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| Product | Description | |
|---|---|---|
| enzyme-thiol transhydrogenase (glutathione-disulfide) | Converts EC 1.17.1.4 xanthine dehydrogenase into EC 1.17.3.2 xanthine oxidase in the presence of glutathione disulfide; also reduces the disulfide bond of ricin. Not inhibited by Cu2+ or thiol reagents. Group: Enzymes. Synonyms: [xanthine-dehydrogenase]:oxidized-glutathione S-oxidoreductase; enzyme-thiol transhydrogenase (oxidized-glutathione); glutathione-dependent thiol:disulfide oxidoreductase; thiol:disulphide oxidoreductase. Enzyme Commission Number: EC 1.8.4.7. CAS No. 85030-79-1. 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-1673; enzyme-thiol transhydrogenase (glutathione-disulfide); EC 1.8.4.7; 85030-79-1; [xanthine-dehydrogenase]:oxidized-glutathione S-oxidoreductase; enzyme-thiol transhydrogenase (oxidized-glutathione); glutathione-dependent thiol:disulfide oxidoreductase; thiol:disulphide oxidoreductase. Cat No: EXWM-1673. |  |
| 3- (2-Pyridyldithio) propanoic Acid | Crosslinking agent in immobilization of thrombogenesis-inhibiting enzymes on polymeric carriers. Targeted delivery of a triplex-forming oligonucleotide to hepatic stellate cells by complexes with phosphated bovine serum albumin for treatment of liver fibrosis. Group: Biochemicals. Alternative Names: 2-Carboxyethyl 2-Pyridyl Disulfide. Grades: Highly Purified. CAS No. 68617-64-1. Pack Sizes: 100mg, 250mg, 500mg, 1g. US Biological Life Sciences. |  Worldwide |
| 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. | |
| alcohol dehydrogenase (cytochrome c) | A periplasmic PQQ-containing quinoprotein. Occurs in Pseudomonas and Rhodopseudomonas. The enzyme from Pseudomonas aeruginosa uses a specific inducible cytochrome c550 as electron acceptor. Acts on a wide range of primary and secondary alcohols, but not methanol. It has a homodimeric structure [contrasting with the heterotetrameric structure of EC 1.1.2.7, methanol dehydrogenase (cytochrome c)]. It is routinely assayed with phenazine methosulfate as electron acceptor. Activity is stimulated by ammonia or amines. 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 I quinoprotein alcohol dehydrogenase; quinoprotein ethanol dehydrogenase. Enzyme Commission Number: EC 1.1.2.8. 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-0390; alcohol dehydrogenase (cytochrome c); EC 1.1.2.8; type I quinoprotein alcohol dehydrogenase; quinoprotein ethanol dehydrogenase. Cat No: EXWM-0390. | |
| alcohol dehydrogenase (quinone) | Only described in acetic acid bacteria where it is involved in acetic acid production. Associated with membrane. Electron acceptor is membrane ubiquinone. A model structure suggests that, like all other quinoprotein alcohol dehydrogenases, the catalytic subunit 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; the catalytic subunit also has a heme c in the C-terminal domain. The enzyme has two additional subunits, one of which contains three molecules of heme c. It does not require amines for activation. It has a restricted substrate specificity, oxidizing a few primary alcohols (C2 to C6), but not methanol, secondary alcohols and some aldehydes. It is assayed with phenazine methosulfate or with ferricyanide. Group: Enzymes. Synonyms: type III ADH; membrane associated quinohaemoprotein alcohol dehydrogenase. Enzyme Commission Number: EC 1.1.5.5. 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-0433; alcohol dehydrogenase (quinone); EC 1.1.5.5; type III ADH; membrane associated quinohaemoprotein alcohol dehydrogenase. Cat No: EXWM-0433. | |
| 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. | |
| arsenate-mycothiol transferase | Reduction of arsenate is part of a defence mechanism of the cell against toxic arsenate. The product arseno-mycothiol is reduced by EC 1.20.4.3 (mycoredoxin) to arsenite and mycothiol-mycoredoxin disulfide. Finally, a second mycothiol recycles mycoredoxin and forms mycothione. Group: Enzymes. Synonyms: ArsC1; ArsC2; mycothiol:arsenate transferase. Enzyme Commission Number: EC 2.8.4.2. 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-3428; arsenate-mycothiol transferase; EC 2.8.4.2; ArsC1; ArsC2; mycothiol:arsenate transferase. Cat No: EXWM-3428. | |
| betaine reductase | The reaction is observed only in the direction of betaine reduction. The enzyme from Eubacterium acidaminophilum consists of subunits A, B and C. Subunit B contains selenocysteine and a pyruvoyl group, and is responsible for betaine binding and trimethylamine release. Subunit A, which also contains selenocysteine, is reduced by thioredoxin, and is needed to convert the carboxymethyl group into a ketene equivalent, in turn used by subunit C to produce acetyl phosphate. Only subunit B distinguishes this enzyme from EC 1.21.4.2 (glycine reductase) and EC 1.21.4.3 (sarcosine reductase). Group: Enzymes. Synonyms: acetyl-phosphate trimethylamine:thioredoxin disulfide oxidoreductase (N,N,N-trimethylglycine-forming). Enzyme Commission Number: EC 1.21.4.4. CAS No. 125752-87-6. 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-1259; betaine reductase; EC 1.21.4.4; 125752-87-6; acetyl-phosphate trimethylamine:thioredoxin disulfide oxidoreductase (N,N,N-trimethylglycine-forming). Cat No: EXWM-1259. | |
| bis-γ-glutamylcystine reductase | Contains FAD. The enzyme, which is found only in halobacteria, maintains the concentration of γ-glutamylcysteine, the major low molecular weight thiol in halobacteria. Not identical with EC 1.8.1.7 (glutathione-disulfide reductase) or EC 1.8.1.14 (CoA-disulfide reductase). Group: Enzymes. Synonyms: NADPH2:bis-γ-glutamylcysteine oxidoreductase; GSR. Enzyme Commission Number: EC 1.8.1.13. CAS No. 117056-54-9. 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-1639; bis-γ-glutamylcystine reductase; EC 1.8.1.13; 117056-54-9; NADPH2:bis-γ-glutamylcysteine oxidoreductase; GSR. Cat No: EXWM-1639. | |
| bontoxilysin | This zinc enzyme, produced by Clostridium botulinum, occurs as forms A-G that differ in specificity of action on the proteins of the neuroexocytosis apparatus. The 150-kDa proenzymes of bontoxilysin are processed to disulfide-linked subunits of 100 and 50 kDa, the latter being responsible for the endopeptidase activities. Weakly inhibited by captopril, and phosphoramidon. Toxicity is due to action at the neuromuscular junctions that blocks release of acetylcholine, causing flaccid paralysis, in contrast to the spastic paralysis caused by tentoxilysin. In peptidase family M27 (tentoxilysin family). Group: Enzymes. Synonyms: botulinum neurotoxin; BoNT. Enzyme Commission Number: EC 3.4.24.69. CAS No. 107231-12-9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4352; bontoxilysin; EC 3.4.24.69; 107231-12-9; botulinum neurotoxin; BoNT. Cat No: EXWM-4352. | |
| Captopril-cysteine Disulfide | Captopril-cysteine Disulfide is an impurity of Captopril, an orally active angiotensin-converting enzyme (ACE) inhibitor. Synonyms: Captopril-cysteine; 1-[(2S)-3-[[(2R)-2-Amino-2-carboxyethyl]dithio]-2-methyl-1-oxopropyl]-L-proline. CAS No. 75479-46-8. Molecular formula: C12H20N2O5S2. Mole weight: 336.43. |  |
| Captopril-N-acetylcysteine Disulfide | Captopril-N-acetylcysteine Disulfide is a metabolite of Captopril, which is an orally active angiotensin-converting enzyme (ACE) inhibitor used as an antihypertensive agent. Synonyms: 1-[(2S)-3-[[(2R)-2-(Acetylamino)-2-carboxyethyl]dithio]-2-methyl-1-oxopropyl]-L-proline; ((S)-3-(((R)-2-acetamido-2-carboxyethyl)disulfaneyl)-2-methylpropanoyl)-L-proline; 1-[(2S)-3-{[(2R)-2-Acetamido-2-carboxyethyl]disulfanyl}-2-methylpropanoyl]-L-proline; Captopril Related Compound 10. Grades: 95%. CAS No. 78636-31-4. Molecular formula: C14H22N2O6S2. Mole weight: 378.46. | |
