymeric product. Group: Enzymes. Synonyms: Endoglycosidase; Endo-β-N-acetylglucosaminidase; EC 3.2.1.96; 231-791-2. Enzyme Commission Number: EC 3.2.1.96. CAS No. 37278-88-9. Purity: min 95% by SDS-PAGE. Endo-β-N-acetylglucosaminidase. Mole weight: 69 kDa. Source: E. coli. Species: Arthrobacter protophormia. Endoglycosidase; Endo-β-N-acetylglucosaminidase; EC 3.2.1.96; 231-791-2; Endo-A; Endo-β-N-Acetylglucosaminidase A. Cat No: NATE-1493. | |
| hydantoin racemase | This enzyme, along with N-carbamoylase (EC 3.5.1.77 and EC 3.5.1.87) 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 Pseudomonas sp. (HyuE) has a preference for hydantoins with aliphatic substituents, e.g. D- and L-5-(2-methylthioethyl)hydantoin, whereas that from Arthrobacter aurescens shows highest activity with arylalkyl substituents, especially 5-benzylhydantoin, at the 5-position. In the enzyme from Sinorhizobium meliloti, Cys76 is responsible for recognition and proton retrieval of D-isomers, while Cys181 is responsible for L-isomer recognition and racemization. Group: Enzymes. Synonyms: 5'-monosubstituted-hydantoin racemase; HyuA; HyuE. Enzyme Commission Number: EC 5.1.99.5. 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-5437; hydantoin racemase; EC 5.1.99.5; 5'-monosubstituted-hydantoin racemase; HyuA; HyuE. Cat No: EXWM-5437. | |
| Native Arthrobacter globiformis Choline oxidase | In enzymology, a choline oxidase (EC 1.1.3.17) is an enzyme that catalyzes the chemical reaction choline + O2<-> betaine aldehyde + H2O2. Thus, the two substrates of this enzyme are choline and O2, whereas its two products are betaine aldehyde and H2O2. Native choline oxidase (ec 1.1.3.17) was purified from arthrobacter globiformis. Group: Enzymes. Synonyms: choline oxidase; EC 1.1.3.17; choline: oxygen 1-oxidoreductase. Enzyme Commission Number: EC 1.1.3.17. CAS No. 9028-67-5. Choline Oxidase. Activity: 8-20 U/mg. Appearance: Yellow amorphous powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Arthrobacter globiformis. choline oxidase; EC 1.1.3.17; choline: oxygen 1-oxidoreductase. Cat No: DIA-139. | |
| Native Arthrobacter luteus Lyticase | Lyticase hydrolyzes poly-β (1?3)-glucose such as yeast cell wall glucan. Applications: Yeast cells are difficult to disrupt because the cell walls may form capsules or resistant spores. dna can be extracted from yeast by using lysing enzymes such as lyticase, chitinase, zymolase, and gluculase to induce partial spheroplast formation; spheroplasts are subsequently lysed to release dna. lyticase is preferred to digest cell walls of yeast and generate spheroplasts from fungi for transformation. reported to be useful for lysis of ashbya, candida, debaryomyces, eremothecium, endomyces, hansenula, hanseniaspora, kloeckera, kluyveromyces, lipomyces, metschikowia, pichia, pullularia, torulopsis, saccharomyces, saccharomycopsis, saccharomycodes, and schwanniomyces species. Group: Enzymes. Synonyms: Lyticase; 37340-57-1. CAS No. 37340-57-1. Lyticase. Activity: > 200 units/mg solid; > 1,500 units/mg protein; > 2,000 units/mg protein, Protein > 20 % by biuret. Storage: 2-8°C. Form: lyophilized powder. Source: Arthrobacter luteus. Lyticase; 37340-57-1. Cat No: NATE-0431. | |
