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| Product | Description | |
|---|---|---|
| (11Z)-hexadec-11-enoyl-CoA conjugase | The enzyme, characterized from the silk moth Bombyx mori, catalyses a step in the pathway for the biosynthesis of bombykol, a sex pheromone produced by the moth. The enzyme converts a single cis double bond at position 11 of (11Z)-hexadec-11-enoyl-CoA into conjugated 10 trans and 12 cis double bonds. Prior to catalysing this reaction, the enzyme catalyses the introduction of the cis bond in position 11 (cf. EC 1.14.19.5, acyl-CoA 11-desaturase). Group: Enzymes. Synonyms: Bmpgdesat1 (gene name). Enzyme Commission Number: EC 1.14.19.15. 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-0977; (11Z)-hexadec-11-enoyl-CoA conjugase; EC 1.14.19.15; Bmpgdesat1 (gene name). Cat No: EXWM-0977. |  |
| 1,2-Dioleoyl-sn-glycerol | ALN29882 is a glycerolipid located on the plasma membrane. It consists of two fatty acid chains covalently linked to a single glycerol molecule by means of an ester bond. 18:1 DG has been used as a source of diacylglycerol in the diacylglycerol O-acyltransferase 1 (DGAT1) assay. It is also used as a substrate in the DGAT-1 enzyme assay to evaluate compounds as potential inhibitors of DGAT-1. Suitable for lipoprotein overlay screening assays with the recombinant protein His-AtROP6. Uses: Scientific research. Group: Biochemical assay reagents. Alternative Names: sn-1,2-Dioleoylglycerol. CAS No. 24529-88-2. Pack Sizes: 5 mg; 10 mg; 25 mg. Product ID: HY-141572. |  |
| 20-O-multi-glycoside ginsenosidase | The 20-O-multi-glycoside ginsenosidase catalyses the hydrolysis of the 20-O-α-(1?6)-glycosidic bond and the 20-O-β-(1?6)-glycosidic bond of protopanaxadiol-type ginsenosides. The enzyme usually leaves a single glucosyl residue attached at position 20, although it can cleave the remaining glucosyl residue with a lower efficiency. Starting with a ginsenoside that is glycosylated at positions 3 and 20, such as ginsenosides Rb1, Rb2, Rb3 and Rc, the most common product is ginsenoside Rd, with a low amount of ginsenoside Rg3 also formed. Group: Enzymes. Synonyms: ginsenosidase type II (erroneous). Enzyme Commission Number: EC 3.2.1.195. 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-3879; 20-O-multi-glycoside ginsenosidase; EC 3.2.1.195; ginsenosidase type II (erroneous). Cat No: EXWM-3879. | |
| 2,3-dihydroxybenzoate 3,4-dioxygenase | This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2. The systematic name of this enzyme class is 2,3-dihydroxybenzoate:oxygen 3,4-oxidoreductase (decyclizing). Other names in common use include o-pyrocatechuate oxygenase, 2,3-dihydroxybenzoate 1,2-dioxygenase, 2,3-dihydroxybenzoic oxygenase, and 2,3-dihydroxybenzoate oxygenase. This enzyme participates in benzoate degradation via hydroxylation. Group: Enzymes. Synonyms: o-pyrocatechuate oxygenase; 2,3-dihydroxybenzoate 1,2-dioxygenase; 2,3-dihydroxybenzoic oxygenase; 2,3-dihydroxybenzoate oxygenase; 2,3-dihydroxybenzoate:oxygen 3,4-oxidoreductase (decyclizing). Enzyme Commission Number: EC 1.13.11.14. CAS No. 9032-31-9. 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-0533; 2,3-dihydroxybenzoate 3,4-dioxygenase; EC 1.13.11.14; 9032-31-9; o-pyrocatechuate oxygenase; 2,3-dihydroxybenzoate 1,2-dioxygenase; 2,3-dihydroxybenzoic oxygenase; 2,3-dihydroxybenzoate oxygenase; 2,3-dihydroxybenzoate:oxygen 3,4-oxidoreductase (decyclizing). Cat No: EXWM-0533. | |
| 2,3-dihydroxyindole 2,3-dioxygenase | This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2. The systematic name of this enzyme class is 2,3-dihydroxyindole:oxygen 2,3-oxidoreductase (decyclizing). This enzyme participates in tryptophan metabolism. Group: Enzymes. Synonyms: 2,3-dihydroxyindole:oxygen 2,3-oxidoreductase (decyclizing). Enzyme Commission Number: EC 1.13.11.23. CAS No. 37256-62-5. 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-0542; 2,3-dihydroxyindole 2,3-dioxygenase; EC 1.13.11.23; 37256-62-5; 2,3-dihydroxyindole:oxygen 2,3-oxidoreductase (decyclizing). Cat No: EXWM-0542. | |
| 2,3-diketo-5-methylthiopentyl-1-phosphate enolase | The enzyme participates in the methionine salvage pathway in Bacillus subtilis.In some species a single bifunctional enzyme, EC 3.1.3.77, acireductone synthase, catalyses both this reaction and EC 3.1.3.87, 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase. Group: Enzymes. Synonyms: DK-MTP-1-P enolase; MtnW; YkrW; RuBisCO-like protein; RLP. Enzyme Commission Number: EC 5.3.2.5. 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-5485; 2,3-diketo-5-methylthiopentyl-1-phosphate enolase; EC 5.3.2.5; DK-MTP-1-P enolase; MtnW; YkrW; RuBisCO-like protein; RLP. Cat No: EXWM-5485. | |
| 2,4'-dihydroxyacetophenone dioxygenase | This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2. The systematic name of this enzyme class is 2,4'-dihydroxyacetophenone oxidoreductase (C-C-bond-cleaving). This enzyme is also called (4-hydroxybenzoyl)methanol oxygenase. This enzyme participates in bisphenol a degradation. Group: Enzymes. Synonyms: (4-hydroxybenzoyl)methanol oxygenase. Enzyme Commission Number: EC 1.13.11.41. CAS No. 257617-97-3. 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-0561; 2,4'-dihydroxyacetophenone dioxygenase; EC 1.13.11.41; 257617-97-3; (4-hydroxybenzoyl)methanol oxygenase. Cat No: EXWM-0561. | |
| 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase | The enzyme participates in the methionine salvage pathway in Bacillus subtilis.In some species a single bifunctional enzyme, EC 3.1.3.77, acireductone synthase, catalyses both this reaction and EC 5.3.2.5, 2,3-diketo-5-methylthiopentyl-1-phosphate enolase. Group: Enzymes. Synonyms: HK-MTPenyl-1-P phosphatase; MtnX; YkrX. Enzyme Commission Number: EC 3.1.3.87. 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-3693; 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase; EC 3.1.3.87; HK-MTPenyl-1-P phosphatase; MtnX; YkrX. Cat No: EXWM-3693. | |
| 2-methylbutanoate polyketide synthase | This polyketide synthase enzyme forms the (S)-2-methylbutanoate side chain during lovastatin biosynthesis by the filamentous fungus Aspergillus terreus. The overall reaction comprises a single condensation reaction followed by α-methylation, β-ketoreduction, dehydration, and α,β enoyl reduction. Group: Enzymes. Synonyms: LovF. Enzyme Commission Number: EC 2.3.1.244. 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-2193; 2-methylbutanoate polyketide synthase; EC 2.3.1.244; LovF. Cat No: EXWM-2193. | |
| 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase | This enzyme is involved in the biosynthesis of vitamin K2 (menaquinone). In most anaerobes and all Gram-positive aerobes, menaquinone is the sole electron transporter in the respiratory chain and is essential for their survival. It had previously been thought that the reactions carried out by this enzyme and EC 2.2.1.9, 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase, were carried out by a single enzyme but this has since been disproved. Group: Enzymes. Synonyms: 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylic acid synthase; 6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate synthase; SHCHC synthase; MenH; YfbB. Enzyme Commission Number: EC 4.2.99.20. CAS No. 122007-88-9. 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-5266; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; EC 4.2.99.20; 122007-88-9; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylic acid synthase; 6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate synthase; SHCHC synthase; MenH; YfbB. Cat No: EXWM-5266. | |