| carbon disulfide lyase | The enzyme contains Zn2+. The hyperthermophilic archaeon Acidianus sp. A1-3 obtains energy by the conversion of carbon disulfide to hydrogen sulfide, with carbonyl sulfide as an intermediate. Group: Enzymes. Synonyms: CS2 hydrolase (misleading); carbon disulfide hydrolase (misleading); CS2-converting enzyme; carbon disulphide-lyase (decarboxylating). Enzyme Commission Number: EC 4.4.1.27. 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-5329; carbon disulfide lyase; EC 4.4.1.27; CS2 hydrolase (misleading); carbon disulfide hydrolase (misleading); CS2-converting enzyme; carbon disulphide-lyase (decarboxylating). Cat No: EXWM-5329. | |
| 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. | |
| cathepsin E | Found in stomach, spleen, erythrocyte membrane; not lysosomal. Pro-cathepsin E is an 86 kDa disulfide-linked dimer; activation or reduction produces monomer. In peptidase family A1 (pepsin A family). Group: Enzymes. Synonyms: slow-moving proteinase; erythrocyte membrane aspartic proteinase; SMP; erythrocyte membrane aspartic proteinase; EMAP; non-pepsin proteinase; cathepsin D-like acid proteinase; cathepsin E-like acid proteinase; cathepsin D-type proteinase. Enzyme Commission Number: EC 3.4.23.34. CAS No. 110910-42-4. 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-4271; cathepsin E; EC 3.4.23.34; 110910-42-4; slow-moving proteinase; erythrocyte membrane aspartic proteinase; SMP; erythrocyte membrane aspartic proteinase; EMAP; non-pepsin proteinase; cathepsin D-like acid proteinase; cathepsin E-like acid proteinase; cathepsin D-type proteinase. Cat No: EXWM-4271. | |
| CoA-disulfide reductase | A flavoprotein. Not identical with EC 1.8.1.6 (cystine reductase), EC 1.8.1.7 (glutathione-disulfide reductase) or EC 1.8.1.13 (bis-γ-glutamylcystine reductase). The enzyme from the bacterium Staphylococcus aureus has a strong preference for NADPH, while the bacterium Bacillus megaterium contains both NADH and NADPH-dependent enzymes. Group: Enzymes. Synonyms: CoA-disulfide reductase (NADH2); NADH2:CoA-disulfide oxidoreductase; CoA:NAD+ oxidoreductase (misleading); CoADR; coenzyme A disulfide reductase. Enzyme Commission Number: EC 1.8.1.14. CAS No. 206770-55-0. 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-1640; CoA-disulfide reductase; EC 1.8.1.14; 206770-55-0; CoA-disulfide reductase (NADH2); NADH2:CoA-disulfide oxidoreductase; CoA:NAD+ oxidoreductase (misleading); CoADR; coenzyme A disulfide reductase. Cat No: EXWM-1640. | |
| CoA-glutathione reductase | A flavoprotein. The substrate is a mixed disulfide. May be identical to EC 1.8.1.9, thioredoxin-disulfide reductase. Group: Enzymes. Synonyms: coenzyme A glutathione disulfide reductase; NADPH-dependent coenzyme A-SS-glutathione reductase; coenzyme A disulfide-glutathione reductase; NADPH2:CoA-glutathione oxidoreductase. Enzyme Commission Number: EC 1.8.1.10. CAS No. 37256-33-0. 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-1636; CoA-glutathione reductase; EC 1.8.1.10; 37256-33-0; coenzyme A glutathione disulfide reductase; NADPH-dependent coenzyme A-SS-glutathione reductase; coenzyme A disulfide-glutathione reductase; NADPH2:CoA-glutathione oxidoreductase. Cat No: EXWM-1636. | |
| coagulation factor Xa | A blood coagulation factor formed from the proenzyme factor X by limited proteolysis. Factor X is a glycoprotein composed of a heavy chain and a light chain, which are generated from a precursor protein by the excision of the tripeptide RKR and held together by one or more disulfide bonds. The activated factor Xa converts prothrombin to thrombin in the presence of factor Va, Ca2+ and phospholipids. Scutelarin (EC 3.4.21.60) has similar specificity, but does not require factor Va. Group: Enzymes. Synonyms: thrombokinase; prothrombase; prothrombinase; activated blood-coagulation factor X; autoprothrombin C; thromboplastin; plasma thromboplastin; factor Xa; activated Stuart-Prower factor; activated factor X. Enzyme Commission Number: EC 3.4.21.6. CAS No. 9002-5-5. Factor Xa. 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-4150; coagulation factor Xa; EC 3.4.21.6; 9002-05-5; thrombokinase; prothrombase; prothrombinase; activated blood-coagulation factor X; autoprothrombin C; thromboplastin; plasma thromboplastin; factor Xa; activated Stuart-Prower factor; activated factor X. Cat No: EXWM-4150. | |
| Cystamine dihydrochloride | Cystamine dihydrochloride is the dihydrochloride salt of cystamine, which is an organic disulfide that inhibits tissue transglutaminase (TGM2) with an IC50 value of approximately 2.5 mM. It is orally available, and decreases aggregated and cross-linked huntingtin in transfected cells. It is neuroprotective in mouse models of Huntington's disease. It has exhibited suppressive effects against HIV replication in infected human cells. It could extend survival and improve motor performance in transgenic HD mice. It inhibits caspase 3, increases intracellular glutathione, and reduces inflammation in a rat model of inflammatory bowel disease. Uses: Enzyme inhibitors. Synonyms: 2-(2-aminoethyldisulfanyl)ethanamine; dihydrochloride. Grades: > 97 %. CAS No. 56-17-7. Molecular formula: C4H14Cl2N2S2. Mole weight: 225.20. | |
| Dipropyl disulfide | Dipropyl disulfide is oxidized to dipropyl thiosulfinate (DPDSO) by rat microsomes. Both flavincontaining monooxygenases (FMO) and cytochrome P450 enzymes (CYPs) are involved in dipropyl disulfide oxidation. Dipropyl disulfide forms two metabolites: propylglutathione sulfide conjugate and propylthiol [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: Propyl Disulfide; DPDS. CAS No. 629-19-6. Pack Sizes: 10 mM * 1 mL; 1 g. Product ID: HY-W196803. |  |
| dissimilatory sulfite reductase | Contain siroheme. The enzyme is essential in prokaryotic sulfur-based energy metabolism, including sulfate/sulfite reducing organisms, sulfur-oxidizing bacteria, and organosulfonate reducers. In sulfur reducers it catalyses the reduction of sulfite to sulfide (reaction 1 in the right to left direction), while in sulfur oxidizers it catalyses the opposite reaction (reaction 2 in the left to right direction). The reaction involves the small protein DsrC, which is present in all the organisms that contain dissimilatory sulfite reductase. During the process an intramolecular disulfide bond is formed between two L-cysteine residues of DsrC. This disulfide can be reduced by a number of proteins including DsrK and TcmB. This enzyme is different from EC 1.8.1.2, assimilatory sulfite reductase (NADPH), and EC 1.8.7.1, assimilatory sulfite reductase (ferredoxin), which are involved in sulfate assimilation. Group: Enzymes. Synonyms: siroheme sulfite reductase; hydrogen-sulfide:(acceptor) oxidoredu. Enzyme Commission Number: EC 1.8.99.5. CAS No. 37256-51-2. 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-1686; dissimilatory sulfite reductase; EC 1.8.99.5; 37256-51-2; siroheme sulfite reductase; hydrogen-sulfide:(acceptor) oxidoreductase (ambiguous); DsrAB. Cat No: EXWM-1686. | |
| 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. | |
