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| Product | Description | |
|---|---|---|
| Dithiothreitol | threo-1,4-Dimercapto-2,3-butanediol; Clelands reagent. CAS No. 3483-12-3. Product ID: 1-01451. Molecular formula: C9H17NO2. Mole weight: 154.24. Purity: 0.98. Properties: mp 42 - 44°C. |  |
| Dithiothreitol (DTT) | Dithiothreitol (DTT) is the common name for a small-molecule redox reagent known as Cleland's reagent. DTT's oxidized form is a disulfide-bonded 6-membered ring. Its name derives from the four-carbon sugar, threose. DTT has an epimeric ('sister') compound, dithioerythritol (DTE).DTT is an unusually strong reducing agent, owing to its high conformational propensity to form a six-membered ring with an internal disulfide bond. It has a redox potential of -0.33 V at pH 7. The reduction of a typical disulfide bond proceeds by two sequential thiol-disulfide exchange reactions and is illustrated below. The intermediate mixed-disulfide state is unstable (i.e., poorly populated) because the...ting."DTT is frequently used to reduce the disulfide bonds of proteins and, more generally, T... Group: Biochemicals. Alternative Names: Cleland's reagent;; (2R,3R)-rel-1,4-Dimercapto-2,3-butanediol; (±)-1,4-Dimercapto-2,3-butanediol; (±)-Dithiothreitol; 1,4-Dithio-DL-threitol; 1,4-Dithiothreitol; DL-1,4-Dimercapto-2,3-dihydroxybutane; DL-1,4-Dithiothreitol; DL-Dithiothreitol; Sputolysin; WR 34678; threo-1,4-Dimercapto-2,3-butanediol; threo-2,3-Dihydroxy-1,4-butanedithiol; threo-2,3-Dihydroxy-1,4-dithiolbutane. Grades: Molecular Biology Grade. CAS No. 3483-12-3. Pack Sizes: 5g, 10g, 25g, 50g, 100g. Molecular Formula: C4H10O2S2, Molecular Weight: 154.24. US Biological Life Sciences. |  Worldwide |
| DL-Dithiothreitol | DL-Dithiothreitol. Group: Monomers. Alternative Names: 1,4-Dithiothreitol. CAS No. 3483-12-3. Product ID: (2S,3S)-1,4-bis(sulfanyl)butane-2,3-diol. Molecular formula: 154.25. Mole weight: C4H10O2S2. C([C@H]([C@@H](CS)O)O)S. InChI=1S/C4H10O2S2/c5-3 (1-7)4 (6)2-8/h3-8H, 1-2H2/t3-, 4-/m1/s1. VHJLVAABSRFDPM-QWWZWVQMSA-N. 98%. |  |
| DL-Dithiothreitol | DL-Dithiothreitol. Synonyms: threo-1,4-Dimercapto-2,3-butanediol, Clelands reagent, DTT. CAS No. 3483-12-3. Pack Sizes: 1, 5, 10, 25, 100 g in poly bottle. Product ID: CDC10-0048. Molecular formula: C4H10O2S2. Category: Antioxidant Cosmetic Chemicals. Product Keywords: Cosmetic Ingredients; Antioxidant Cosmetic Chemicals; DL-Dithiothreitol; CDC10-0048; 3483-12-3; C4H10O2S2; threo-1,4-Dimercapto-2,3-butanediol, Clelands reagent, DTT; 222-468-7; MFCD00004877; 3483-12-3. Purity: ≥98%. Color: White. EC Number: 222-468-7. Physical State: Powder. Solubility: H2O: soluble 50 mg/mL, clear, colorless to very faintly yellow. Quality Level: 200. Storage: 2-8°C. Boiling Point: 125 °C. Melting Point: 41-44 °C (lit.). Density: 1.04 g/mL at 20 °C. Product Description: An excellent reagent for maintaining SH groups in reduced state; quantitatively reduces disulfides. DTT is effective in sample buffers for reducing protein disulfide bonds prior to SDS-PAGE. DTT can also be used for reducing the disulfide bridge of the cross-linker N,N'-bis(acryloyl)cystamine to break apart the matrix of a polyacrylamide gel. DTT is less pungent and is less toxic than 2-mercaptoethanol. Typically, a seven fold lower concentration of DTT (100 mM) is needed than is used for 2-mercaptoethanol (5% v/v, 700 mM). |  |