| 5-(carboxyamino)imidazole ribonucleotide mutase | In eubacteria, fungi and plants, this enzyme, along with EC 6.3.4.18, 5-(carboxyamino)imidazole ribonucleotide synthase, is required to carry out the single reaction catalysed by EC 4.1.1.21, phosphoribosylaminoimidazole carboxylase, in vertebrates. In the absence of EC 6.3.2.6, phosphoribosyl aminoimidazolesuccinocarboxamide synthase, the reaction is reversible. The substrate is readily converted into 5-amino-1-(5-phospho-D-ribosyl)imidazole by non-enzymic decarboxylation. Group: Enzymes. Synonyms: N5-CAIR mutase; PurE; N5-carboxyaminoimidazole ribonucleotide mutase; class I PurE. Enzyme Commission Number: EC 5.4.99.18. CAS No. 255379-40-9. 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-5557; 5-(carboxyamino)imidazole ribonucleotide mutase; EC 5.4.99.18; 255379-40-9; N5-CAIR mutase; PurE; N5-carboxyaminoimidazole ribonucleotide mutase; class I PurE. Cat No: EXWM-5557. | |
| 5-(carboxyamino)imidazole ribonucleotide synthase | In Escherichia coli, this enzyme, along with EC 5.4.99.18, 5-(carboxyamino)imidazole ribonucleotide mutase, is required to carry out the single reaction catalysed by EC 4.1.1.21, phosphoribosylaminoimidazole carboxylase, in vertebrates. Belongs to the ATP grasp protein superfamily. Carboxyphosphate is the putative acyl phosphate intermediate. Involved in the late stages of purine biosynthesis. Group: Enzymes. Synonyms: N5-CAIR synthetase; N5-carboxyaminoimidazole ribonucleotide synthetase; PurK. Enzyme Commission Number: EC 6.3.4.18. CAS No. 255379-40-9. 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-5787; 5-(carboxyamino)imidazole ribonucleotide synthase; EC 6.3.4.18; 255379-40-9; N5-CAIR synthetase; N5-carboxyaminoimidazole ribonucleotide synthetase; PurK. Cat No: EXWM-5787. | |
| 5' to 3' exodeoxyribonuclease (nucleoside 3'-phosphate-forming) | Preference for single-stranded DNA. The enzyme from the archaeon Sulfolobus solfataricus contains a [4Fe-4S] cluster and requires a divalent metal cation, such as Mg2+ or Mn2+, for activity. Group: Enzymes. Synonyms: Cas4; 5' to 3' single stranded DNA exonuclease. Enzyme Commission Number: EC 3.1.12.1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3535; 5' to 3' exodeoxyribonuclease (nucleoside 3'-phosphate-forming); EC 3.1.12.1; Cas4; 5' to 3' single stranded DNA exonuclease. Cat No: EXWM-3535. | |
| Acetyl-Coenzyme A acetyltransferase 2 from Human, Recombinant | ACAT2 enzyme participates in lipid metabolism. ACAT2 takes part in lipoprotein assembly, catalyzing cholesterol esterification in mammalian cells. ACAT2 is an integral membrane protein that localizes to the endoplasmic reticulum of human intestinal cells. ACAT2 deficiency contributes to severe mental retardation and hypotonus. Acat2 recombinant human produced in e. coli is a single, non-glycosylated polypeptide chain containing 433 amino acids (1-397 a.a.) and having a molecular mass of 45.4 kda. the acat2 is fused to 36 amino acid his-tag at n-terminus and purified by proprietary chromatographic techniques. Group: Enzymes. Synonyms: Acetyl-CoA acetyltransferase cytosolic; Cytosolic acetoacetyl-CoA thiolase; ACAT2; Acetyl CoA transferase-like protein; ACAT-2. Purity: Greater than 95.0% as determined by SDS-PAGE. ACAT-2. Mole weight: 45.4 kDa. Stability: ACAT2 Human although stable at 4°C for 1 week, should be stored desiccated below -18°C. Please prevent freeze thaw cycles. Appearance: Sterile Filtered clear solution. Source: E. coli. Species: Human. Acetyl-CoA acetyltransferase cytosolic; Cytosolic acetoacetyl-CoA thiolase; ACAT2; Acetyl CoA transferase-like protein; ACAT-2. Cat No: NATE-0798. | |
| adamalysin | From the venom of the eastern diamondback rattlesnake (Crotalus adamanteus). Two isoenzymes of approx. 24 kDa that inactivate α1-proteinase inhibitor by a single cleavage. In peptidase family M12 (astacin family). Group: Enzymes. Synonyms: Crotalus adamanteus metalloendopeptidase; proteinase I and II; Crotalus adamanteus venom proteinase II; adamalysin II. Enzyme Commission Number: EC 3.4.24.46. CAS No. 74812-51-4. 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-4328; adamalysin; EC 3.4.24.46; 74812-51-4; Crotalus adamanteus metalloendopeptidase; proteinase I and II; Crotalus adamanteus venom proteinase II; adamalysin II. Cat No: EXWM-4328. | |
| alcohol dehydrogenase (azurin) | A soluble, periplasmic PQQ-containing quinohemoprotein. Also contains a single heme c. Occurs in Comamonas and Pseudomonas. Does not require an amine activator. Oxidizes a wide range of primary and secondary alcohols, and also aldehydes and large substrates such as sterols; methanol is not a substrate. Usually assayed with phenazine methosulfate or ferricyanide. Like all other quinoprotein alcohol dehydrogenases it has an 8-bladed propeller structure, a calcium ion bound to the PQQ in the active site and an unusual disulfide ring structure in close proximity to the PQQ. Group: Enzymes. Synonyms: type II quinoprotein alcohol dehydrogenase; quinohaemoprotein ethanol dehydrogenase; QHEDH; ADHIIB. Enzyme Commission Number: EC 1.1.9.1. 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-0438; alcohol dehydrogenase (azurin); EC 1.1.9.1; type II quinoprotein alcohol dehydrogenase; quinohaemoprotein ethanol dehydrogenase; QHEDH; ADHIIB. Cat No: EXWM-0438. | |
| α amylase | α-Amylase isolated from porcine pancreas is a glycoprotein.2 It is a single polypeptide chain of approximately 475 residues containing 2 SH groups and four disulfide bridges and a tightly bound Ca2+ necessary for stability.3,4 Chloride ions are necessary for activity and stability5 The pH range for activity is 5.5 to 8.0, with the pH optimum at 7.6. Α-amylase from porcine pancreas. Applications: Α-amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. product is from porcine pancreas and is type i-a. α-amylase has been used in various plant studies, such as metabolism studies in arabidopsis. Group: Enzymes. S...mission Number: EC 3.2.1.1. CAS No. 9000-90-2. α-Amylase. Mole weight: 51-54 kDa. Activity: 700-1400 units/mg protein (E1%/280). Stability: α-Amylase is stable in 25 mM Tris-HCl, pH 7.5, with 100 mM KCl, at 0 °C or at -20 °C for at least 9 days.8 Another recommended storage condition is in 1 mM phosphate, pH 7.3, with 30 mM CaCl2 at -15 °C. Appearance: Appearance (Color): White to Light Yellow Appearance (Form): Suspension. Form: PMSF treated, saline suspension. Alpha amylase enzyme; for flour; fungal alpha amylase enzyme; enhance quality of flour enzyme; enhance quality; alpha amylase enzyme; flour; alpha amylase; Alpha amylase enzyme for flour; FLO-1301. Cat No: BAK-250. | |
| α-glucosidase | This single entry covers a group of enzymes whose specificity is directed mainly towards the exohydrolysis of (1?4)-α-glucosidic linkages, and that hydrolyse oligosaccharides rapidly, relative to polysaccharide, which are hydrolysed relatively slowly, or not at all. The intestinal enzyme also hydrolyses polysaccharides, catalysing the reactions of EC 3.2.1.3 glucan 1,4-α-glucosidase and, more slowly, hydrolyses (1?6)-α-D-glucose links. Group: Enzymes. Synonyms: maltase; glucoinvertase; glucosidosucrase; maltase-glucoamylase; α-glucopyranosidase; glucosidoinvertase; α-D-glucosidase; α-glucoside hydrolase; α-1,4-glucosidase. Enzyme Commission Number: EC 3.2.1.20. CAS No. 9001-42-7. α-Glucosidase. 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-3885; α-glucosidase; EC 3.2.1.20; 9001-42-7; maltase; glucoinvertase; glucosidosucrase; maltase-glucoamylase; α-glucopyranosidase; glucosidoinvertase; α-D-glucosidase; α-glucoside hydrolase; α-1,4-glucosidase. Cat No: EXWM-3885. | |
| α-Lactalbumin | α-Lactalbumin is a Ca 2+ -binding protein. α-Lactalbumin has a single strong Ca 2+ -binding site and for this reason it frequently serves as a simple model Ca 2+ -binding protein. α-Lactalbumin is a component of lactose synthase, an enzyme system, which consists of galactosyltransferase (GT) and α-Lactalbumin [1] [2]. Uses: Scientific research. Group: Biochemical assay reagents. CAS No. 9051-29-0. Pack Sizes: 5 mg; 10 mg. Product ID: HY-NP009. | |