| Disulfide Oxidoreductase, Recombinant | DsbA appears to be necessary for correct formulation of disulfide bonds in exported proteins in vivo. DsbA is useful as a standard in immunoblotting. This protein catalyses the reduction and exchange of disulfide bonds and the oxidation of free sulfhydryl groups in vitro. It is the strongest oxidant of the thioredoxin superfamily. This thio/disulfide oxidoreductase is required for efficient disulfide bond formation in the periplasm of E. coli. Disulfide oxidoreductase produced in e. coli is a periplasmic protein isolated from e. coli, containing 208 amino acids having a molecular mass of 23,149 dalton. the dsba is purified by proprietary chromatographic techniques. Applications: Western blot. Group: Enzymes. Syno. Purity: Greater than 95.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. DsbA. Mole weight: 23,149 Da. Stability: Lyophilized DsbA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution DsbA should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles. Appearance: Sterile Filtered White lyophilized (freeze-dried) powder. Source: E. coli. DsbA; Thiol:disulfide interchange protein dsbA; Disulfide Oxidoreductase. Cat No: NATE-0828. | |
| DX600 | DX600 is an inhibitor of angiotensin-converting enzyme 2 (ACE2). Synonyms: DX-600; Ac-Gly-Asp-Tyr-Ser-His-Cys-Ser-Pro-Leu-Arg-Tyr-Tyr-Pro-Trp-Trp-Lys-Cys-Thr-Tyr-Pro-Asp-Pro-Glu-Gly-Gly-Gly-NH2 (Disulfide bridge: Cys6-Cys17); N-{ [ (6S, 9R, 14R, 17S, 20S, 23S, 25aS, 31S, 34S, 37S, 40S, 42aS) -9- [ (N-Acetylglycyl-L-α -aspartyl-L-tyrosyl-L-seryl-L-histidyl) amino] -17- (4-aminobutyl) -37- (3-carbamimidamidopropyl) -31, 34-bis (4-hydroxybenzyl) -6- (hydroxymethyl) -20, 23-bis (1H-indol-3-ylmethyl) -40-isobutyl-5, 8, 16, 19, 22, 25, 30, 33, 36, 39, 42-undecaoxooctatriacontahydro-1H, 13H-dipyrrolo [2, 1-p: 2', 1'-e1] [1, 2, 5, 8, 11, 14, 17, 20, 23, 26, 29, 32, 35] dithiaundecaazacyclooctatriacontin-14-yl] carbonyl}-L-threonyl-L-tyrosyl-L-prolyl-L-α -aspartyl-L-prolyl-L-α -glutamylglycylglycylglycinamide; N-acetyl-glycyl-L-alpha-aspartyl-L-tyrosyl-L-seryl-L-histidyl-L-cysteinyl-L-seryl-L-prolyl-L-leucyl-L-arginyl-L-tyrosyl-L-tyrosyl-L-prolyl-L-tryptophyl-L-tryptophyl-L-lysyl-L-cysteinyl-L-threonyl-L-tyrosyl-L-prolyl-L-alpha-aspartyl-L-prolyl-L-alpha-glutamyl-glycyl-glycyl-glycinamide (6->17)-disulfide. Grades: ≥95%. CAS No. 478188-26-0. Molecular formula: C141H185N35O40S2. Mole weight: 3074.32. | |
| DX600 TFA | DX600 TFA is an inhibitor of angiotensin-converting enzyme 2 (ACE2) and does not cross-react with ACE. Synonyms: Glycinamide, N-acetylglycyl-L-α-aspartyl-L-tyrosyl-L-seryl-L-histidyl-L-cysteinyl-L-seryl-L-prolyl-L-leucyl-L-arginyl-L-tyrosyl-L-tyrosyl-L-prolyl-L-tryptophyl-L-tryptophyl-L-lysyl-L-cysteinyl-L-threonyl-L-tyrosyl-L-prolyl-L-α-aspartyl-L-prolyl-L-α-glutamylglycylglycyl-, cyclic (6?17)-disulfide, trifluoroacetate salt (1:1); Ac-Gly-Asp-Tyr-Ser-His-Cys-Ser-Pro-Leu-Arg-Tyr-Tyr-Pro-Trp-Trp-Lys-Cys-Thr-Tyr-Pro-Asp-Pro-Glu-Gly-Gly-Gly-NH2.TFA (Disulfide bridge: Cys6-Cys17); N-acetyl-glycyl-L-alpha-aspartyl-L-tyrosyl-L-seryl-L-histidyl-L-cysteinyl-L-seryl-L-prolyl-L-leucyl-L-arginyl-L-tyrosyl-L-tyrosyl-L-prolyl-L-tryptophyl-L-tryptophyl-L-lysyl-L-cysteinyl-L-threonyl-L-tyrosyl-L-prolyl-L-alpha-aspartyl-L-prolyl-L-alpha-glutamyl-glycyl-glycyl-glycinamide (6->17)-disulfide trifluoroacetic acid. Grades: ≥95%. Molecular formula: C123H169F3N32O39S2. Mole weight: 2841.01. | |
| (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase (ferredoxin) | An iron-sulfur protein found in plant chloroplasts and cyanobacteria that contains a [4Fe-4S] cluster. Forms part of an alternative non-mevalonate pathway for isoprenoid biosynthesis. Bacteria have a similar enzyme that uses flavodoxin rather than ferredoxin (cf. EC 1.17.7.3). The enzyme from the plant Arabidopsis thaliana is active with photoreduced 5-deazaflavin but not with flavodoxin. Group: Enzymes. Synonyms: 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (ambiguous); (E)-4-hydroxy-3-methylbut-2-en-1-yl-diphosphate:protein-disulfide oxidoreductase (hydrating) (incorrect); (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase (ambiguous); gcpE (gene name); ISPG (gene name); (E)-4-hydroxy-3-methylbut-2-eny. Enzyme Commission Number: EC 1.17.7.1. 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-1096; (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase (ferredoxin); EC 1.17.7.1; 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (ambiguous); (E)-4-hydroxy-3-methylbut-2-en-1-yl-diphosphate:protein-disulfide oxidoreductase (hydrating) (incorrect); (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase (ambiguous); gcpE (gene name); ISPG (gene name); (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase. Cat No: EXWM-1096. | |
| (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase (flavodoxin) | A bacterial iron-sulfur protein that contains a [4Fe-4S] cluster. Forms part of an alternative non-mevalonate pathway for isoprenoid biosynthesis that is found in most bacteria. Plants and cyanobacteria have a similar enzyme that utilizes ferredoxin rather than flavodoxin (cf. EC 1.17.7.1). Group: Enzymes. Synonyms: 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (ambiguous); (E)-4-hydroxy-3-methylbut-2-en-1-yl-diphosphate:protein-disulfide oxidoreductase (hydrating) (incorrect); (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase (ambiguous); ispG (gene name). Enzyme Commission Number: EC 1.17.7.3. 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-1098; (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase (flavodoxin); EC 1.17.7.3; 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (ambiguous); (E)-4-hydroxy-3-methylbut-2-en-1-yl-diphosphate:protein-disulfide oxidoreductase (hydrating) (incorrect); (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase (ambiguous); ispG (gene name). Cat No: EXWM-1098. | |
| ferredoxin:thioredoxin reductase | The enzyme contains a [4Fe-4S] cluster and internal disulfide. It forms a mixed disulfide with thioredoxin on one side, and docks ferredoxin on the other side, enabling two one-electron transfers. The reduced thioredoxins generated by the enzyme activate the Calvin cycle enzymes EC 3.1.3.11 (fructose-bisphosphatase), EC 3.1.3.37(sedoheptulose-bisphosphatase) and EC 2.7.1.19 (phosphoribulokinase) as well as other chloroplast enzymes by disulfide reduction. Group: Enzymes. Enzyme Commission Number: EC 1.8.7.2. 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-1681; ferredoxin:thioredoxin reductase; EC 1.8.7.2. Cat No: EXWM-1681. | |
| Free Methionine-(R)-Sulfoxide Reductase from E. coli, recombinant | The Free Methionine-(R)-Sulfoxide Reductase (fRMsr) reduces free methionine sulfoxide (Met(O)) to methionine using thiol-disulfide exchange chemistry. This enzyme is involved in oxidative defense and known to form a sulfenic acid intermediate at the active site Cys during the course of turnover. In this variant, all Cys other than the peroxide-sensitive Cys have been removed by mutagenesis in order to stabilize the active site sulfenic acid with respect to disulfide bond formation. Applications: Free methionine-(r)-sulfoxide reductase (c84s, c94s), or frmsr, can be selectively derivatized at a single cys residue with a variety of cys-soh specific probes and be used as a positive control. Group: Enzymes. Enzyme Commission Number: EC 1.8.4.14. Purity: >98% by SDS-PAGE. Mole weight: 18,752 Da. Storage: at -80 °C. Form: Liquid. Source: E. coli. Free Methionine-(R)-Sulfoxide Reductase; fRMsr; EC 1.8.4.14. Cat No: NATE-1693. | |