| Native Arthrobacter sp. acyl-CoA oxidase | In enzymology, an acyl-CoA oxidase (EC 1.3.3.6) is an enzyme that catalyzes the chemical reaction acyl-CoA + O2<-> trans-2, 3-dehydroacyl-CoA + H2O2. Thus, the two substrates of this enzyme are acyl-CoA and O2, whereas its two products are trans-2, 3-dehydroacyl-CoA and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with oxygen as acceptor. This enzyme participates in 3 metabolic pathways: fatty acid metabolism, polyunsaturated fatty acid biosynthesis, and ppar signaling pathway. It employs one cofactor, FAD. Native acyl-coa oxidase (ec 1.3.3.6) was purified from arthrobacter sp. Group: Enzymes. Synonyms: acyl-CoA oxidase; EC 1.3.3.6; fatty acyl-CoA oxidase; acyl coenzyme A oxidase; and fatty acyl-coenzyme A oxidase. Enzyme Commission Number: EC 1.3.3.6. CAS No. 61116-22-1. Acyl-CoA oxidase. Activity: > 20 U/mg. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Yellowish Freeze dried powder. Source: Arthrobacter sp. acyl-CoA oxidase; EC 1.3.3.6; fatty acyl-CoA oxidase; acyl coenzyme A oxidase; and fatty acyl-coenzyme A oxidase. Cat No: DIA-121. | |
| Native Arthrobacter sp. Tyramine Oxidase | Amine oxidases (AO) are enzymes that catalyze the oxidation of a wide range of biogenic amines including many neurotransmitters, histamine and xenobiotic amines. There are two classes of amine oxidases: flavin-containing (EC 1.4.3.4) and copper-containing (EC 1.4.3.6). Copper-containing AO act as a disulphide-linked homodimer. They catalyse the oxidation of primary amines to aldehydes, with the subsequent release of ammonia and hydrogen peroxide, which requires one copper ion per subunit and topaquinone as cofactor: RCH2NH2 + H2O + O2 <-> RCHO + NH3 + H2O2. The 3 substrates of this enzyme are primary amines (RCH2NH2), H2O, and O2, whereas its 3 products are RCHO, NH3, and H2O2. Native tyramine oxidase (ec 1.4.3.4) was purified from arthrobacter sp. Applications: Useful for enzymatic determiantion of leucine aminopeptidase. Group: Enzymes. Synonyms: Tyramine Oxidase; TOD; EC 1.4.3.6. Enzyme Commission Number: EC 1.4.3.6. CAS No. 9001-53-0. Tyramine Oxidase. Activity: > 3 U/mg. Appearance: White to light brown powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Arthrobacter sp. Tyramine Oxidase; TOD; EC 1.4.3.6. Cat No: DIA-158. | |
| Native Arthrobacter ureafaciens α (2?3,6,8,9) Neuraminidase | Neuraminidase enzymes are glycoside hydrolase enzymes (EC 3.2.1.18) that cleave the glycosidic linkages of neuraminic acids. Neuraminidase enzymes are a large family, found in a range of organisms. The best-known neuraminidase is the viral neuraminidase, a drug target for the prevention of the spread of influenza infection. The viral neuraminidases are frequently used as antigenic determinants found on the surface of the Influenza virus. Some variants of the influenza neuraminidase confer more virulence to the virus than others. Other homologs are found in mammalian cells, which have a range of functions. Applications: Neuraminidase is an important deglycosyl... resulting in partial or complete o-deglycosylation. sds-page and maldi-tof ms are typically utilized in purification, structural analysis, and sequencing process. these techniques also remove heterogeneity and charge from the glycoprotein. Group: Enzymes. Synonyms: neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6. Enzyme Commission Number: EC 3.2.1.18. CAS No. 9001-67-6. Neuraminidase. Storage: 2-8°C. Form: Lyophilized powder. Source: Arthrobacter ureafaciens. neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6. Cat No: NATE-0756. | |