| 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 | |
| amylo-α-1,6-glucosidase | This enzyme hydrolyses an unsubstituted glucose unit linked by an α(1?6) bond to an α(1?4) glucose chain. The enzyme activity found in mammals and yeast is in a polypeptide chain containing two active centres. The other activity is similar to that of EC 2.4.1.25 (4-α-glucanotransferase), which acts on the glycogen phosphorylase limit dextrin chains to expose the single glucose residues, which the 6-α-glucosidase activity can then hydrolyse. Together, these two activities constitute the glycogen debranching system. Group: Enzymes. Synonyms: amylo-1,6-glucosidase; dextrin 6-α-D-glucosidase; amylopectin 1,6-glucosidase; dextrin-1,6-glucosidase; glycogen phosphorylase-limit dextrin α-1,6-glucohydrolase. Enzyme Commission Number: EC 3.2.1.33. CAS No. 9012-47-9. 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-3896; amylo-α-1,6-glucosidase; EC 3.2.1.33; 9012-47-9; amylo-1,6-glucosidase; dextrin 6-α-D-glucosidase; amylopectin 1,6-glucosidase; dextrin-1,6-glucosidase; glycogen phosphorylase-limit dextrin α-1,6-glucohydrolase. Cat No: EXWM-3896. | |
| androst-4-ene-3,17-dione monooxygenase | Has a wide specificity. A single enzyme from the ascomycete Neonectria radicicola (EC 1.14.13.54, ketosteroid monooxygenase) catalyses both this reaction and that catalysed by EC 1.14.99.4, progesterone monooxygenase. Group: Enzymes. Synonyms: androstene-3,17-dione hydroxylase; androst-4-ene-3,17-dione 17-oxidoreductase; androst-4-ene-3,17-dione hydroxylase; androstenedione monooxygenase; 4-androstene-3,17-dione monooxygenase. Enzyme Commission Number: EC 1.14.99.12. CAS No. 37256-74-9. 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-1033; androst-4-ene-3,17-dione monooxygenase; EC 1.14.99.12; 37256-74-9; androstene-3,17-dione hydroxylase; androst-4-ene-3,17-dione 17-oxidoreductase; androst-4-ene-3,17-dione hydroxylase; androstenedione monooxygenase; 4-androstene-3,17-dione monooxygenase. Cat No: EXWM-1033. | |
| angiotensin-converting enzyme 2 | A transmembrane glycoprotein with an extracellular catalytic domain. Angiotensin-converting enzyme 2 functions as a carboxypeptidase, cleaving a single C-terminal residue from a distinct range of substrates. Catalytic efficiency is 400-fold higher with angiotensin II (1-8) as a substrate than with angiotensin I (1-10). Angiotensin-converting enzyme 2 also efficiently hydrolyses des-Arg9-bradykinin, but it does not hydrolyse bradykinin. In peptidase family M2. Group: Enzymes. Synonyms: ACE-2; ACE2; hACE2; angiotensin converting enzyme 2; angiotensin converting enzyme-2; Tmem27. Enzyme Commission Number: EC 3.4.17.23. 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-4076; angiotensin-converting enzyme 2; EC 3.4.17.23; ACE-2; ACE2; hACE2; angiotensin converting enzyme 2; angiotensin converting enzyme-2; Tmem27. Cat No: EXWM-4076. | |
| ascorbate ferrireductase (transmembrane) | A diheme cytochrome that transfers electrons across a single membrane, such as the outer membrane of the enterocyte, or the tonoplast membrane of the plant cell vacuole. Acts on hexacyanoferrate(III) and other ferric chelates. Group: Enzymes. Synonyms: cytochrome b561 (ambiguous). Enzyme Commission Number: EC 7.2.1.3 (Formerly EC 1.16.5.1). 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-1077; ascorbate ferrireductase (transmembrane); EC 1.16.5.1; cytochrome b561 (ambiguous). Cat No: EXWM-1077. | |
| Aspartate Aminotransferase from Human, Recombinant | GOT1 is a pyridoxal phosphate-dependent enzyme which exists in cytoplasmic and mitochondrial forms, GOT1 and GOT2, which participate in amino acid metabolism and the urea and tricarboxylic acid cycles. Both enzymes are homodimeric and show close homology.GOT1 Human Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 433 amino acids (1-413 a.a.) and having a molecular mass of 48.4 kDa. The GOT1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques. Group: Enzymes. Synonyms: Aspartate transaminase; AST; aspartate aminotransferase; sgot AspAT; ASAT; AAT; serum glutamic oxaloac. Purity: Greater than 95.0% as determined by SDS-PAGE. AST. Activity: > 50 units/mg. 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. Form: Sterile filtered colorless solution. Source: E.coli. Species: Human. Aspartate transaminase; AST; aspartate aminotransferase; sgot AspAT; ASAT; AAT; serum glutamic oxaloacetic transaminase; SGOT; pyridoxal phosphate PLP-dependent transaminase enzyme; EC 2.6.1.1; 9000-97-9; Aspartate aminotransferase 1; Transaminase A; GIG18. Cat No: DIA-128. | |
| Aspergillus deoxyribonuclease K1 | Preference for single-stranded DNA. Group: Enzymes. Synonyms: Aspergillus DNase K1. Enzyme Commission Number: EC 3.1.22.2. CAS No. 264922-12-5. 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-3581; Aspergillus deoxyribonuclease K1; EC 3.1.22.2; 264922-12-5; Aspergillus DNase K1. Cat No: EXWM-3581. | |
| Aspergillus nuclease S1 | Aspergillus nuclease S1 is an endonuclease enzyme derived from Aspergillus oryzae that splits single-stranded DNA (ssDNA) and RNA into oligo- or mononucleotides. Group: Enzymes. Synonyms: endonuclease S1 (Aspergillus); single-stranded-nucleate endonuclease; deoxyribonuclease S1; deoxyribonuclease S1; nuclease S1; Neurospora crassa single-strand specific endonuclease; S1 nuclease; single-strand endodeoxyribonuclease; single-stranded DNA specific endonuclease; single-strand-specific endodeoxyribonuclease; single strand-specific DNase; Aspergillus oryzae S1 nuclease. Enzyme Commission Number: EC 3.1.30.1. CAS No. 37288-25-8. Nuclease. 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-3707; Aspergillus nuclease S1; EC 3.1.30.1; 37288-25-8; endonuclease S1 (Aspergillus); single-stranded-nucleate endonuclease; deoxyribonuclease S1; deoxyribonuclease S1; nuclease S1; Neurospora crassa single-strand specific endonuclease; S1 nuclease; single-strand endodeoxyribonuclease; single-stranded DNA specific endonuclease; single-strand-specific endodeoxyribonuclease; single strand-specific DNase; Aspergillus oryzae S1 nuclease. Cat No: EXWM-3707. | |
| Atto 590 nhs ester | ATTO 590 is a novel fluorescent label belonging to the class of Rhodamine dyes. The dye is designed for application in the area of life science, e.g. labeling of DNA, RNA or proteins. The ATTO dyes are a series of fluorescent dyes that provide all the crucial properties required for modern fluorescent technologies, such as fluorescence microscopy, flow-cytometry, fluorescence in situ hybridization (FISH), receptor binding assays or enzyme assays. The dye is highly suitable for single-molecule detection applications and high-resolution microscopy. The NHS-esters are used in common conjugation protocols.ATTO 590 is a novel fluorescent label belonging to the class of Rhodamine dyes, which has an absorption maximum of 594 nm and an emission maximum of 624 nm. ATTO 590-N-hydroxysuccinimide (NHS) is membrane permeable. Uses: Molar absorption 120,000 1/m cm, abs: 593 nm, em: 620 nm, qy=0.93, tfl 4.0 ns (unpublished data)atto 590 nhs ester may be suitable for use in site-specific labeling of human embryonic kidney (hek293t) cell lysates for western blotting, fluorescence, and widefield microscopy studies. Synonyms: 2-(6, 20-diethyl-7, 7, 9, 17, 19, 19-hexamethyl-2-oxa-20-aza-6-azoniapentacyclo[12.8.0.03, 12.05, 10.016, 21; docosa-1(14),3,5,8,10,12,15,17,21-nonaen-13-yl)-4-(2,5-dioxopyrrolidin-1-yl)oxycarbonylbenzoic acid;perchlorate; 6-(2-Carboxy-5-{[(2,5-dioxopyrrolidin-1-yl)oxy]carbonyl}phenyl)-1,11-diethyl-2,2,4,8,10,10-hexamethyl-10,11-dihydro-2H-pyrano[3,2-g:5,6-g']diquinolin-1-ium perchlorate. Grades: ≥60% (coupling to amines). CAS No. 670269-33-7. Molecular formula: C41H42ClN3O11. Mole weight: 788.24. |  |
