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| Product | Description | |
|---|---|---|
| prenylcysteine oxidase | A flavoprotein (FAD). Cleaves the thioether bond of S-prenyl-L-cysteines, such as S-farnesylcysteine and S-geranylgeranylcysteine. N-Acetyl-prenylcysteine and prenylcysteinyl peptides are not substrates. May represent the final step in the degradation of prenylated proteins in mammalian tissues. Originally thought to be a simple lyase so it had been classified as EC 4.4.1.18. Group: Enzymes. Synonyms: prenylcysteine lyase. Enzyme Commission Number: EC 1.8.3.5. CAS No. 196717-99-4. 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-1662; prenylcysteine oxidase; EC 1.8.3.5; 196717-99-4; prenylcysteine lyase. Cat No: EXWM-1662. |  |
| cysteine dioxygenase | Requires Fe2+ and NAD(P)H. Group: Enzymes. Synonyms: cysteine oxidase. Enzyme Commission Number: EC 1.13.11.20. CAS No. 37256-59-0. 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-0540; cysteine dioxygenase; EC 1.13.11.20; 37256-59-0; cysteine oxidase. Cat No: EXWM-0540. | |
| farnesylcysteine lyase | A flavoprotein (FAD). In contrast to mammalian EC 1.8.3.5 (prenylcysteine oxidase) the farnesylcysteine lyase from Arabidopsis is specific for S-farnesyl-L-cysteine and shows no activity with S-geranylgeranyl-L-cysteine. Group: Enzymes. Synonyms: FC lyase; FCLY. Enzyme Commission Number: EC 1.8.3.6. 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-1663; farnesylcysteine lyase; EC 1.8.3.6; FC lyase; FCLY. Cat No: EXWM-1663. | |
| glutathione oxidase | A flavoprotein (FAD). Also acts, more slowly, on L-cysteine and several other thiols. Group: Enzymes. Enzyme Commission Number: EC 1.8.3.3. CAS No. 55467-56-6. 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-1660; glutathione oxidase; EC 1.8.3.3; 55467-56-6. Cat No: EXWM-1660. | |
| N-Acetylcysteine Amide | N-Acetylcysteine amide is a blood brain barrier permeant and cell membranes thiol antioxidant with anti-inflamatory activity via regulation of activation of NF-κB and HIF-1α as well as modulation of ROS. It readily crosses cell membranes, replenishes intracellular GSH, and defends the cell from oxidative stress. It may be used in research and exploration for the treatment of radiation exposure, neurodegeneration and other oxidation-mediated disorders. It is also used for the treatment of acquired immune deficiency syndrome and HIV infection. It is also used as an authentic imaging probe for accurate tracing of cells viability from beginning to end to distinguish apoptotic and necrotic cells. It improves neuronal mitochondrial bioenergetics, reduces tissue damage and enhances behavioral recovery in rats following traumatic brain injury. It is a neuroprotective agent. Synonyms: (2R)-2-(Acetylamino)-3-mercaptopropanamide;N-Acetyl-L-cysteinamide. CAS No. 38520-57-9. Molecular formula: C5H10N2O2S. Mole weight: 162.21. |  |
| Native Aspergillus niger Glucose Oxidase | The glucose oxidase enzyme (GOx) also known as notatin (EC number 1.1.3.4) is an oxido-reductase that catalyses the oxidation of glucose to hydrogen peroxide and D-glucono-δ-lactone. This enzyme is produced by certain species of fungi and insects and displays antibacterial activity when oxygen and glucose are present. Glucose oxidase from aspergillus niger is a dimer consisting of 2 equal subunits with a molecular mass of 80 kda each. each subunit contains one flavin adenine dinulceotide moiety and one iron. the enzyme is a glycoprotein containing ~16% neutral sugar and 2% amino sugars. the enzyme also contains 3 cysteine residues