| DTT (Dithiothreitol) | 100g Pack Size. Group: Analytical Reagents, Biochemicals, Carbohydrates. Formula: C4H10O2S2. CAS No. 3483-12-3. Prepack ID 19733320-100g. Molecular Weight 154.25. See USA prepack pricing. |  |
| DTT (Dithiothreitol) | 25g Pack Size. Group: Analytical Reagents, Biochemicals, Carbohydrates. Formula: C4H10O2S2. CAS No. 3483-12-3. Prepack ID 19733320-25g. Molecular Weight 154.25. See USA prepack pricing. | |
| DTT (Dithiothreitol) | 5g Pack Size. Group: Analytical Reagents, Biochemicals, Carbohydrates. Formula: C4H10O2S2. CAS No. 3483-12-3. Prepack ID 19733320-5g. Molecular Weight 154.25. See USA prepack pricing. | |
| 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. |  |
| L-Dithiothreitol | L-Dithiothreitol. Group: Biochemicals. Grades: Reagent Grade. CAS No. 16096-97-2. Pack Sizes: 250mg, 1g, 5g. US Biological Life Sciences. | Worldwide |
| L-(-)-Dithiothreitol | L-(-)-Dithiothreitol. Group: Biochemicals. Alternative Names: (-)-Cleland's Reagent; L-DTT. Grades: Highly Purified. CAS No. 16096-97-2. Pack Sizes: 1g, 2g, 5g. Molecular Formula: C4H10O2S2. US Biological Life Sciences. | Worldwide |
| 1,4-Dithio-DL-threitol | Reagent for the quantitative reduction of disulfide group. Prevents the oxidation of cholecystokinin during its extraction from brain and duodenal tissues. Cleavage of disulfide bonds in proteins. Uses: Used as a reagent in biochemistry to prevent oxidation of thiol groups and to reduce disulfides to dithiols; has been used as a radioprotectant; dithiothreitol (dtt) is the common name for a small-molecule redox reagent known as cleland's reagent. Synonyms: DL-1,4-Dithiothreitol; DTT; Cleland's reagent; threo-1,4-Dimercapto-2,3-butanediol; Dithiothreitol; dl-Dithiothreitol; 1,4-Dithiothreitol; D-Dtt; 1,4-Dithio-dl-threitol; DL-Dithiothreitol; threo-1,4-Dimercapto-2,3-butanediol. Grades: ≥ 99 % (Assay by titration). CAS No. 3483-12-3. Molecular formula: C4H10O2S2. Mole weight: 154.25. |  |
| Acid-PEG4-S-S-PEG4-acid | Acid-PEG4-SS-PEG4-acid is a homobifunctional cleavable linker with carboxylic acid groups at both sides. The terminal carboxylic acids can be reacted with primary amines in the presences of activators such as EDC and HATU to form stable amide bonds. The disulfide bonds can be cleaved by using Dithiothreitol (DTT) reagent. Synonyms: 4,7,10,13,20,23,26,29-octaoxa-16,17-dithiadotriacontanedioic acid; 4,7,10,13,20,23,26,29-Octaoxa-16,17-dithiadotriacontane-1,32-dioic acid. Grades: ≥95%. CAS No. 2055015-40-0. Molecular formula: C22H42O12S2. Mole weight: 562.69. | |
| adenylyl-sulfate reductase (glutathione) | This enzyme differs from EC 1.8.99.2, adenylyl-sulfate reductase, in using glutathione as the reductant. Glutathione can be replaced by γ-glutamylcysteine or dithiothreitol, but not by thioredoxin, glutaredoxin or mercaptoethanol. The enzyme from the mouseear cress, Arabidopsis thaliana, contains a glutaredoxin-like domain. The enzyme is also found in other photosynthetic eukaryotes, e.g., the Madagascar periwinkle, Catharanthus roseus and the hollow green seaweed, Enteromorpha intestinalis. Group: Enzymes. Synonyms: 5'-adenylylsulfate reductase (also used for EC 1.8.99.2); AMP,sulfite:oxidized-glutathione oxidoreductase (adenosine-5'-phosphosulfate-forming); plant-type 5'-adenylylsulfate reductase. Enzyme Commission Number: EC 1.8.4.9. CAS No. 355840-27-6. 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-1675; adenylyl-sulfate reductase (glutathione); EC 1.8.4.9; 355840-27-6; 5'-adenylylsulfate reductase (also used for EC 1.8.99.2); AMP,sulfite:oxidized-glutathione oxidoreductase (adenosine-5'-phosphosulfate-forming); plant-type 5'-adenylylsulfate reductase. Cat No: EXWM-1675. |  |