| AZD-5904 | AZD-5904 is a potent orally bioavailable MPO inhibitor. It inhibited the isolated MPO enzyme with an IC50 value of 140 nM and was approximately equipotent in assays of rat and mouse MPO enzyme activity. It was used for multiple sclerosis and COPD and has been evaluated in single and multiple dose studies in healthy volunteers. Uses: Azd-5904 was used for multiple sclerosis and copd. Synonyms: AZ1, AZ 1 AZ-1; TX4; TX-4; TX 4; AZD-5904; AZD 5904; AZD5904. (S)-3-((tetrahydrofuran-2-yl)methyl)-2-thioxo-1,2,3,7-tetrahydro-6H-purin-6-one. Grades: 98%. CAS No. 618913-30-7. Molecular formula: C10H12N4O2S. Mole weight: 252.29. | |
| β-Acetylglucosaminidase 18A from Bacteroides thetaiotaomicron, Recombinant | β-acetylglucosaminidase 18A, is an enzyme from Bacteroides thetaiotaomicron that participates in the endohydrolysis of the diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the (Man(GlcNAc)(2))Asn-structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact. Recombinant BtAcp18A (GH18), purified from Escherichia coli, is a single domain family 18 Glycoside Hydrolase (GH18). Group: Enzymes. Synonyms: beta-N-acetyl-D-hexosaminide; N-acetylhexosaminohydrolase; β-N-Acetylhexosaminidase; N-Acetyl-β-D-glucosaminidase, β-N-Acetylglucosaminidase. Enzyme Commission Number: EC 3.2.1.96. CAS No. 37278-88-9. Purity: >50% by SDS-PAGE. β-N-Acetylhexosaminidase. Mole weight: 50.3 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Bacteroides thetaiotaomicron. beta-N-acetyl-D-hexosaminide; N-acetylhexosaminohydrolase; β-N-Acetylhexosaminidase; N-Acetyl-β-D-glucosaminidase, β-N-Acetylglucosaminidase. Cat No: NATE-1291. | |
| β-apiosyl-β-glucosidase | The enzyme from the tropical tree Dalbergia nigrescens Kurz belongs inglycosyl hydrolase family 1. The enzyme removes disaccharides from the natural substrates dalpatein 7-O-β-D-apiofuranosyl-(1?6)-β-D-glucopyranoside and 7-hydroxy-2',4',5',6-tetramethoxy-7-O-β-D-apiofuranosyl-(1?6)-β-D-glucopyranoside (dalnigrein 7-O-β-D-apiofuranosyl-(1?6)-β-D-glucopyranoside) although it can also remove a single glucose residue from isoflavonoid 7-O-glucosides. Daidzin and genistin are also substrates. Group: Enzymes. Synonyms: isoflavonoid-7-O-β[D-apiosyl-(1?6)-β-D-glucoside] disaccharidase; isoflavonoid 7-O-β-apiosyl-glucoside β-glucosidase; furcatin hydrolase. Enzyme Commission Number: EC 3.2.1.161. CAS No. 1000598-83-3. 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-3843; β-apiosyl-β-glucosidase; EC 3.2.1.161; 1000598-83-3; isoflavonoid-7-O-β[D-apiosyl-(1?6)-β-D-glucoside] disaccharidase; isoflavonoid 7-O-β-apiosyl-glucoside β-glucosidase; furcatin hydrolase. Cat No: EXWM-3843. | |
| β-phosphoglucomutase | The enzyme requires Mg2+ and phosphorylation of an aspartate residue at the active site. The enzyme is able to autophosphorylate itself with its substrate β-D-glucose 1-phosphate. Although this is a slow reaction, only a single turnover is required for activation. Once the phosphorylated enzyme is formed, it generates the reaction intermediate β-D-glucose 1,6-bisphosphate, which can be used to phosphorylate the enzyme in subsequent cycles. cf. EC 5.4.2.2, phosphoglucomutase (α-D-glucose-1,6-bisphosphate-dependent). Group: Enzymes. Synonyms: β-pgm (gene name). Enzyme Commission Number: EC 5.4.2.6. CAS No. 68651-99-0. β-Phosphoglucomutase. 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-5528; β-phosphoglucomutase; EC 5.4.2.6; 68651-99-0; β-pgm (gene name). Cat No: EXWM-5528. | |
| biliverdin reductase | Biliverdin reductase (BVR) is an enzyme (EC 1.3.1.24) found in all tissues under normal conditions, but especially in reticulo-macrophages of the liver and spleen. BVR facilitates the conversion of biliverdin to bilirubin via the reduction of a double-bond between the second and third pyrrole ring into a single-bond. Group: Enzymes. Enzyme Commission Number: EC 1.3.1.24. CAS No. 9074-10-6. 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-1298; biliverdin reductase; EC 1.3.1.24; 9074-10-6. Cat No: EXWM-1298. | |
| biotin synthase | The enzyme binds a [4Fe-4S] and a [2Fe-2S] cluster. In every reaction cycle, the enzyme consumes two molecules of AdoMet, each producing 5'-deoxyadenosine and a putative dethiobiotinyl carbon radical. Reaction with another equivalent of AdoMet results in abstraction of the C6 methylene pro-S hydrogen atom from 9-mercaptodethiobiotin, and the resulting carbon radical is quenched via formation of an intramolecular C-S bond, thus closing the biotin thiophane ring. The sulfur donor is believed to be the [2Fe-2S] cluster, which is sacrificed in the process, so that in vitro the reaction is a single turnover. In vivo, the [2Fe-2S] cluster can be reassembled by the Isc or Suf iron-sulfur cluster assembly systems, to allow further catalysis. Group: Enzymes. Synonyms: dethiobiotin:sulfur sulfurtransferase. Enzyme Commission Number: EC 2.8.1.6. CAS No. 80146-93-6. 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-3364; biotin synthase; EC 2.8.1.6; 80146-93-6; dethiobiotin:sulfur sulfurtransferase. Cat No: EXWM-3364. | |
| BMN-673 8R,9S | BMN-673 is an orally bioavailable inhibitor of the nuclear enzyme poly(ADP-ribose) polymerase (PARP) with potential antineoplastic activity. PARP inhibitor BMN-673 selectively binds to PARP and prevents PARP-mediated DNA repair of single strand DNA breaks via the base-excision repair pathway. This enhances the accumulation of DNA strand breaks, promotes genomic instability and eventually leads to apoptosis. PARP catalyzes post-translational ADP-ribosylation of nuclear proteins that signal and recruit other proteins to repair damaged DNA and is activated by single-strand DNA breaks. BMN-673 has been proven to be highly active in mouse models of human cancer and also appears to be more selectively cytotoxic with a longer half-life and better bioavailability as compared to other compounds in development. Synonyms: Talazoparib (8R,9S); (8R,9S)-BMN-673; BMN673 (8R,9S); BMN 673 (8R,9S). Grades: >98%. CAS No. 1207456-00-5. Molecular formula: C19H14F2N6O. Mole weight: 380.35. | |
| caffeate 3,4-dioxygenase | This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2. The systematic name of this enzyme class is 3,4-dihydroxy-trans-cinnamate:oxygen 3,4-oxidoreductase (decyclizing). This enzyme participates in phenylpropanoid biodegradation. Group: Enzymes. Synonyms: 3,4-dihydroxy-trans-cinnamate:oxygen 3,4-oxidoreductase (decyclizing). Enzyme Commission Number: EC 1.13.11.22. CAS No. 37256-61-4. 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-0541; caffeate 3,4-dioxygenase; EC 1.13.11.22; 37256-61-4; 3,4-dihydroxy-trans-cinnamate:oxygen 3,4-oxidoreductase (decyclizing). Cat No: EXWM-0541. | |
| Carboxypeptidase B from Porcine, Recombinant | Carboxypeptidase B (or peptidyl-L-lysine (-L-arginine) hydrolase) catalyzes the hydrolysis of the basic amino acids, lysine, arginine, and ornithine from the C-terminal position of polypeptides. It has been shown to be a single polypeptide of 34 kDa Da. Trypsin is capable of converting native enzyme to the active enzyme, carboxypeptidase B II in vitro. The optimum pH is found to be 9.0. The enzyme may be used for sequence analysis by successive cleavage of C-terminal basic amino acids. It can also be used as a serum marker for the diagnosis of acute pancreatitis. Carboxypeptidase b (ec 3.4.17.2), also well known as protaminase, pancreatic procarboxy-peptidase b (pcpb), ... mature chain. the secreted cpb zymogen is converted to enzymatically active cpb by limited proteolysis by trypsin. Group: Enzymes. Synonyms: carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5. Enzyme Commission Number: EC 3.4.17.2. Purity: >90% (SDS-PAGE test). Mole weight: About 35kDa (SDS-PAGE detection). Activity: >180U/mg. Appearance: White powder, lyophilized. Storage: Redissolved in 20% glycerol, 4°C, store at -20°C for long-term preservation, Avoid multiple freeze-thaw cycles. Form: Freeze dried powder. Source: Porcine. carboxypeptidase B; protaminase; C | |