| nicotine blue oxidoreductase | The enzyme, characterized from the nicotine degrading bacterium Arthrobacter nicotinovorans, catalyses the reduction of "nicotine blue" to its hydroquinone form (the opposite direction from that shown). Nicotine blue is the name given to the compound formed by the autocatalytic condensation of two molecules of 2,3,6-trihydroxypyridine, an intermediate in the nicotine degradation pathway. The main role of the enzyme may be to prevent the intracellular formation of nicotine blue semiquinone radicals, which by redox cycling would lead to the formation of toxic reactive oxygen species. The enzyme possesses a slight preference for NADH over NADPH. Group: Enzymes. Synonyms: nboR (gene name). Enzyme Commission Number: EC 1.1.1.328. 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-0241; nicotine blue oxidoreductase; EC 1.1.1.328; nboR (gene name). Cat No: EXWM-0241. | |
| 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. | |
| N-substituted formamide deformylase | Zinc is a cofactor. While N-benzylformamide is the best substrate, the enzyme from Arthrobacter pascens can also act on the N-substituted formamides N-butylformamide, N-allylformamide, N-[2-(cyclohex-1-enyl)ethyl]formamide and N-(1-phenylethyl)formamide, but much more slowly. Amides of other acids do not act as substrates. Group: Enzymes. Synonyms: NfdA. Enzyme Commission Number: EC 3.5.1.91. CAS No. 115299-95-1. 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-4483; N-substituted formamide deformylase; EC 3.5.1.91; 115299-95-1; NfdA. Cat No: EXWM-4483. | |
| opine dehydrogenase | In the forward direction, the enzyme from Arthrobacter sp. acts also on secondary amine dicarboxylates such as N-(1-carboxyethyl)methionine and N-(1-carboxyethyl)phenylalanine. Dehydrogenation forms an imine, which dissociates to the amino acid and pyruvate. In the reverse direction, the enzyme acts also on neutral amino acids as an amino donor. They include L-amino acids such as 2-aminopentanoic acid, 2-aminobutyric acid, 2-aminohexanoic acid, 3-chloroalanine, O-acetylserine, methionine, isoleucine, valine, phenylalanine, leucine and alanine. The amino acceptors include 2-oxoacids such as pyruvate, oxaloacetate, glyoxylate and 2-oxobutyrate. Group: Enzymes. Synonyms: (2S)-2-{[1-(R)-carboxyethyl]amino}pentanoate dehydrogenase (NAD+, L-aminopentanoate-forming). Enzyme Commission Number: EC 1.5.1.28. CAS No. 108281-02-3. 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-1510; opine dehydrogenase; EC 1.5.1.28; 108281-02-3; (2S)-2-{[1-(R)-carboxyethyl]amino}pentanoate dehydrogenase (NAD+, L-aminopentanoate-forming). Cat No: EXWM-1510. | |
| (R)-6-hydroxynicotine oxidase | A flavoprotein (FAD). The enzyme, which participates in nicotine degradation, is specific for (R) isomer of 6-hydroxynicotine, derived from the uncommon (R)-nicotine. The bacterium Arthrobacter nicotinovorans, in which this enzyme was originally discovered, has a different enzyme that catalyses a similar reaction with the (S)-isomer (cf. EC 1.5.3.5, (S)-6-hydroxynicotine oxidase). Group: Enzymes. Synonyms: D-6-hydroxynicotine oxidase; 6-hydroxy-D-nicotine oxidase. Enzyme Commission Number: EC 1.5.3.6. CAS No. 37233-46-8. 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-1553; (R)-6-hydroxynicotine oxidase; EC 1.5.3.6; 37233-46-8; D-6-hydroxynicotine oxidase; 6-hydroxy-D-nicotine oxidase. Cat No: EXWM-1553. | |
| synephrine dehydratase | Removal of H2O from (R)-synephrine produces a 2,3-enamine, which hydrolyses to the products shown in the reaction above. The enzyme from Arthrobacter synephrinum is highly specific. Group: Enzymes. Synonyms: syringinase. Enzyme Commission Number: EC 4.2.1.88. CAS No. 104118-54-9. 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-5072; synephrine dehydratase; EC 4.2.1.88; 104118-54-9; syringinase. Cat No: EXWM-5072. | |