and 8 potential sites for n-linked ...xidase oxidizes β-d-glucose to d-gluconolactate and hydrogen peroxide, horseradish peroxidase is often used as the coupling enzyme for glucose determination. although glucose oxidase is specific for β-d-glucose, solutions of d-glucose can be quantified as α-d-glucose will mutorotate to β-d-glucose as the β-d-glucose is consumed by the enzymatic reaction. Applications: Glucose oxidase is widely used in the food and pharmaceutical industries as well as a major component of glucose biosensors. Group: Enzymes. Synonyms: EC 1.1.3.4; glucose oxyhydrase; corylophyline; penatin; glucose aerodehydrogenase; microcid; β-D-glucose oxidase; D-glucose oxi | |
| Native Plant origin Diamine Oxidase | DAO is an enzyme (EC 1.4.3.22) composed of 642 amino acids. It is a homo-dimer of two identical subunits. Each subunit contains 2 disulfide bounds and a free cysteine with a theoretical molecular weight of 72,878 daltons per unit (a nominal molecular weight of 73 ±3 kDa is used for analytical purposes). DAO active site contains copper (II) and phenylalanine quinone: 2,4,5-trihydroxyphenylalanine quinone (TPQ). The products of the CuAO-catalysed oxidative deamination of amines such as histamine are various aldehydes, ammonia, and hydrogen peroxide. The copper is essential for activity and is believed to play a redox role in substrate turnover.Plant DAOs (histaminase) differs...oms, various plants, and animals. A review article by R. Medda, et al. in 1995 describes in detail research in this area. Applications: Dao catalyzes the oxidation of diamines (and some monoamines) to produce the aldehyde, ammonia, and h2o2. Group: Enzymes. Synonyms: EC 1.4.3.6; 9001-53-0; Amine:oxygen oxidoreductase (deaminating) (pyridoxal-containing); Diamine Oxidase; Amine oxidase (copper-containing). Enzyme Commission Number: EC 1.4.3.6. CAS No. 9001-53-0. Diamine Oxidase. Form: Tan Liquid. Source: Pisum sativum. EC 1.4.3.6; 9001-53-0; Amine:oxygen oxidoreductase (deaminating) (pyridoxal-containing); Diamine Oxidase; Amine oxidase (copper-containing). Cat No: NATE-0188. | |
| VAS3947 | VAS3947 is a selective inhibitor of NADPH oxidase activity in low micromolar concentrations, interfering neither with ROS detection nor with XOD or eNOS activities. VAS3947 induces apoptosis in AML cells independently of its anti-NOX activity. VAS3947 thiol alkylates cysteine residues of glutathione (GSH), while also interacting with proteins. Remarkably, VAS3947 decreased detectable GSH in the MV-4-11 cell line, thereby suggesting possible oxidative stress induction. Overall, VAS3947 induces apoptosis independently of anti-NOX activity, via UPR activation, mainly due to aggregation and misfolding of proteins. Group: Inhibitors. Alternative Names: VA-S3947; VA S3947; VAS3947. CAS No. 869853-70-3. Molecular formula: C14H10N6OS. Mole weight: 310.34. Appearance: Solid powder. Purity: >98%. IUPACName: 3-Benzyl-7-(2-oxazolyl)thio-1,2,3-triazolo[4,5-d]pyrimidine. Canonical SMILES: C12=NC=NC (SC3=NC=CO3)=C1N=NN2CC4=CC=CC=C4. Catalog: ACM869853703. |  |