| Carboxypeptidase-B rat, Recombinant | Carboxypeptidase B (or peptidyl-L-lysine (-L-arginine) hydrolase) catalyzes the hydrolysis of the basic amino acids, lysine, arginine, and ornithine from the C-terminal position of polypeptides. It has been shown to be a single polypeptide of 34 kDa Da. Trypsin is capable of converting native enzyme to the active enzyme, carboxypeptidase B II in vitro. The optimum pH is found to be 9.0. The enzyme may be used for sequence analysis by successive cleavage of C-terminal basic amino acids. It can also be used as a serum marker for the diagnosis of acute pancreatitis. Caspase 3 is synthesized as a 32 kda proenzyme. the active enzyme is a heterodimer of two large (17 kda) subunit...sponsible for rapidly metabolizing the c5a protein into c5a des-arg, with one less amino acid. Group: Enzymes. Synonyms: carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5. Enzyme Commission Number: EC 3.4.17.2. CAS No. 9025-24-5. CPB1. Activity: 50-55 units/mg protein carboxypeptidase B. Storage: -20°C. Form: Lyophilized from 20 mM Tris, pH 8.0 + 50 mM NaCl. Source: E. coli. Species: Rat. carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5. Cat No: NATE-0153. | |
| Cathepsin D from Human, recombinant | Cathepsin D is a lysosomal aspartyl protease composed of a protein dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. It is an estrogen-regulated protein associated with tissue breakdown. Levels of cathepsin D have been positively correlated with recurring breast cancers of both node negative and node positive types. Additionally cathepsin D has been associated with amyloid formation in Alzheimer's plaques. Cathepsin D is produced initially as a pre-pro-enzyme which gets transported to lysosomes via endosomes in most cell types. In endosomes, it gets proteolyzed by unidentified proteases by removal of the pro-peptide to generate...e cathepsins B and L generates mature, active double-chain Cathepsin D. Group: Enzymes. Synonyms: CTSD; 9025-26-7; EC 3.4.23.5; CLN10; CPSD; HEL-S-130P; Procathepsin D. Enzyme Commission Number: EC 3.4.23.5. CAS No. 9025-26-7. Purity: > 80% by SDS-PAGE. CTSD. Mole weight: 45.1 kDa. Activity: >100 pmol/min/mg. Storage: Store at -20°C. Stable for at least 6 months as supplied. Reconstitute to 1 mg/ml in sterile water, store at -80°C in aliquots and use within 6 months after reconstitution. Avoid repeated freeze-thaw cycles. Form: Freeze-Dried. Source: E. coli. Species: Human. CTSD; cathepsin D; 9025-26-7; EC 3.4.23.5; CLN10; CPSD; HEL-S-130P; Procathepsin D. Cat No: NATE-1707. | |
| CCA tRNA nucleotidyltransferase | The acylation of all tRNAs with an amino acid occurs at the terminal ribose of a 3' CCA sequence. The CCA sequence is added to the tRNA precursor by stepwise nucleotide addition performed by a single enzyme that is ubiquitous in all living organisms. Although the enzyme has the option of releasing the product after each addition, it prefers to stay bound to the product and proceed with the next addition. Group: Enzymes. Synonyms: CCA-adding enzyme; tRNA adenylyltransferase; tRNA cytidylyltransferase; tRNA CCA-pyrophosphorylase; tRNA-nucleotidyltransferase; transfer-RNA nucleotidyltransferase; transfer ribonucleic acid nucleotidyl transferase; C. Enzyme Commission Number: EC 2.7.7.72. 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-3284; CCA tRNA nucleotidyltransferase; EC 2.7.7.72; CCA-adding enzyme; tRNA adenylyltransferase; tRNA cytidylyltransferase; tRNA CCA-pyrophosphorylase; tRNA-nucleotidyltransferase; transfer-RNA nucleotidyltransferase; transfer ribonucleic acid nucleotidyl transferase; CTP(ATP):tRNA nucleotidyltransferase; transfer ribonucleate adenylyltransferase; transfer ribonucleate adenyltransferase; transfer RNA adenylyltransferase; transfer ribonucleate nucleotidyltransferase; ATP (CTP):tRNA nucleotidyltransferase; ribonucleic cytidylic cytidylic | |
| CC-preferring endodeoxyribonuclease | Prefers CC sites in double-stranded circular and linear DNA. Greater affinity for double-stranded than single-stranded DNA. Produces nicks, generating double-stranded fragments with 5'- and/or 3'-protruding single-stranded tails. Requires magnesium ions for activity. The endonuclease from Chlorella-like green algae infected with NYs-1 virus 4 may be the same enzyme. Group: Enzymes. Synonyms: Streptomyces glaucescens exocytoplasmic dodeoxyribonuclease. Enzyme Commission Number: EC 3.1.21.6. CAS No. 37211-67-9. 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-3576; CC-preferring endodeoxyribonuclease; EC 3.1.21.6; 37211-67-9; Streptomyces glaucescens exocytoplasmic dodeoxyribonuclease. Cat No: EXWM-3576. | |
| CEP-9722 | CEP-9722 is a small-molecule prodrug of CEP-8983, a novel 4-methoxy-carbazole inhibitor of the nuclear enzymes poly(ADP-ribose) polymerase (PARP) 1 and 2, with potential antineoplastic activity. Upon administration and conversion from CEP-9722, CEP-8983 selectively binds to PARP 1 and 2, preventing repair of damaged DNA via base excision repair (BER). This agent enhances the accumulation of DNA strand breaks and promotes genomic instability and apoptosis. CEP-8983 may potentiate the cytotoxicity of DNA-damaging agents and reverse tumor cell chemo- and radioresistance. PARP catalyzes post-translational ADP-ribosylation of nuclear proteins that signal and recruit other proteins to repair damaged DNA and can be activated by single strand breaks in DNA. Synonyms: CEP 9722; CEP9722; 11-methoxy-2-((4-methylpiperazin-1-yl)methyl)-4,5,6,7-tetrahydro-1H-cyclopenta[a]pyrrolo[3,4-c]carbazole-1,3(2H)-dione. CAS No. 916574-83-9. Molecular formula: C24H26N4O3. Mole weight: 418.49. | |
| cob(I)yrinic acid a,c-diamide adenosyltransferase | The corrinoid adenosylation pathway comprises three steps: (I) reduction of Co(III) to Co(II) by a one-electron transfer. This can be carried out by EC 1.16.1.3, aquacobalamin reductase or non-enzymically in the presence of dihydroflavin nucleotides. (II) Co(II) is reduced to Co(I) in a second single-electron transfer by EC 1.16.1.4, cob(II)alamin reductase and (iII) the Co(I) conducts a nucleophilic attack on the adenosyl moiety of ATP to leave the cobalt atom in a Co(III) state (EC 2.5.1.17). The enzyme responsible for the adenosylation reaction is the product of the gene cobO in the aerobic bacterium Pseudomonas denitrificans and of the gene cobA in the anaerobic ...I)alamin adenosyltransferase; aquacob(I)alamin adenosyltransferase; aquocob(I)alamin vitamin B12s adenosyltransferase; ATP:cob(I)alamin Coβ-adenosyltransferase. Enzyme Commission Number: EC 2.5.1.17. CAS No. 37277-84-2. 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-2753; cob(I)yrinic acid a,c-diamide adenosyltransferase; EC 2.5.1.17; 37277-84-2; CobA; CobO; ATP:corrinoid adenosyltransferase; cob(I)alamin adenosyltransferase; aquacob(I)alamin adenosyltransferase; aquocob(I)alamin vitamin B12s adenosyltransferase; ATP:cob(I)alamin Coβ-adenosyltransferase. Cat No: EXWM-2753. | |