| 2-(hydroxymethyl)-3-(acetamidomethylene)succinate hydrolase | Involved in the degradation of pyridoxin by Pseudomonas and Arthrobacter. Group: Enzymes. Synonyms: compound B hydrolase; α-hydroxymethyl-α'-(N-acetylaminomethylene)succinic acid hydrolase. Enzyme Commission Number: EC 3.5.1.66. CAS No. 95829-26-8. 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-4456; 2-(hydroxymethyl)-3-(acetamidomethylene)succinate hydrolase; EC 3.5.1.66; 95829-26-8; compound B hydrolase; α-hydroxymethyl-α'-(N-acetylaminomethylene)succinic acid hydrolase. Cat No: EXWM-4456. | |
| 4-hydroxyphenylpyruvate oxidase | Involved in tyrosine degradation pathway in Arthrobacter sp. Group: Enzymes. Enzyme Commission Number: EC 1.2.3.13. CAS No. 78213-74-8. 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-1207; 4-hydroxyphenylpyruvate oxidase; EC 1.2.3.13; 78213-74-8. Cat No: EXWM-1207. | |
| 4-methylaminobutanoate oxidase (methylamine-forming) | The enzyme participates in the nicotine degradation pathway of the soil bacterium Arthrobacter nicotinovorans. Has a very weak monoamine oxidase (EC 1.4.3.4) activity with 4-aminobutanoate. Group: Enzymes. Synonyms: mao (gene name, ambiguous). Enzyme Commission Number: EC 1.5.3.21. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1549; 4-methylaminobutanoate oxidase (methylamine-forming); EC 1.5.3.21; mao (gene name, ambiguous). Cat No: EXWM-1549. | |
| 5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenase | Involved in the tyrosine degradation pathway in Arthrobacter sp. Group: Enzymes. Synonyms: carboxymethylhydroxymuconic semialdehyde dehydrogenase. Enzyme Commission Number: EC 1.2.1.60. CAS No. 63241-20-3. 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-1162; 5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenase; EC 1.2.1.60; 63241-20-3; carboxymethylhydroxymuconic semialdehyde dehydrogenase. Cat No: EXWM-1162. | |
| Abs I | One unit of the enzyme is the amount required to hydrolyze 1 μg of pUC19SE/DriI -digest in 1 hour at 37°C in a total reaction volume of 50 μl. Applications: After 2-fold overdigestion with enzyme about 90% of the dna fragments can be ligated with t4 dna ligase at 16°c and recut. Group: Restriction Enzymes. Purity: 50U; 250U. CC↑TCGAGG GGAGCT↓CC. Activity: 500-1000u.a./ml. Appearance: 10 X SE-buffer AbsI. Storage: -20°C. Form: Liquid. Source: Arthrobacter species 7M06. Pack: 10 mM Tris-HCl (pH 7.5); 50 mM KCl; 0.1 mM EDTA; 7 mM 2-mercaptoethanol; 200 μg/ml BSA; 50% glycerol. Cat No: RE-1002EN. | |
| Acs I | One unit of the enzyme is the amount required to hydrolyze 1 μg of Lambda DNA in 1 hour at 50°C in a total reaction volume of 50 μl. Applications: After 10-fold overdigestion with enzyme more than 90% of the dna fragments can be ligated and recut. Group: Restriction Enzymes. Purity: 500U; 2500U. R↑AATTY YTTAA↓R. Activity: 10000u.a./ml. Appearance: 10 X SE-buffer W, BSA. Storage: -20°C. Form: Liquid. Source: Arthrobacter citreus. Pack: 20 mM Tris-HCl (pH 7.5); 50 mM KCl; 0.1 mM EDTA; 10 mM 2-mercaptoethanol; 50% glycerol. Cat No: RE-1012EN. | |
| AluB I | One unit of the enzyme is the amount required to hydrolyze 1 μg of Lambda DNA in 1 hour at 37°C in a total reaction volume of 50 μl. Applications: After 10-fold overdigestion with enzyme 80% of the lambda dna fragments can be ligated with t4 dna ligase and can be recut. Group: Restriction Enzymes. Purity: 200U; 1000U. AG↑CT TC↓GA. Activity: 5000u.a./ml. Appearance: 10 X SE-buffer B, BSA. Storage: -20°C. Form: Liquid. Source: Arthrobacter luteus B. Pack: 10 mM Tris-HCl (pH 7.5); 200 mM NaCl; 0.1 mM EDTA; 7 mM 2-mercaptoethanol; 200 μg/ml BSA; 50% glycerol. Cat No: RE-1019EN. | |