| glutathione amide-dependent peroxidase | This enzyme, which has been characterized from the proteobacterium Marichromatium gracile, is a chimeric protein, containing a peroxiredoxin-like N-terminus and a glutaredoxin-like C terminus. The enzyme has peroxidase activity towards hydrogen peroxide and several small alkyl hydroperoxides, and is thought to represent an early adaptation for fighting oxidative stress. The glutathione amide disulfide produced by this enzyme can be restored to glutathione amide by EC 1.8.1.16 (glutathione amide reductase). Group: Enzymes. Enzyme Commission Number: EC 1.11.1.17. 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-0498; glutathione amide-dependent peroxidase; EC 1.11.1.17. Cat No: EXWM-0498. | |
| glutathione amide reductase | A dimeric flavoprotein (FAD). The enzyme restores glutathione amide disulfide, which is produced during the reduction of peroxide by EC 1.11.1.17 (glutathione amide-dependent peroxidase), back to glutathione amide (it catalyses the reaction in the opposite direction to that shown). The enzyme belongs to the family of flavoprotein disulfide oxidoreductases, but unlike other members of the family, which are specific for NADPH, it prefers NADH. Group: Enzymes. Synonyms: GAR. Enzyme Commission Number: EC 1.8.1.16. 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-1642; glutathione amide reductase; EC 1.8.1.16; GAR. Cat No: EXWM-1642. | |
| glutathione-CoA-glutathione transhydrogenase | This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a disulfide as acceptor. This enzyme participates in cysteine metabolism and glutathione metabolism. Group: Enzymes. Synonyms: glutathione-coenzyme A glutathione disulfide transhydrogenase; glutathione-coenzyme A glutathione disulfide transhydrogenase; glutathione coenzyme A-glutathione transhydrogenase; glutathione:coenzyme A-glutathione transhydrogenase; coenzyme A:oxidized-glutathione oxidoreductase; coenzyme A:glutathione-disulfide oxidoreductase. Enzyme Commission Number: EC 1.8.4.3. CAS No. 37256-48-7. 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-1671; glutathione-CoA-glutathione transhydrogenase; EC 1.8.4.3; 37256-48-7; glutathione-coenzyme A glutathione disulfide transhydrogenase; glutathione-coenzyme A glutathione disulfide transhydrogenase; glutathione coenzyme A-glutathione transhydrogenase; glutathione:coenzyme A-glutathione transhydrogenase; coenzyme A:oxidized-glutathione oxidoreductase; coenzyme A:glutathione-disulfide oxidoreductase. Cat No: EXWM-1671. | |
| glutathione-cystine transhydrogenase | This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a disulfide as acceptor. The systematic name of this enzyme class is glutathione:cystine oxidoreductase. Other names in common use include GSH-cystine transhydrogenase, and NADPH-dependent GSH-cystine transhydrogenase. This enzyme participates in cysteine metabolism and glutathione metabolism. Group: Enzymes. Synonyms: GSH-cystine transhydrogenase; NADPH-dependent GSH-cystine transhydrogenase. Enzyme Commission Number: EC 1.8.4.4. CAS No. 37256-49-8. 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-1672; glutathione-cystine transhydrogenase; EC 1.8.4.4; 37256-49-8; GSH-cystine transhydrogenase; NADPH-dependent GSH-cystine transhydrogenase. Cat No: EXWM-1672. | |
| glutathione-disulfide reductase | A dimeric flavoprotein (FAD); activity is dependent on a redox-active disulfide in each of the active centres. Group: Enzymes. Synonyms: glutathione reductase; glutathione reductase (NADPH); NADPH-glutathione reductase; GSH reductase; GSSG reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase. Enzyme Commission Number: EC 1.8.1.7. CAS No. 9001-48-3. GR. 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-1651; glutathione-disulfide reductase; EC 1.8.1.7; 9001-48-3; glutathione reductase; glutathione reductase (NADPH); NADPH-glutathione reductase; GSH reductase; GSSG reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase. Cat No: EXWM-1651. | |
| Glutathione Reductase from Human, Recombinant | Glutathione reductase enzyme is a homodimeric enzyme containing 1 FAD molecule and 1 NADPH binding domain per subunit., Both human GR (hGR) and Plasmodium falciparum GR (PfGR) are essential for the survival of the malaria parasite within the human erythrocyte. Thus, this enzyme may be used for studies of candidate anti-malaria reagents. Group: Enzymes. Synonyms: glutathione-disulfide reductase; glutathione reductase; glutathione reductase (NADPH); NADPH-glutathione reductase; GSH reductase; GSSG reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase; EC 1.8.1.7; 9001-48-3; GR. Enzyme Commission Number: EC 1.8.1.7. CAS No. 9001-48-3. GR. Activity: > 10 units/mg protein. Storage: -20°C. Form: buffered aqueous solution; Solution containing 25 mM Tris-HCl, pH 7.4, 1 mM EDTA, and 50% (v/v) glycerol. Source: E. coli. Species: Human. glutathione-disulfide reductase; glutathione reductase; glutathione reductase (NADPH); NADPH-glutathione reductase; GSH reductase; GSSG reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase; EC 1.8.1.7; 9001-48-3; GR. Cat No: NATE-0320. | |
| glutathione transferase | A group of enzymes of broad specificity. R may be an aliphatic, aromatic or heterocyclic group; X may be a sulfate, nitrile or halide group. Also catalyses the addition of aliphatic epoxides and arene oxides to glutathione, the reduction of polyol nitrate by glutathione to polyol and nitrile, certain isomerization reactions and disulfide interchange. Group: Enzymes. Synonyms: glutathione S-transferase; glutathione S-alkyltransferase; glutathione S-aryltransferase; S-(hydroxyalkyl)glutathione lyase; glutathione S-aralkyltransferase; glutathione S-alkyl transferase; GST. Enzyme Commission Number: EC 2.5.1.18. CAS No. 50812-37-8. Glutathione S-Transferase. 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-2754; glutathione transferase; EC 2.5.1.18; 50812-37-8; glutathione S-transferase; glutathione S-alkyltransferase; glutathione S-aryltransferase; S-(hydroxyalkyl)glutathione lyase; glutathione S-aralkyltransferase; glutathione S-alkyl transferase; GST. Cat No: EXWM-2754. | |
| Immobilized Pepsin (Agarose Resin) | Immobilized Pepsin allows efficient generation of F(ab?)2 from IgG. Pepsin is a nonspecific endopeptidase that is active only at acid pH and irreversibly denatured at neutral or alkaline pH. Immobilized Pepsin is advantageous because the digestion can be immediately stopped by simply removing the gel from the IgG. Digestion by pepsin normally produces a F(ab?)2 fragment and numerous small peptides of the Fc portion. The resulting F(ab?)2 fragment is composed of two disulfide-connected Fab units. The Fc fragment is extensively degraded, and its small fragments can be separated from F(ab?)2 by dialysis, gel filtration or ion exchange chromatography. Group: Enzymes. Synonyms: Immobilized Pepsin. Enzyme Commission Number: EC 3.4.23.1. Pepsin. Storage: Upon receipt store product at 4-8°C. Product is shipped at ambient temperature. Form: 50% slurry containing 50% glycerol in 0.1M sodium acetate; pH 4.5, and 0.05% sodium azide as a preservative. Immobilized Pepsin (Agarose Resin); Protein Fragmentation Enzymes Kits; Fab fragment; Immobilized Pepsin; Pepsin. Pack: 5mL settled gel, contains sufficient material to generate F(ab?)2 fragments from up to 20 samples containing up to 10mg of IgG. Cat No: NATE-1866. | |