| xanthine dehydrogenase | Acts on a variety of purines and aldehydes, including hypoxanthine. The mammalian enzyme can also convert all-trans retinol to all-trans-retinoate, while the substrate is bound to a retinoid-binding protein. The enzyme from eukaryotes contains [2Fe-2S], FAD and a molybdenum centre. The mammalian enzyme predominantly exists as the NAD-dependent dehydrogenase (EC 1.17.1.4). During purification the enzyme is largely converted to an O2-dependent form, xanthine oxidase (EC 1.17.3.2). The conversion can be triggered by several mechanisms, including the oxidation of cysteine thiols to form disulfide bonds [which can be catalysed by EC 1.8.4.7, enzyme-thiol transhydrogenase (glutathione-disulfide) in the presence of glutathione disulfide] or limited proteolysis, which results in irreversible conversion. The conversion can also occur in vivo. Group: Enzymes. Synonyms: NAD+-xanthine dehydrogenase; xanthine-NAD+ oxidoreductase; xanthine/NAD+ oxidoreductase; xanthine oxidoreductase. Enzyme Commission Number: EC 1.17.1.4. CAS No. 9054-84-6. XDH. 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-1082; xanthine dehydrogenase; EC 1.17.1.4; 9054-84-6; NAD+-xanthine dehydrogenase; xanthine-NAD+ oxidoreductase; xanthine/NAD+ oxidoreductase; xanthine oxidoreductase. Cat No: EXWM-1082. | |
| xanthine oxidase | An iron-molybdenum flavoprotein (FAD) containing [2Fe-2S] centres. Also oxidizes hypoxanthine, some other purines and pterins, and aldehydes, but is distinct from EC 1.2.3.1, aldehyde oxidase. Under some conditions the product is mainly superoxide rather than peroxide: RH + H2O + 2 O2 = ROH + 2 O2.- + 2 H+. The mammalian enzyme predominantly exists as an NAD-dependent dehydrogenase (EC 1.17.1.4, xanthine dehydrogenase). During purification the enzyme is largely converted to the O2-dependent xanthine oxidase form (EC 1.17.3.2). The conversion can be triggered by several mechanisms, including the oxidation of cysteine thiols to form disulfide bonds [which can be catalysed by EC 1.8.4.7, enzyme-thiol transhydrogenase (glutathione-disulfide) in the presence of glutathione disulfide] or limited proteolysis, which results in irreversible conversion. The conversion can also occur in vivo. Group: Enzymes. Synonyms: hypoxanthine o. Enzyme Commission Number: EC 1.17.3.2. CAS No. 9002-17-9. 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-1088; xanthine oxidase; EC 1.17.3.2; 9002-17-9; hypoxanthine oxidase; hypoxanthine:oxygen oxidoreductase; Schardinger enzyme; xanthine oxidoreductase; hypoxanthine-xanthine oxidase; xanthine:O2 oxidoreductase; xanthine:xanthine oxidase. Cat No: EXWM-1088. | |
| Monoamine Oxidase A from Human, Recombinant | MAO's are proteins of the mitochondrial membrane. These enzymes are responsible for catalyzing oxidative deamination of endo-and xenobiotic amines. Substrate specificity differs for each isozyme. Monoamine oxidase a contains binding sites for 8α-s-cysteinyl-fad. Applications: Monoamine oxidase a has been used in a study to assess abnormal behavior in a large kindred of males where a deficiency of enzymatic activity of monamine oxidase a was found. it has also been used in a study to investigate an ass ociation between smoking and the inhibition of maoa. Group: Enzymes. Synonyms: MAO-A; MAOA; EC 1.4.3.4; Monoamine Oxidase A; adrenalin oxidase; adrenaline oxidase; amine oxidase (ambiguous); amine oxidase (flavin-containing); amine:oxygen oxidoreducta. Enzyme Commission Number: EC 1.4.3.4. CAS No. 231-791-2. Monoamine Oxidase. Storage: -70°C. Source: Baculovirus infected BTI insect cells. Species: Human. MAO-A; MAOA; EC 1.4.3.4; Monoamine Oxidase A; adrenalin oxidase; adrenaline oxidase; amine oxidase (ambiguous); amine oxidase (flavin-containing); amine:oxygen oxidoreductase (deaminating) (flavin-containing); epinephrine oxidase; monoamine:O2 oxidoreductase (deaminating); polyamine oxidase (ambiguous); serotonin deaminase; spermidine oxidase (ambiguous); spermine oxidase (ambiguous); tyraminase; tyramine oxidase. Cat No: NATE-0440. | |
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