| Ars I | One unit of the enzyme is the amount required to hydrolyze 1 μg of T7 DNA in 1 hour at 30°C in a total reaction volume of 50 μl. Applications: After 3-fold overdigestion with enzyme 70% of dna fragments can be ligated. of these 80% can be recut. Group: Restriction Enzymes. Purity: 100U; 500U. ↑(N)8GACNNNNNNTTYG(N)11↑ ↓(N)13CTGNNNNNNAARC(N)6&darr. Activity: 3000-5000u.a./ml. Appearance: 10 X SE-buffer Y, BSA. Storage: -20°C. Form: Liquid. Source: Arthrobacter species NTS. Pack: 10 mM KH2PO4(pH 7.4); 200 mM KCl; 0,1 mM EDTA; 7 mM 2-mercaptoethanol; 200 μg/ml BSA, 50% glycerol. Cat No: RE-1022EN. | |
| AsiG I | One unit of the enzyme is the amount required to hydrolyze 1 μg of Lambda DNA in 1 hour at 37°C in a total reaction volume of 50 μl. Applications: After 5-fold overdigestion with enzyme more than 90% of the dna fragments can be ligated and recut. Group: Restriction Enzymes. A↑CCGGT TGGCC↓A. Appearance: 10 X SE-buffer O. Storage: -20°C. Form: Liquid. Source: Arthrobacter species G. Pack: 10 mM Tris-HCl (pH 7.5); 250 mM NaCl; 0.1 mM EDTA; 7 mM 2-mercaptoethanol; 100 μg/ml BSA; 50% glycerol. Cat No: RE-1023EN. | |
| AspA2 I | One unit of the enzyme is the amount required to hydrolyze 1 μg of Lambda DNA (HindIII-digest) in 1 hour at 37°C in a total reaction volume of 50 μl. Applications: After 10-fold overdigestion with enzyme more than 90% of the dna fragments can be ligated and recut. Group: Restriction Enzymes. Purity: 500U; 2500U. C↑CTAGG GGATC↓C. Activity: 10000u.a./ml. Storage: -20°C. Form: Liquid. Source: Arthrobacter species A2. Pack: 10 mM Tris-HCl (pH 7.5); 100 mM NaCl; 0.1 mM EDTA; 7 mM 2-mercaptoethanol; 100 μg/ml BSA; 50% glycerol. Cat No: RE-1024EN. | |
| AspLE I | One unit of the enzyme is the amount required to hydrolyze 1 μg of Lambda DNA in 1 hour at 37°C in a total reaction volume of 50 μl. Applications: After 10-fold overdigestion with enzyme more than 90% of the dna fragments can be ligated and recut. Group: Restriction Enzymes. Purity: 500U; 2500U. GCG↑C C↓GCG. Activity: 10000u.a./ml. Appearance: 10 X SE-buffer O. Storage: -20°C. Form: Liquid. Source: Arthrobacter species LE3860. Pack: 10 mM Tris-HCl (pH 7.5); 100 mM NaCl; 0.1 mM EDTA; 7 mM 2-mercaptoethanol; 100 μg/ml BSA; 50% glycerol. Cat No: RE-1025EN. | |
| AspS9 I | One unit of the enzyme is the amount required to hydrolyze 1 μg of Lambda DNA in 1 hour at 37°C in a total reaction volume of 50 μl. Applications: After 20-fold overdigestion with enzyme more than 90% of the dna fragments can be ligated and recut. Group: Restriction Enzymes. Purity: 1000U; 5000U. G↑GNCC CCNG↓G. Activity: 20000u.a./ml. Appearance: 10 X SE-buffer W. Storage: -20°C. Form: Liquid. Source: Arthrobacter species S9. Pack: 10 mM Tris-HCl (pH 7.5); 50 mM KCl; 0.1 mM EDTA; 7 mM 2-mercaptoethanol; 200 μg/ml BSA; 50% glycerol. Cat No: RE-1026EN. | |
| fluoren-9-ol dehydrogenase | Involved in the pathway for fluorene metabolism in Arthrobacter sp. Group: Enzymes. Enzyme Commission Number: EC 1.1.1.256. CAS No. 154215-16-4. 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-0161; fluoren-9-ol dehydrogenase; EC 1.1.1.256; 154215-16-4. Cat No: EXWM-0161. | |