| JX-06 | JX-06 is a potent and selective pyruvate dehydrogenase kinase (PDK) 1/2/3 inhibitor (IC50 values are 28, 49 and 313 nM for PDK2, PDK1 and PDK3, respectively). JX06 Selectively Inhibits Pyruvate Dehydrogenase Kinase PDK1 by a Covalent Cysteine Modification. JX06, as a selective covalent inhibitor of PDK1 in cells, forms a disulfide bond with the thiol group of a conserved cysteine residue (C240) based on recognition of a hydrophobic pocket adjacent to the ATP pocket of the PDK1 enzyme. Uses: Designed for use in research and industrial production. Additional or Alternative Names: JX-06; JX 06; JX06. Product Category: Inhibitors. Appearance: Solid powder. CAS No. 729-46-4. Molecular formula: C10H16N2O2S4. Mole weight: 324.49. Purity: >98%. IUPACName: Bis(morpholinothiocarbonyl) disulfide. Canonical SMILES: S=C(SSC(N1CCOCC1)=S)N2CCOCC2. Product ID: ACM729464. Alfa Chemistry ISO 9001:2015 Certified. Categories: JP-06. |  |
| Lanreotide | Laromustine is a sulfonyl hydrazine prodrug with antineoplastic activity. Laromustine releases the DNA chloroethylating agent 90CE after entering the blood stream; 90CE chloroethylates alkylates the 06 position of guanine, resulting in DNA crosslinking, strand breaks, chromosomal aberrations, and disruption of DNA synthesis. Intracellular metabolism of this agent also releases methyl isocyanate which inhibits 06-alkyl-guanine transferase, an enzyme involved with DNA repair. Synonyms: Angiopeptin; Autogel; BIM 23014; DC 13-116; Dermopeptin; Ipstyl; L-Autogel; Lanreotide Autogel; Somatulin; Somatulin-Autogel; Somatuline Depot; L-Threoninamide, 3-(2-naphthalenyl)-D-alanyl-L-cysteinyl-L-tyrosyl-D-tryptophyl-L-lysyl-L-valyl-L-cysteinyl-, cyclic (2?7)-disulfide; H-D-2Nal-Cys(1)-Tyr-D-Trp-Lys-Val-Cys(1)-Thr-NH2; 3-(2-naphthyl)-D-alanyl-L-cysteinyl-L-tyrosyl-D-tryptophyl-L-lysyl-L-valyl-L-cysteinyl-L-threoninamide (2->7)-disulfide. Grades: 98%. CAS No. 108736-35-2. Molecular formula: C54H69N11O10S2. Mole weight: 1096.33. | |
| L-Dithiothreitol | L-Dithiothreitol (DTT) is a reducing agent commonly used in various biochemical applications to break disulfide bonds in proteins, thereby denaturing proteins or preventing the formation of unwanted aggregates. DTT has a unique chemical property that cleaves the sulfur-sulfur bond in the disulfide bond to form a sulfhydryl group. This makes it a useful tool for protein purification, enzyme assays, and protein structure studies. Uses: Scientific research. Group: Biochemical assay reagents. CAS No. 16096-97-2. Pack Sizes: 10 mg; 25 mg; 50 mg; 100 mg. Product ID: HY-15917A. | |
| methanol dehydrogenase (cytochrome c) | A periplasmic quinoprotein alcohol dehydrogenase that only occurs in methylotrophic bacteria. It uses the novel specific cytochrome cL as acceptor. Acts on a wide range of primary alcohols, including ethanol, duodecanol, chloroethanol, cinnamyl alcohol, and also formaldehyde. Activity is stimulated by ammonia or methylamine. It is usually assayed with phenazine methosulfate. 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. It differs from EC 1.1.2.8, alcohol dehydrogenase (cytochrome c), in having a high affinity for methanol and in having a second essential small subunit (no known function). Group: Enzymes. Synonyms: methanol dehydrogenase; MDH. Enzyme Commission Number: EC 1.1.2.7. CAS No. 37205-43-9. 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-0389; methanol dehydrogenase (cytochrome c); EC 1.1.2.7; 37205-43-9; methanol dehydrogenase; MDH. Cat No: EXWM-0389. | |
| mycothione reductase | Contains FAD. No activity with glutathione, trypanothione or coenzyme A as substrate. Group: Enzymes. Synonyms: mycothiol-disulfide reductase. Enzyme Commission Number: EC 1.8.1.15. CAS No. 252212-92-3. 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-1641; mycothione reductase; EC 1.8.1.15; 252212-92-3; mycothiol-disulfide reductase. Cat No: EXWM-1641. | |
| Native Bacillus licheniformis Protease | Protease catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate. Protease is a serine endoproteinase with a broad specificity towards native and denatured proteins, and is active under alkaline conditions. It is active in some organic solvents such as dry octane. The enzyme is found to be stable at ph 8-10, retaining activity of up to 90% for 24 hours. it shows maximum activity at temperatures between 55-60°c. Applications: The product has been used with other enzymes for in situ proteolysis to produce crystals suitable for structure determi...f bacillus licheniformis. it is a serine endoproteinase with a broad specificity towards native and denatured proteins, and is active under alkaline conditions. Group: Enzymes. Synonyms: Protease; 9014-01-1; Subtilisin A; EC 3.4.21.62; Alcalase. Enzyme Commission Number: EC 3.4.21.62. CAS No. 9001-92-7. Protease. Mole weight: Subtilisin is a non-glycosylated single polypeptide chain without disulfide bonds and has a molecular weight of 27 KDa. Activity: Type VIII, 7-15 units/mg solid; Type I, > 2.4 U/g. Form: Type VIII, lyophilized powder; Type I, aqueous solution. Source: Bacillus licheniformis. Protease; 9014-01-1; Subtilisin A; EC 3.4.21.62; Alcalase. Cat No: NATE-0633. | |
| Native Bacillus licheniformis Proteinase | Proteinase catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate. Subtilisin is a non-glycosylated single polypeptide chain without disulfide bonds and has a molecular weight of 27 kda. Applications: The enzyme from creative enzymes has been used to optimize release of all mit ochondrial populations from homogenized ventricular tissue of rat heart. it has also been used in the pre-hybridisation treatment of formalin fixed, paraffin wax-embedded liver specimens for detecting human and viral dna. this is a proteolytic enzyme isolated from th...ls to study the silencing of cardiac mit ochondrial nhe1. Group: Enzymes. Synonyms: protease; peptidase; proteinase; EC 3.4.21.62; 9014-01-1; Alkaline Protease; Protease from Bacillus licheniformis; Proteinase from Bacillus licheniformis; Subtilo peptidase A. Enzyme Commission Number: EC 3.4.21.62. CAS No. 9001-92-7. Purity: crystallization. Proteinase. Mole weight: 27 KDa. Activity: 7.0-14.0 units/mg solid. Storage: -20°C. Form: lyophilized powder. Source: Bacillus licheniformis. protease; peptidase; proteinase; EC 3.4.21.62; 9014-01-1; Alkaline Protease; Protease from Bacillus licheniformis; Proteinase from Bacillus licheniformis; Subtilo peptidase A. Cat No: NATE-0639. | |
| Native Bovine Protein Disulfide Isomerase | Protein Disulfide Isomerase (PDI) has the C-terminal ER retention sequence Lys-Asp-Glu-Leu. It has active, intracellular traffic to different cell compartments. PDI supports internalization of Chlamydia, cholera and diphtheria toxins in some hosts. PDI is required for Sindbis virus infection and aids in reducing HIV gp120 protein thiols. PDI facilitates formation of the correct disulfide bonds by promoting rapid reshuffling of disulfide pairings. Protein disulfide isomerase (pdi) from bovine liver is a homodimer with a molecular weight of 107 kda (gel filtration) and the molecular weight of the monomer has been reported at 57 kda (sds-page). the enzyme is a glycoprotein ... is mainly l ocated in the er, where it assists in protein-folding and thiol-disulfide exchanges. it is used to study functional role of pdi in parasite infection and the interaction between macrophage pdi and l. chagasi. Group: Enzymes. Synonyms: Protein disulfide isomerase; PDI; EC 5.3.4.1; 37318-49-3; S-S rearrangase. Enzyme Commission Number: EC 5.3.4.1. CAS No. 37318-49-3. Purity: >95% (SDS-PAGE). PDI. Activity: 100-400 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing potassium phosphate buffer salts and stabilizer. Source: Bovine liver. Species: Bovine. Protein disulfide isomerase; PDI; EC 5.3.4.1; 37318-49-3; S-S rearrangase. Cat No: NATE-0533. | |