| Collagenase/Neutral Protease Blend (GMP Grade) | NATE-1917 is an avian and mammalian tissue-free Collagenase and neutral protease enzyme blend produced under GMP quality conditions. Applications: Nate-1917 is specifically designed for stem cell isolation from human and other adipose tissue with following advantages:o a single, sterile, ready-to-use vial containing both collagenase and neutral protease can digest up to 280g of adipose tissue with best-in-class gmp quality and shelf life of up to 72 months.o currently included in ide applications approved by the u.s. fda for alopecia, chronic heart failure, hamstring injuries, osteoarthritis of the knee, and hand manifestations of scleroderma.o research protocols are a...sociation of nucleated cells from adipose tissue.o produced using avian and mammalian tissue-free raw materials, aseptic processes and sterile filtration under gmp guidelines to assure the lowest levels of impurities and stringent quality standards. Group: Enzymes. Synonyms: Collagenase/Neutral Protease Blend; GMP, Collagenase/Neutral Protease Blend; Collagenase; Neutral Protease; GMP. Collagenase. Stability: 48 months at -15 to -25° C. Appearance: White lyophilizate. Source: Clostridium histolyticum/Bacillus polymyxa. Collagenase/Neutral Protease Blend; GMP, Collagenase/Neutral Protease Blend; Collagenase; Neutral Protease; GMP. Pack: 1 vial, 35 mg. Cat No: NATE-1917. | |
| crossover junction endodeoxyribonuclease | The enzyme from Saccharomyces cerevisiae has no endonuclease or exonuclease activity on single-stranded or double-stranded DNA molecules that do not contain Holliday junctions. Group: Enzymes. Synonyms: Hje endonuclease; Holliday junction endonuclease CCE1; Holliday junction resolvase; Holliday junction-cleaving endonuclease; Holliday junction-resolving endoribonuclease; RusA Holliday junction resolvase; RusA endonuclease; RuvC endonuclease; SpCCe1 Holliday junction resolvase; crossover junction endoribonuclease; cruciform-cutting endonuclease; endo X3; endonuclease RuvC; endonuclease VII; endonuclease X3; resolving enzyme CCE1. Enzyme Commission Number: EC 3.1.22.4. CAS No. 99676-43-4. 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-3582; crossover junction endodeoxyribonuclease; EC 3.1.22.4; 99676-43-4; Hje endonuclease; Holliday junction endonuclease CCE1; Holliday junction resolvase; Holliday junction-cleaving endonuclease; Holliday junction-resolving endoribonuclease; RusA Holliday junction resolvase; RusA endonuclease; RuvC endonuclease; SpCCe1 Holliday junction resolvase; crossover junction endoribonuclease; cruciform-cutting endonuclease; endo X3; endonuclease RuvC; endonuclease VII; endonuclease X3; resolving enzyme CCE1. Cat No: EXWM-3582. | |
| Cysteine protease from Streptococcus pyogenes, Recombinant | Cysteine protease is an enzyme for single site digestion of antibodies in the hinge region. Incubation for one hour at 37°C under reducing conditions is enough for cysteine protease to cleave all subclasses of human, mouse, rat, goat and sheep IgG. Cysteine protease is supplied as lyophilized powder with no preservatives added and is available in a 2000 units pack size. Cysteine protease contains a His-tag and can easily be removed after digestion. Group: Enzymes. Synonyms: Cysteine protease; FabULOUS. Purity: > 95% homogeneity as determined by SDS-PAGE analysis using Coomassie Blue detection. Cysteine protease. Stability: The enzyme is reconstituted by addition of water and after reconstitution it is stable for 1 month at +4-8°C. The product is shipped on ice and should be stored at -20°C upon arrival. Appearance: White to light yellow powder. Storage: at -20°C. Form: Lyophilized powder with no preservatives added. Source: E.coli. Species: Streptocoocus pyogenes. Cysteine protease; FabULOUS Enzyme; FabULOUS; protease. Cat No: NATE-1600. | |
| dCTP deaminase (dUMP-forming) | Requires Mg2+. Is highly specific for dCTP as substrate as dCMP, CTP, CDP, CMP, cytosine or deoxycytosine are not deaminated. While most bacteria require two enzymes to form dUMP from dCTP (EC 3.5.4.13, dCTP deaminase and EC 3.6.1.23, dUTP diphosphatase), the archaeon Methanocaldococcus jannaschii uses a single enzyme to carry out both functions. This enzyme can also act as a dUTP diphosphatase, but more slowly. Group: Enzymes. Enzyme Commission Number: EC 3.5.4.30. 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-4558; dCTP deaminase (dUMP-forming); EC 3.5.4.30. Cat No: EXWM-4558. | |
| Δ12 acyl-lipid conjugase (11E,13E-forming) | The enzyme, characterized from the plants Impatiens balsamina, Momordica charantia (bitter gourd) and Vernicia fordii (tung tree), converts a single cis double bond at carbon 12 to two conjugated trans bonds at positions 11 and 13. The enzyme from Vernicia fordii can also act as a 12(E) desaturase when acting on the monounsaturated fatty acids oleate and palmitoleate. cf. EC 1.14.19.16, linoleoyl-lipid Δ12 conjugase (11E,13Z-forming). Group: Enzymes. Synonyms: fatty acid Δ12-conjugase (ambiguous); FADX (gene name). Enzyme Commission Number: EC 1.14.19.33. 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-0997; Δ12 acyl-lipid conjugase (11E,13E-forming); EC 1.14.19.33; fatty acid Δ12-conjugase (ambiguous); FADX (gene name). Cat No: EXWM-0997. | |
| deoxyribonuclease IV | The enzyme is an apurinic/apyrimidinic (AP) site endonuclease that primes DNA repair synthesis at AP sites. It specifically cleaves the DNA backbone at AP sites and also removes 3' DNA-blocking groups such as 3' phosphates, 3' phosphoglycolates, and 3' α,β-unsaturated aldehydes that arise from oxidative base damage and the activity of combined glycosylase/lyase enzymes. It is also the only known repair enzyme that is able to cleave the DNA backbone 5' of the oxidative lesion α-deoxyadenosine. The enzyme has a strong preference for single-stranded DNA. Group: Enzymes. Synonyms: deoxyribonuclease IV. coli endonuclease IV; endodeoxyribonuclease (misleading); redoxyendonuclease; deoxriboendonuclease (misleading); endonuclease II; endonuclease IV; DNA-adenine-transferase; nfo (gene name). Enzyme Commission Number: EC 3.1.21.2. CAS No. 63363-78-0. 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-3572; deoxyribonuclease IV; EC 3.1.21.2; 63363-78-0; deoxyribonuclease IV (phage-T4-induced) (misleading); endodeoxyribonuclease IV (phage T4-induced) (misleading); E. coli endonuclease IV; endodeoxyribonuclease (misleading); redoxyendonuclease; deoxriboendonuclease (misleading); endonuclease II; endonuclease IV; DNA-adenine-transferase; nfo (gene name). Cat No: EXWM-3572. | |
| deoxyribonuclease X | Preference for supercoiled DNA; little activity on linear double-stranded DNA. Inhibited by single-stranded DNA, ATP and AMP. Group: Enzymes. Synonyms: Escherichia coli endodeoxyribonuclease; Escherichia coli endodeoxyribonuclease X. Enzyme Commission Number: EC 3.1.22.5. CAS No. 97002-82-9. 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-3583; deoxyribonuclease X; EC 3.1.22.5; 97002-82-9; Escherichia coli endodeoxyribonuclease; Escherichia coli endodeoxyribonuclease X. Cat No: EXWM-3583. | |
| dihydrofolate synthase | In some bacteria, a single protein catalyses both this activity and that of EC 6.3.2.17, tetrahydrofolate synthase, the combined activity of which leads to the formation of the coenzyme polyglutamated tetrahydropteroate (H4PteGlun), i.e. various tetrahydrofolates. In contrast, the activities are located on separate proteins in most eukaryotes studied to date. This enzyme is reponsible for attaching the first glutamate residue to dihydropteroate to form dihydrofolate and is present only in those organisms that have the ability to synthesize tetrahydrofolate de novo, e.g. plants, most bacteria, fungi and protozoa. Group: Enzymes. Synonyms: dihydrofolate synthetase; 7,8-dihydrofolate synthetase; H2-folate synthetase; 7,8-dihydropteroate:L-glutamate ligase (ADP); dihydropteroate:L-glutamate ligase (ADP-forming); DHFS. Enzyme Commission Number: EC 6.3.2.12. CAS No. 37318-62-0. 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-5733; dihydrofolate synthase; EC 6.3.2.12; 37318-62-0; dihydrofolate synthetase; 7,8-dihydrofolate synthetase; H2-folate synthetase; 7,8-dihydropteroate:L-glutamate ligase (ADP); dihydropteroate:L-glutamate ligase (ADP-forming); DHFS. Cat No: EXWM-5733. | |