| Native Arthrobacter globiformis Uricase | The enzyme urate oxidase (UO) catalyzes the oxidation of uric acid to 5-hydroxyisourate:Uric acid + O2 + H2O ? 5-hydroxyisourate + H2O2 ? allantoin + CO2. Group: Enzymes. Synonyms: uric acid oxidase; uricase; uricase II; urate oxidase; factor-independent urate hydroxylase; EC 1.7.3.3; 9002-12-4; UO. Enzyme Commission Number: EC 1.7.3.3. CAS No. 9002-12-4. UO. Mole weight: 4 × ~32 KDa (tetramer). Activity: 15-30 units/mg protein (biuret). Storage: -20°C. Form: lyophilized powder. Source: Arthrobacter globiformis. uric acid oxidase; uricase; uricase II; urate oxidase; factor-independent urate hydroxylase; EC 1.7.3.3; 9002-12-4; UO. Cat No: NATE-0729. | |
| Native Arthrobacter luteus Zymolyase | Native Arthrobacter luteus Zymolyase. Group: Enzymes. Synonyms: Zymolyase. Zymolyase. Activity: 20U/mg. Stability: Stable for one year at 4°C. Storage: -20°C. Form: Lyophilized powder. Source: Arthrobacter luteus. Zymolyase. Cat No: NATE-0739. | |
| (S)-6-hydroxynicotine oxidase | A flavoprotein (FAD). The enzyme, which participates in nicotine degradation, is specific for the (S) isomer of 6-hydroxynicotine. The bacterium Arthrobacter nicotinovorans, in which this enzyme was originally discovered, has a different enzyme that catalyses a similar reaction with the less common (R)-isomer (cf. EC 1.5.3.6, (R)-6-hydroxynicotine oxidase). Group: Enzymes. Synonyms: L-6-hydroxynicotine oxidase; 6-hydroxy-L-nicotine oxidase; 6-hydroxy-L-nicotine:oxygen oxidoreductase; nctB (gene name). Enzyme Commission Number: EC 1.5.3.5. CAS No. 37256-29-4. 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-1552; (S)-6-hydroxynicotine oxidase; EC 1.5.3.5; 37256-29-4; L-6-hydroxynicotine oxidase; 6-hydroxy-L-nicotine oxidase; 6-hydroxy-L-nicotine:oxygen oxidoreductase; nctB (gene name). Cat No: EXWM-1552. | |
| Uricase (Recombinant) | Uricase, Arthrobacter globiformis is a peroxidase enzyme responsible for catalyzing the oxidative reaction of uric acid, converting it into the soluble product allantoin. Uricase, Arthrobacter globiformis can be used for the determination of uric acid levels in serum. The lack of uricase in mammals can lead to kidney diseases caused by the accumulation of uric acid. Uricase, Arthrobacter globiformis can be utilized in research on gout and hyperuricemia [1] [2]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: Uox (Recombinant). CAS No. 9002-12-4. Pack Sizes: 1 KU. Product ID: HY-P2921C. |  |
| vanillate monooxygenase | Forms part of the vanillin degradation pathway in Arthrobacter sp. Group: Enzymes. Synonyms: 4-hydroxy-3-methoxybenzoate demethylase; vanillate demethylase. Enzyme Commission Number: EC 1.14.13.82. CAS No. 39307-11-4. 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-0890; vanillate monooxygenase; EC 1.14.13.82; 39307-11-4; 4-hydroxy-3-methoxybenzoate demethylase; vanillate demethylase. Cat No: EXWM-0890. | |
| Xanthine Oxidase from Arthrobacter sp. | Xanthine oxidase is a form of xanthine oxidoreductase, a type of enzyme that generates reactive oxygen species. These enzymes catalyze the oxidation of hypoxanthine to xanthine and can further catalyze the oxidation of xanthine to uric acid. These enzymes play an important role in the catabolism of purines in some species, including humans. Group: Enzymes. Synonyms: EC 1.17.3.2; Xanthine oxidase; XO; XAO. Enzyme Commission Number: EC 1.17.3.2. CAS No. 9002-17-9. Mole weight: 160 kDa (gel). Activity: >50U/mg protein. Storage: Store at -20°C. Form: Reddish brown amorphous powder, lyophilized. Source: Arthrobacter sp. EC 1.17.3.2; Xanthine oxidase; XO; XAO; XOD. Cat No: NATE-1719. | |
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