| Native Escherichia coli Thioredoxin Reductase | Thioredoxin reductase (TrxR) is an NADPH-dependent oxidoreductase containing one FAD per subunit that reduces the active site disulfide in oxidised thioredoxin (Trx). The molecular weight of the isozymes from mammalian sources vary between 55-67 kDa as compared with 35 kDa in prokaryotes, plants or yeast. The substrate specificity of the mammalian enzyme is much broader than the prokaryotic enzyme reducing both mammalian and E. coli thioredoxins as well as well as non-disulfide substrates such selenite, lipoic acids, lipid hydroperoxides and hydrogen peroxide. Applications: Thioredoxin reductase from escherichia coli can be used in peroxidase-coupled thioredoxin system assay for assessing the peroxidase activitiy of cys-based thiol peroxidases. the product was used for determining the enzymatic activity of his6-ahp1p. Group: Enzymes. Synonyms: NADP-thioredoxi. Enzyme Commission Number: EC 1.8.1.9. CAS No. 9074-14-0. TrxR. Activity: >25 units/mg protein (Bradford). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 3.6 M (NH4)2SO4 containing 30 mM potassium phosphate buffer, pH 7.5, and 2 mM EDTA. Source: Escherichia coli. NADP-thioredoxin reductase; NADPH-thioredoxin reductase; thioredoxin reductase (NADPH); NADPH2:oxidized thioredoxin oxidoreductase; thioredoxin-disulfide reductase; EC 1.8.1.9; TrxR. Cat No: NATE-0718. | |
| Native Human Cathepsin H | Cathepsin H is a protein that in humans is encoded by the CTSH gene. The protein encoded by this gene is a lysosomal cysteine proteinase important in the overall degradation of lysosomal proteins. It is composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. The encoded protein, which belongs to the peptidase C1 protein family, can act both as an aminopeptidase and as an endopeptidase. Increased expression of this gene has been correlated with malignant progression of prostate tumors. Two transcript variants encoding different isoforms have been found for this gene. Group: Enzymes. Synonyms: CTSH; cathepsin H; CPSB; ACC-4; ACC-5; ACC4; ACC5; CPSB; minichain. Purity: > 95% (SDS-PAGE). CTSH. Mole weight: 28 kDa. Storage: -40°C. Form: Liquid. Source: Human Liver. Species: Human. CTSH; cathepsin H; CPSB; ACC-4; ACC-5; ACC4; ACC5; CPSB; minichain. Cat No: NATE-0176. | |
| Native Human Elastase | Neutrophil elastase is a serine proteinase in the same family as chymotrypsin and has broad substrate specificity. Secreted by neutrophils and macrophages during inflammation, it destroys bacteria and host tissue. It also localizes to Neutrophil extracellular traps (NETs), via its high affinity for DNA, an unusual property for serine proteases. Leuk ocyte elastase is a 29 kda serine endoprotease of the proteinase s1 family. it exists as a single 238 amino acid-peptide chain with four disulfide bonds. it contains two or thee n-linked glycans of variable composition which account for its three major isoforms. Applications: Elastase from creative enzymes has been used to digest fibro...mal models. Group: Enzymes. Synonyms: ELANE; elastase; EC 3.4.21.37; leukocyte elastase; ELA2; elastase 2; neutrophil elaszym; serine elastase; lysosomal elastase; neutrophil elastase; polymorphonuclear leukocyte elastase; elaszym; granulocyte elastase. Enzyme Commission Number: EC 3.4.21.37. CAS No. 9004-6-2. ELA2. Mole weight: 29 kDa. Activity: > 50 units/mg protein (Bradford). Storage: -20°C. Form: Lyophilized from 0.05 M sodium acetate (pH 5.5) and 0.6 M NaCl. Source: Human leuk ocytes. Species: Human. ELANE; elastase; EC 3.4.21.37; leukocyte elastase; ELA2; elastase 2; neutrophil elaszym; serine elastase; lysosomal elastase; neutrophil elastase; polymorphonuclear leukocyte ela | |
| Native Lysobacter enzymogenes Endoproteinase Lys-C | Endoproteinase Lys-C inactivates the enzyme inositol monophosphatase by cleaving it at a single site directly after Lys 36. Endoproteinase lys-c is an enzyme that preferentially cleaves at the carboxyl side of lysine residues. Applications: Endoproteinase lys-c from lysobacter enzymogenes is useful in the determination of primary structures of proteins. it has been used in a study to investigate the evidence for trisulfide bonds in a recombinant variant of a human igg2 mon oclonal antibody. endoproteinase lys-c has been used for the digestion mon oclonal antibodies for disulfide bond assignment. Group: Enzymes. Synonyms: EC 3.4.21.50; chromobacter proteinase I; Achromobacter lyticus alkaline proteinase I; protease I; achromopeptidase; lysyl bond specific proteinase; 72561-05-8; Achromobacter proteinase I; Endoproteinase Lys-C. Enzyme Commission Number: EC 3.4.21.50. CAS No. 72561-05-8. Achromopeptidase. Storage: 2-8°C. Form: lyophilized powder. Source: Lysobacter enzymogenes. EC 3.4.21.50; chromobacter proteinase I; Achromobacter lyticus alkaline proteinase I; protease I; achromopeptidase; lysyl bond specific proteinase; 72561-05-8; Achromobacter proteinase I; Endoproteinase Lys-C. Cat No: NATE-0220. | |
| 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. | |
| Native Rat Thioredoxin Reductase | Thioredoxin reductase (TrxR) is an NADPH-dependent oxidoreductase containing one FAD per subunit that reduces the active site disulfide in oxidised thioredoxin (Trx). The molecular weight of the isozymes from mammalian sources vary between 55-67 kDa as compared with 35 kDa in prokaryotes, plants or yeast. The substrate specificity of the mammalian enzyme is much broader than the prokaryotic enzyme reducing both mammalian and E. coli thioredoxins as well as well as non-disulfide substrates such selenite, lipoic acids, lipid hydroperoxides and hydrogen peroxide. Applications: Thioredoxin reductase from rat liver can be used for studying the uptake and reduction of a-lipoic acid... NADP-thioredoxin reductase; NADPH-thioredoxin reductase; thioredoxin reductase (NADPH); NADPH2:oxidized thioredoxin oxidoreductase; thioredoxin-disulfide reductase; EC 1.8.1.9; TrxR; 9074-14-0. Enzyme Commission Number: EC 1.8.1.9. CAS No. 9074-14-0. TrxR. Activity: > 100 units/mg protein (Bradford). Storage: -20°C. Form: buffered aqueous glycerol solution; Solution in 50 mM Tris-HCl, pH 7.5, 300 mM NaCl, 1 mM EDTA, and 10% glycerol. Source: Rat liver. Species: Rat. NADP-thioredoxin reductase; NADPH-thioredoxin reductase; thioredoxin reductase (NADPH); NADPH2:oxidized thioredoxin oxidoreductase; thioredoxin-disulfide reductase; EC 1.8.1.9; TrxR; 9074-14-0. Cat No: NATE-0713. | |