| 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. | |
| dinoflagellate luciferase | A luciferase from dinoflagelates such as Gonyaulax polyedra, Lingulodinium polyedrum, Noctiluca scintillans, and Pyrocystis lunula. It is a single protein with three luciferase domains. The luciferin is strongly bound by a luciferin binding protein above a pH of 7. Group: Enzymes. Synonyms: (dinoflagellate luciferin) luciferase; Gonyaulax luciferase. Enzyme Commission Number: EC 1.13.12.18. CAS No. 303183-71-3. 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-0610; dinoflagellate luciferase; EC 1.13.12.18; 303183-71-3; (dinoflagellate luciferin) luciferase; Gonyaulax luciferase. Cat No: EXWM-0610. | |
| Disulfide Bond Isomerase, Recombinant | Dsb proteins (DsbA, DsbB, DsbC, and DsbD) catalyze formation and isomerization of protein disulfide bonds in the periplasm of Escherichia coli. DsbC is periplasmic enzyme known as a disulfide isomerase and can convert aberrant disulfide bonds to correct ones. Disulfide-bond isomerase recombinant produced in e. coli is a single, non-glycosylated, polypeptide chain containing 216 amino acids (21-236) and having a molecular mass of 23.5 kda. dsbc is purified by proprietary chromatographic techniques. Applications: Western blot; elisa. Group: Enzymes. Synonyms: DsbC; Thiol:disulfide interchange protein dsbC. Purity: Greater than 95.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. DsbC. Mole weight: 23.5 kDa. Stability: Disulfide-Bond Isomerase Recombinant although stable at 4°C for 1 week, should be stored desiccated below -18°C. Please prevent freeze-thaw cycles. Appearance: Sterile filtered colorless solution. Source: E. coli. DsbC; Thiol:disulfide interchange protein dsbC. Cat No: NATE-0827. | |
| D-lactate dehydratase | The enzyme converts methylglyoxal to D-lactate in a single glutathione (GSH)-independent step. The other known route for this conversion is the two-step GSH-dependent pathway catalysed by EC 4.4.1.5 (lactoylglutathione lyase) and EC 3.1.2.6 (hydroxyacylglutathione hydrolase). Group: Enzymes. Synonyms: glyoxylase III. Enzyme Commission Number: EC 4.2.1.130. 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-4971; D-lactate dehydratase; EC 4.2.1.130; glyoxylase III. Cat No: EXWM-4971. | |
| DNA ligase (ATP) | The enzyme catalyses the ligation of DNA strands with 3'-hydroxyl and 5'-phosphate termini, forming a phosphodiester and sealing certain types of single-strand breaks in duplex DNA. Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by ATP, forming a phosphoramide bond between adenylate and a lysine residue. The adenylate group is then transferred to the 5'-phosphate terminus of the substrate, forming the capped structure 5'-(5'-diphosphoadenosine)-[DNA]. Finally, the enzyme catalyses a nucleophilic attack of the 3'-OH terminus on the capped terminus, which results in formation of the phosphodiester bond and release of the adenylate. RNA can also act as substrate, to some extent. cf. EC 6.5.1.2, DNA ligase (NAD+), EC 6.5.1.6, DNA ligase (ATP or NAD+), and EC 6.5.1.7, DNA ligase (ATP, ADP or GTP). Group: Enzymes. Synonyms: polydeoxyribonucleotide synthase (ATP);. Enzyme Commission Number: EC 6.5.1.1. CAS No. 9015-85-4. 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-5820; DNA ligase (ATP); EC 6.5.1.1; 9015-85-4; polydeoxyribonucleotide synthase (ATP); polynucleotide ligase (ambiguous); sealase; DNA repair enzyme (ambiguous); DNA joinase (ambiguous); DNA ligase (ambiguous); deoxyribonucleic ligase (ambiguous); deoxyribonucleate ligase (ambiguou | |
| DNA ligase (NAD+) | Catalyses the formation of a phosphodiester at the site of a single-strand break in duplex DNA. RNA can also act as substrate, to some extent. cf. EC 6.5.1.1, DNA ligase (ATP), EC 6.5.1.6, DNA ligase (ATP or NAD+), and EC 6.5.1.7, DNA ligase (ATP, ADP or GTP). Group: Enzymes. Synonyms: polydeoxyribonucleotide synthase (NAD+); polynucleotide ligase (NAD+); DNA repair enzyme (ambiguous); DNA joinase (ambiguous); polynucleotide synthetase (nicotinamide ad. Enzyme Commission Number: EC 6.5.1.2. CAS No. 37259-52-2. 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-5821; DNA ligase (NAD+); EC 6.5.1.2; 37259-52-2; polydeoxyribonucleotide synthase (NAD+); polynucleotide ligase (NAD+); DNA repair enzyme (ambiguous); DNA joinase (ambiguous); polynucleotide synthetase (nicotinamide adenine dinucleotide); deoxyribonucleic-joining enzyme (ambiguous); deoxyribonucleic ligase (ambiguous); deoxyribonucleic repair enzyme (ambiguous); deoxyribonucleic joinase (ambiguous); DNA ligase (ambiguous); deoxyribonucleate ligase (ambiguous); polynucleotide ligase (ambiguous); deoxyribonucleic acid ligase (ambiguous); polynucleotide synthetase (ambiguous); deoxyribonucleic acid joinase (ambiguous); DNA-joining enzyme (ambiguous); polynucleotide ligase (nicotinamide adenine dinucleotide). Cat No: EXWM-5821. | |
| DNA oxidative demethylase | Contains iron; activity is slightly stimulated by ascorbate. Catalyses oxidative demethylation of the DNA base lesions N1-methyladenine, N3-methylcytosine, N1-methylguanine, and N3-methylthymine. It works better on single-stranded DNA (ssDNA) and is capable of repairing damaged bases in RNA. Group: Enzymes. Synonyms: alkylated DNA repair protein; α-ketoglutarate-dependent dioxygenase ABH1; alkB (gene name). Enzyme Commission Number: EC 1.14.11.33. 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-0651; DNA oxidative demethylase; EC 1.14.11.33; alkylated DNA repair protein; α-ketoglutarate-dependent dioxygenase ABH1; alkB (gene name). Cat No: EXWM-0651. | |
| DNA Polymerase for PAGE | DNA Polymerase for PAGE. Dna polymerase for page is purified from e. coliexpressing a cloned dna polymerase from thermus aquaticus. the enzyme consists of a single polypeptide with a molecular weight of approximately 94 kda. dna polymerase for page has 5?-3? dna polymerase activity and 5?-3? exonuclease activity. lt lacks 3?-5? exonuclease activity. this enzyme is supplied with unique buffer, and its pcr product is suitable for sds-page and agarose gel electrophoresis. Group: Cloning Enzymes. Purity: 2500U. Storage: Store at -20 ?. Cat No: CE-3004. | |
| DNA topoisomerase | These enzymes bring about the conversion of one topological isomer of DNA into another, e.g., the relaxation of superhelical turns in DNA, the interconversion of simple and knotted rings of single-stranded DNA, and the intertwisting of single-stranded rings of complementary sequences, cf. EC 5.99.1.3 DNA topoisomerase (ATP-hydrolysing). Group: Enzymes. Synonyms: type I DNA topoisomerase; untwisting enzyme; relaxing enzyme; nicking-closing enzyme; swivelase; ω-protein; deoxyribonucleate topoisomerase; topoisomerase; type I DNA topoisomerase. Enzyme Commission Number: EC 5.99.1.2. CAS No. 80449-01-0. TOPO I. 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-5637; DNA topoisomerase; EC 5.99.1.2; 80449-01-0; type I DNA topoisomerase; untwisting enzyme; relaxing enzyme; nicking-closing enzyme; swivelase; ω-protein; deoxyribonucleate topoisomerase; topoisomerase; type I DNA topoisomerase. Cat No: EXWM-5637. | |
| double-stranded uracil-DNA glycosylase | No activity on DNA containing a T/G mispair or single-stranded DNA containing either a site-specific uracil or 3,N4-ethenocytosine residue, significant role for double-stranded uracil-DNA glycosylase in mutation avoidance in non-dividing E. coli. Uracil-DNA glycosylases are widespread enzymes that are found in all living organisms. Uracil-DNA glycosylase (EC 3.2.2.27) and EC 3.2.2.28 form a central part of the DNA-repair machinery since they initiate the DNA base-excision repair pathway by hydrolysing the N-glycosidic bond between uracil and the deoxyribose sugar thereby catalysing the removal of mis-incorporated uracil from DNA. Group: Enzymes. Synonyms: Mug; double-strand uracil-DNA glycosylase; Dug; dsUDG; double-stranded DNA specific UDG; dsDNA specific UDG; UdgB (ambiguous); G:T/U mismatch-specific DNA glycosylase; UDG (ambiguous). Enzyme Commission Number: EC 3.2.2.28. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3982; double-stranded uracil-DNA glycosylase; EC 3.2.2.28; Mug; double-strand uracil-DNA glycosylase; Dug; dsUDG; double-stranded DNA specific UDG; dsDNA specific UDG; UdgB (ambiguous); G:T/U mismatch-specific DNA glycosylase; UDG (ambiguous). Cat No: EXWM-3982. | |
| (E3-independent) E2 ubiquitin-conjugating enzyme | The enzyme transfers a single ubiquitin directly from an ubiquitinated E1 ubiquitin-activating enzyme to itself, and on to a lysine residue of the acceptor protein without involvement of E3 ubiquitin transferases (cf. EC 2.3.2.26, EC 2.3.2.27). It forms a labile ubiquitin adduct in the presence of E1, ubiquitin, and Mg2+-ATP and catalyses the conjugation of ubiquitin to protein substrates, independently of E3. This transfer has only been observed with small proteins. In vitro a transfer to small acceptors (e.g. L-lysine, N-acetyl-L-lysine methyl ester) has been observed. Group: Enzymes. Synonyms: E2-230K; UBE2O; E3-independent ubiquitin-conjugating enzyme E2. Enzyme Commission Number: EC 2.3.2.24. 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-2298; (E3-independent) E2 ubiquitin-conjugating enzyme; EC 2.3.2.24; E2-230K; UBE2O; E3-independent ubiquitin-conjugating enzyme E2. Cat No: EXWM-2298. | |
| E7016 | E7016 is an inhibitor of the nuclear enzyme poly(ADP-ribose) polymerase (PARP) with potential chemo- and/or radiosensitizing activity. PARP inhibitor E7016 selectively binds to PARP and prevents PARP-mediated DNA repair of single strand DNA breaks via the base-excision repair pathway. This enhances the accumulation of DNA strand breaks and promotes genomic instability and eventually leads to apoptosis. In addition, this agent may enhance the cytotoxicity of DNA-damaging agents and reverse tumor cell resistance to chemotherapy and radiation therapy. PARP catalyzes post-translational ADP-ribosylation of nuclear proteins that signal and recruit other proteins to repair damaged DNA and is activated by single-strand DNA breaks. Synonyms: E 7016; E-7016; 10-((4-Hydroxypiperidin-1-yl)methyl)chromeno[4,3,2-de]phthalazin-3(2H)-one. Grades: ≥98%. CAS No. 902128-92-1. Molecular formula: C20H19N3O3. Mole weight: 349.39. | |
| EDA-ATP - ATTO-655 | EDA-ATP - ATTO-655, a fluorescent probe of utmost importance in biomedical research with its unwavering ability to label ATP binding proteins; paving the way for multiphoton microscopy and single-molecule imaging. With its capabilities, it also opens up opportunities to study drug development for ATP-dependent enzymes and ion channels. Synonyms: 2'/3'-O-(2-Aminoethyl-carbamoyl)-Adenosine-5'-triphosphate, labeled with ATTO 655, Triethylammonium salt. Grades: ≥ 95 % by HPLC. Molecular formula: C13H22N7O14P3- ATTO 655 (free acid). Mole weight: 1102.27 (free acid). | |
| Edotecarin | Edotecarin is a synthetic indolocarbazole with antineoplastic activity. Edotecarin inhibits the enzyme topoisomerase I through stabilization of the DNA-enzyme complex and enhanced single-strand DNA cleavage, resulting in inhibition of DNA replication and decreased tumor cell proliferation. Synonyms: J 107088; PF 804950; 5H-Indolo[2,3-a]pyrrolo[3,4-c]carbazole-5,7(6H)-dione, 12-β-D-glucopyranosyl-12,13-dihydro-2,10-dihydroxy-6-[[2-hydroxy-1-(hydroxymethyl)ethyl]amino]-; 6-[(1,3-Dihydroxy-2-propanyl)amino]-12-(β-D-glucopyranosyl)-2,10-dihydroxy-12,13-dihydro-5H-indolo[2,3-a]pyrrolo[3,4-c]carbazole-5,7(6H)-dione. Grades: ≥95%. CAS No. 174402-32-5. Molecular formula: C29H28N4O11. Mole weight: 608.56. | |
| enterobactin synthase | This enzyme complex catalyses the conversion of three molecules each of 2,3-dihydroxybenzoate and L-serine to form the siderophore enterobactin. In Escherichia coli the complex is formed by EntB (an aryl carrier protein that has to be activated by 4'-phosphopantetheine), EntD (a phosphopantetheinyl transferase that activates EntB), EntE (catalyses the ATP-dependent condensation of 2,3-dihydroxybenzoate and holo-EntB to form the covalently arylated form of EntB), and EntF (a four domain protein that catalyses the activation of L-serine by ATP, the condensation of the activated L-serine with the activated 2,3-dihydroxybenzoate, and the trimerization of three such moieties to a single enterobactin molecule). Group: Enzymes. Synonyms: N-(2,3-dihydroxybenzoyl)-serine synthetase; 2,3-dihydroxybenzoylserine synthetase; 2,3-dihydroxybenzoate-serine ligase. Enzyme Commission Number: EC 6.3.2.14. CAS No. 37318-63-1. 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-5735; enterobactin synthase; EC 6.3.2.14; 37318-63-1; N-(2,3-dihydroxybenzoyl)-serine synthetase; 2,3-dihydroxybenzoylserine synthetase; 2,3-dihydroxybenzoate-serine ligase. Cat No: EXWM-5735. | |
| epi-cedrol synthase | The enzyme is activated by Mg2+. Similar to many other plant terpenoid synthases, this enzyme produces many products from a single substrate. The predominant product is the cyclic sesquiterpenoid alcohol, 8-epi-cedrol, with minor products including cedrol and the olefins α-cedrene, β-cedrene, (E)-β-farnesene and (E)-α-bisabolene. Group: Enzymes. Synonyms: 8-epicedrol synthase; epicedrol synthase. Enzyme Commission Number: EC 4.2.3.39. 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-5197; epi-cedrol synthase; EC 4.2.3.39; 8-epicedrol synthase; epicedrol synthase. Cat No: EXWM-5197. | |
| exodeoxyribonuclease I | Preference for single-stranded DNA. The Escherichia coli enzyme hydrolyses glucosylated DNA. Group: Enzymes. Synonyms: Escherichia coli exonuclease I; E. coli exonuclease I; exonuclease I. Enzyme Commission Number: EC 3.1.11.1. CAS No. 9037-46-1. 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-3529; exodeoxyribonuclease I; EC 3.1.11.1; 9037-46-1; Escherichia coli exonuclease I; E. coli exonuclease I; exonuclease I. Cat No: EXWM-3529. | |
| exodeoxyribonuclease (lambda-induced) | Preference for double-stranded DNA. Does not attack single-strand breaks. Group: Enzymes. Synonyms: lambda exonuclease; phage lambda-induced exonuclease; Escherichia coli exonuclease IV; E. coli exonuclease IV; exodeoxyribonuclease IV; exonuclease IV. Enzyme Commission Number: EC 3.1.11.3. CAS No. 37367-70-7. 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-3531; exodeoxyribonuclease (lambda-induced); EC 3.1.11.3; 37367-70-7; lambda exonuclease; phage lambda-induced exonuclease; Escherichia coli exonuclease IV; E. coli exonuclease IV; exodeoxyribonuclease IV; exonuclease IV. Cat No: EXWM-3531. | |
| exodeoxyribonuclease (phage SP3-induced) | Preference for single-stranded DNA. Group: Enzymes. Synonyms: phage SP3 DNase; DNA 5'-dinucleotidohydrolase; deoxyribonucleate 5'-dinucleotidase; deoxyribonucleic 5'-dinucleotidohydrolase; bacteriophage SP3 deoxyribonuclease; deoxyribonucleate 5'-dinucleotidase. Enzyme Commission Number: EC 3.1.11.4. CAS No. 37288-30-5. 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-3532; exodeoxyribonuclease (phage SP3-induced); EC 3.1.11.4; 37288-30-5; phage SP3 DNase; DNA 5'-dinucleotidohydrolase; deoxyribonucleate 5'-dinucleotidase; deoxyribonucleic 5'-dinucleotidohydrolase; bacteriophage SP3 deoxyribonuclease; deoxyribonucleate 5'-dinucleotidase. Cat No: EXWM-3532. | |
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