| OBP-801 | OBP-801, also known YM753 and spiruchostatin A, is a novel cyclic-peptide-based HDAC inhibitor. YM753 is a bacteria-derived natural product containing a disulfide bond. It potently inhibited HDAC enzyme with an IC50 of 2.0 nM in the presence of dithiothreitol. YM753 was rapidly converted to a reduced form in tumor cells, and then induced accumulation of acetylated histones, followed by p21WAF1/Cip1 expression, tumor cell growth inhibition and tumor-selective cell death. In an in vitro washout study, YM753 showed prolonged accumulation of acetylated histones in WiDr human colon carcinoma cells. In vivo YM753 dosing of mice harboring WiDr colon tumor xenografts significantly inhibited the tumor growth via sustained accumulation of acetylated histones in the tumor tissue. In a pharmacokinetic study, YM753 rapidly disappeared from the plasma, but its reduced form remained in the tumor tissue. Moreover, the accumulation of acetylated histones induced by YM753 was tumor tissue selective compared to several normal tissues. YM753 has attractive pharmacodynamic and pharmacokinetic properties giving it potential as an antitumor agent. Synonyms: OBP 801; OBP801; spiruchostatin A; YM-753; YM 753; (1S,5S,6R,9S,20R,E)-5-hydroxy-6-isopropyl-20-methyl-2-oxa-11,12-dithia-7,19,22-triazabicyclo[7.7.6]docos-15-ene-3,8,18,21-tetraone. Grades: >98%. CAS No. 328548-11-4. Molecular formula: C20H31N3O6S2. Mole weight: 473.60. | |
| pappalysin-1 | A 400-kDa disulfide-linked dimer. Circulates in human pregnancy mainly as a complex with the proform of eosinophil major basic protein, which acts as an inhibitor of the peptidase. The rate of hydrolysis of IGFBP-4 is increased about 20-fold by the presence of insulin-like growth factor (IGF), whereas that of IGFBP-5 is decreased about two-fold. In peptidase family M43. Group: Enzymes. Synonyms: insulin-like growth factor binding protein-4 protease; pregnancy-associated plasma protein-A. Enzyme Commission Number: EC 3.4.24.79. 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-4363; pappalysin-1; EC 3.4.24.79; insulin-like growth factor binding protein-4 protease; pregnancy-associated plasma protein-A. Cat No: EXWM-4363. | |
| peptidase K | From the mold Tritirachium album Limber. A peptidase of family S8 (subtilisin family) containing two disulfide bridges and one free Cys near the active site His. Formerly included in EC 3.4.21.14. Group: Enzymes. Synonyms: Tritirachium alkaline proteinase; Tritirachium album serine proteinase; proteinase K; Tritirachium album proteinase K; endopeptidase K. Enzyme Commission Number: EC 3.4.21.64. CAS No. 39450-01-6. Proteinase K. 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-4155; peptidase K; EC 3.4.21.64; 39450-01-6; Tritirachium alkaline proteinase; Tritirachium album serine proteinase; proteinase K; Tritirachium album proteinase K; endopeptidase K. Cat No: EXWM-4155. | |
| prostamide/prostaglandin F2α synthase | The enzyme contains a thioredoxin-type disulfide as a catalytic group. Prostamide H2 and prostaglandin H2 are the best substrates; the latter is converted to prostaglandin F2&alpha. The enzyme also reduces tert-butyl hydroperoxide, cumene hydroperoxide and H2O2, but not prostaglandin D2 or prostaglandin E2. Group: Enzymes. Synonyms: prostamide/PGF synthase; prostamide F synthase; prostamide/prostaglandin F synthase; tPGF synthase. Enzyme Commission Number: EC 1.11.1.20. 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-0502; prostamide/prostaglandin F2α synthase; EC 1.11.1.20; prostamide/PGF synthase; prostamide F synthase; prostamide/prostaglandin F synthase; tPGF synthase. Cat No: EXWM-0502. | |
| protein disulfide-isomerase | Needs reducing agents or partly reduced enzyme; the reaction depends on sulfhydryl-disulfide interchange. Group: Enzymes. Synonyms: S-S rearrangase. Enzyme Commission Number: EC 5.3.4.1. CAS No. 37318-49-3. PDI. 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-5507; protein disulfide-isomerase; EC 5.3.4.1; 37318-49-3; S-S rearrangase. Cat No: EXWM-5507. | |
| Protein Disulfide Isomerase from Human, Recombinant | Protein disulfide isomerases (PDIs) constitute a family of structurally related enzymes which catalyze disulfide bonds formation, reduction, or isomerization of newly synthesized proteins in the lumen of the endoplasmic reticulum (ER). They act also as chaperones, and are, therefore, part of a quality-control system for the correct folding of the proteins in the same subcellular compartment. PDI has been found to have moderate effects (25-fold) on the rate of oxidative folding of proteins in vitro. Recombinant Human Protein Disulfide Isomerase is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. Recomb... EC 5.3.4.1. CAS No. 37318-49-3. Purity: Greater than 95.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. PDI. Mole weight: 62.4 kDa. Stability: Lyophilized Protein Disulfide Isomerase although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Human PDI should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please avoid freeze-thaw cycles. Appearance: Sterile Filtered White lyophilized (freeze-dried) powder. Source: E. coli. Species: Human. Protein Disulfide Isomerase; PDI; EC 5.3.4.1; Prolyl 4- | |
| protein-disulfide reductase | This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with NAD+ or NADP+ as acceptor. Group: Enzymes. Synonyms: protein disulphide reductase; insulin-glutathione transhydrogenase; disulfide reductase; NAD(P)H2:protein-disulfide oxidoreductase. Enzyme Commission Number: EC 1.8.1.8. CAS No. 9029-19-0. 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-1652; protein-disulfide reductase; EC 1.8.1.8; 9029-19-0; protein disulphide reductase; insulin-glutathione transhydrogenase; disulfide reductase; NAD(P)H2:protein-disulfide oxidoreductase. Cat No: EXWM-1652. | |
| protein-disulfide reductase (glutathione) | Reduces insulin and some other proteins. Group: Enzymes. Synonyms: glutathione-insulin transhydrogenase; insulin reductase; reductase, protein disulfide (glutathione); protein disulfide transhydrogenase; glutathione-protein disulfide oxidoreductase; protein disulfide reductase (glutathione); GSH-insulin transhydrogenase; protein-disulfide interchange enzyme; protein-disulfide isomerase/oxidoreductase; thiol:protein-disulfide oxidoreductase; thiol-protein disulphide oxidoreductase. Enzyme Commission Number: EC 1.8.4.2. CAS No. 9082-53-5. 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-1670; protein-disulfide reductase (glutathione); EC 1.8.4.2; 9082-53-5; glutathione-insulin transhydrogenase; insulin reductase; reductase, protein disulfide (glutathione); protein disulfide transhydrogenase; glutathione-protein disulfide oxidoreductase; protein disulfide reductase (glutathione); GSH-insulin transhydrogenase; protein-disulfide interchange enzyme; protein-disulfide isomerase/oxidoreductase; thiol:protein-disulfide oxidoreductase; thiol-protein disulphide oxidoreductase. Cat No: EXWM-1670. | |
| Pseudo RACK1 | Pseudo RACK1 is an activator of protein kinase C which is a family of protein kinase enzymes involved in controlling the function of other proteins through the phosphorylation of hydroxyl groups of serine and threonine amino acid residues on these proteins. Consists of peptide derived from the C2 domain of PKC β linked by a disulfide bridge to the Antennapedia domain vector peptide. Molecular formula: C144H225N43O34S3. Mole weight: 3198.81. | |
| pyrimidodiazepine synthase | In the reverse direction, the reduction of 6-pyruvoyl-tetrahydropterin is accompanied by the opening of the 6-membered pyrazine ring and the formation of the 7-membered diazepine ring. The pyrimidodiazepine formed is an acetyldihydro derivative. Involved in the formation of the eye pigment drosopterin in Drosophila melanogaster. Group: Enzymes. Synonyms: PDA synthase; pyrimidodiazepine:oxidized-glutathione oxidoreductase (ring-opening, cyclizing); pyrimidodiazepine:glutathione-disulfide oxidoreductase (ring-opening, cyclizing). Enzyme Commission Number: EC 1.5.4.1. CAS No. 93586-06-2. 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-1555; pyrimidodiazepine synthase; EC 1.5.4.1; 93586-06-2; PDA synthase; pyrimidodiazepine:oxidized-glutathione oxidoreductase (ring-opening, cyclizing); pyrimidodiazepine:glutathione-disulfide oxidoreductase (ring-opening, cyclizing). Cat No: EXWM-1555. | |
| quinolinate synthase | An iron-sulfur protein that requires a [4Fe-4S] cluster for activity. Quinolinate synthase catalyses the second step in the de novo biosynthesis of NAD+ from aspartate in some bacteria, with EC 1.4.3.16 (L-aspartate oxidase) catalysing the first step and EC 2.4.2.19 [nicotinate-nucleotide diphosphorylase (carboxylating)] the third step. In Escherichia coli, two of the residues that are involved in the [4Fe-4S] cluster binding appear to undergo reversible disulfide-bond formation that regulates the activity of the enzyme. Group: Enzymes. Synonyms: NadA; QS; quinolinate synthetase. Enzyme Commission Number: EC 2.5.1.72. 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-2810; quinolinate synthase; EC 2.5.1.72; NadA; QS; quinolinate synthetase. Cat No: EXWM-2810. | |
| tentoxilysin | Zinc enzyme produced by Clostridium tetani. Proenzyme of 150 kDa is processed to disulfide-linked subunits of 100 and 50 kDa, the latter being responsible for the endopeptidase activity. Weakly inhibited by captopril, and phosphoramidon. The clostridial neurotoxins disable the neuroexocytosis apparatus, and have been described as the most toxic substances known. Tentoxilysin acts at the spinal inhibitory interneurons, blocking the release of various neurotransmitters to produce spastic paralysis. Type example of peptidase family M27 (tentoxilysin family). Group: Enzymes. Synonyms: tetanus neurotoxin. Enzyme Commission Number: EC 3.4.24.68. CAS No. 107231-12-9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4351; tentoxilysin; EC 3.4.24.68; 107231-12-9; tetanus neurotoxin. Cat No: EXWM-4351. | |
| thioredoxin-disulfide reductase | A flavoprotein (FAD). Group: Enzymes. Synonyms: NADP-thioredoxin reductase; NADPH-thioredoxin reductase; thioredoxin reductase (NADPH); NADPH2:oxidized thioredoxin oxidoreductase. Enzyme Commission Number: EC 1.8.1.9. CAS No. 9074-14-0. TrxR. 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-1653; thioredoxin-disulfide reductase; EC 1.8.1.9; 9074-14-0; NADP-thioredoxin reductase; NADPH-thioredoxin reductase; thioredoxin reductase (NADPH); NADPH2:oxidized thioredoxin oxidoreductase. Cat No: EXWM-1653. | |
| Thioredoxin Reductase (NADPH) from Yeast, Recombinant | Thioredoxin reductase (TrxR/NTR), an enzyme belonging to the flavoprotein family of pyridine nucleotide-disulfide oxidoreductases. Thioredoxin reductase (TrxR), a component of the thioredoxin system, including thioredoxin (Trx) and NADPH, catalyzes the transfer of electrons from NADPH to Trx, acts as a reductant of disulfide-containing proteins and participates in the defense system against oxidative stresses. Thioredoxin reductase (nadph) yeast recombinant produced in e. coli is a single, nonglycosylated, polypeptide chain having a molecular mass of 36 kda. thioredoxin reductase is purified by proprietary chromatographic techniques. Group: Enzymes. Synonyms: NADP-thioredoxin reductase; NADPH-thioredoxin reductase; thioredoxin reductase (NADPH); NADPH. CAS No. 9074-14-0. Purity: Greater than 98.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. TrxR. Mole weight: 36 kDa. Activity: 5 IU/mg. Stability: NTR although stable at 4°C for 3 weeks, should be stored desiccated below -18°C. Please prevent freeze thaw cycles. Appearance: Sterile Filtered White lyophilized (freeze-dried) powder. Source: E. coli. Species: Yeast. NADP-thioredoxin reductase; NADPH-thioredoxin reductase; thioredoxin reductase (NADPH); NADPH2:oxidized thioredoxin oxidoreductase; thioredoxin-disulfide reductase; NTR; TrxR. Cat No: NATE-0917. | |
| thiosulfate-thiol sulfurtransferase | The primary product is glutathione hydrodisulfide, which reacts with glutathione to give glutathione disulfide and sulfide. L-Cysteine can also act as acceptor. Group: Enzymes. Synonyms: glutathione-dependent thiosulfate reductase; sulfane reductase; sulfane sulfurtransferase. Enzyme Commission Number: EC 2.8.1.3. CAS No. 111070-24-7. 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-3361; thiosulfate-thiol sulfurtransferase; EC 2.8.1.3; 111070-24-7; glutathione-dependent thiosulfate reductase; sulfane reductase; sulfane sulfurtransferase. Cat No: EXWM-3361. | |
| Tissue plasminogen activator from Human, Recombinant | Tissue plasminogen activator (abbreviated PLAT or tPA) is a secreted serine proteasewhich converts the proenzymeplasminogento plasmin, a fibrinolyticenzyme. Plasminogen is synthesized as a single chain which is cleaved by PLAT into the two chain disulfide linked plasmin. This enzyme plays a role in cell migrationand tissue remodeling. Increased enzymatic activity causes hyperfibrinolysis, which manifests as excessive bleeding; decreased activity leads to hypofibrinolysiswhich can result in thrombosisor embolism. Tissue plasminogen activator human recombinant produced in cho cells is a single, glycosylated polypeptide chain containing 527 amino acids and having a mol...0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. tPA. Mole weight: 59008.71 Da. Activity: 580,000 IU/mg. Stability: Lyophilized t-PA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution tPA should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles. Appearance: Sterile Filtered White lyophilized (freeze-dried) powder. Source: CHO. Species: Human. Tissue-type plasminogen activator; EC 3.4.21.68; tPA; t-PA; t-plasminogen activator; TPA; T-PA. Cat No: NATE-0920. | |
| trypanothione-disulfide reductase | Trypanothione disulfide is the oxidized form of N1,N8-bis(glutathionyl)-spermidine from the insect-parasitic trypanosomatid Crithidia fasciculata. The enzyme from Crithidia fasciculata is a flavoprotein (FAD), whose activity is dependent on a redox-active cystine at the active centre. (cf. EC 1.8.1.7, glutathione-disulfide reductase). Group: Enzymes. Synonyms: trypanothione reductase; NADPH2:trypanothione oxidoreductase. Enzyme Commission Number: EC 1.8.1.12. CAS No. 102210-35-5. 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-1638; trypanothione-disulfide reductase; EC 1.8.1.12; 102210-35-5; trypanothione reductase; NADPH2:trypanothione oxidoreductase. Cat No: EXWM-1638. | |
| vitamin-K-epoxide reductase (warfarin-insensitive) | Vitamin K 2,3-epoxide is reduced to 3-hydroxy- (and 2-hydroxy-) vitamin K by 1,4-dithiothreitol, which is oxidized to a disulfide. Not inhibited by warfarin [cf. EC 1.17.4.4, vitamin-K-epoxide reductase (warfarin-sensitive)]. Group: Enzymes. Enzyme Commission Number: EC 1.17.4.5. CAS No. 97089-80-0. 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-1093; vitamin-K-epoxide reductase (warfarin-insensitive); EC 1.17.4.5; 97089-80-0. Cat No: EXWM-1093. | |
| vitamin-K-epoxide reductase (warfarin-sensitive) | Vitamin K 2,3-epoxide is reduced to vitamin K and possibly to vitamin K hydroquinone by 1,4-dithiothreitol, which is oxidized to a disulfide; some other dithiols and 4-butanethiol can also act. Inhibited strongly by warfarin [cf. EC 1.17.4.5, vitamin-K-epoxide reductase (warfarin-insensitive)]. Group: Enzymes. Enzyme Commission Number: EC 1.17.4.4. CAS No. 55963-40-1. 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-1092; vitamin-K-epoxide reductase (warfarin-sensitive); EC 1.17.4.4; 55963-40-1. Cat No: EXWM-1092. | |
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