| cytosol nonspecific dipeptidase | A zinc enzyme with broad specificity, varying somewhat with source species. Activated and stabilized by dithiothreitol and Mn2+. Inhibited by bestatin and leucine. Group: Enzymes. Synonyms: N2-β-alanylarginine dipeptidase; glycyl-glycine dipeptidase; glycyl-leucine dipeptidase; iminodipeptidase; peptidase A; Pro-X dipeptidase; prolinase; prolyl dipeptidase; prolylglycine dipeptidase; iminodipeptidase; prolinase; L-prolylglycine dipe. Enzyme Commission Number: EC 3.4.13.18. CAS No. 9025-31-4. 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-4032; cytosol nonspecific dipeptidase; EC 3.4.13.18; 9025-31-4; N2-β-alanylarginine dipeptidase; glycyl-glycine dipeptidase; glycyl-leucine dipeptidase; iminodipeptidase; peptidase A; Pro-X dipeptidase; prolinase; prolyl dipeptidase; prolylglycine dipeptidase; iminodipeptidase; prolinase; L-prolylglycine dipeptidase; prolylglycine dipeptidase; diglycinase; Gly-Leu hydrolase; glycyl-L-leucine dipeptidase; glycyl-L-leucine hydrolase; glycyl-L-leucine peptidase; L-amino-acyl-L-amino-acid hydrolase; glycylleucine peptidase; glycylleucine hydrolase; glycylleucine dipeptide hydrolase; non-specific dipeptidase; human cytosolic non-specific dipeptidase; glycyl-L-leucine hydrolase; glycyl-glycine dipeptidase. Cat No: EXWM-4032. | |
| DTE | DTE (Dithioerythritol) is a sulfur-containing sugar derived from the corresponding 4-carbon monosaccharide erythrose; an epimer of dithiothreitol (DTT). DTE is a thiol reducing agent [1]. Uses: Scientific research. Group: Biochemical assay reagents. Alternative Names: Dithioerythritol; Clelands reagent. CAS No. 6892-68-8. Pack Sizes: 10 mM * 1 mL; 500 mg; 1 g; 5 g. Product ID: HY-15916. | |
| glycoprotein N-palmitoyltransferase | Acts on mucins. Activated by 1,4-dithiothreitol. Group: Enzymes. Synonyms: mucus glycoprotein fatty acyltransferase. Enzyme Commission Number: EC 2.3.1.96. CAS No. 97162-74-8. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2278; glycoprotein N-palmitoyltransferase; EC 2.3.1.96; 97162-74-8; mucus glycoprotein fatty acyltransferase. Cat No: EXWM-2278. | |
| Inorganic Pyrophosphatase from Saccharomyces cerevisiae, Recombinant | Pyrophosphatase (or inorganic pyrophosphatase) is an enzyme (EC 3.6.1.1) that catalyzes the conversion of one molecule of pyrophosphate to two phosphate ions. This is a highly exergonic reaction, and therefore can be coupled to unfavorable biochemical transformations in order to drive these transformations to completion. The functionality of this enzyme plays a critical role in lipid metabolism (including lipid synthesis and degradation), calcium absorption and bone formation, and DNA synthesis,as well as other biochemical transformations. Inorganic pyrophosphatase (ppase) catalyzes the hydrolysis of inorganic pyrophosphate to form orthophosphate. a variety ...actions that can be pulled far in the synthesis direction by the action of inorganic pyrophosphatase. Applications: Enhancing yields of rna in transcription reactions. Group: Enzymes. Synonyms: Pyrophosphate phosphohydrolase; inorganic pyrophosphatase; EC 3.6.1.1; 9024-82-2; iphosphate phosphohydrolase. CAS No. 9024-82-2. Inorganic pyrophosphatase. Mole weight: 71 kDa. Storage: at -20°C. Form: 20 mM Tris-HCl (pH 8.0), 100 mM KCl, 0.1 mM EDTA, 1 mM dithiothreitol and 50% glycerol. Source: E. coli. Species: Saccharomyces cerevisiae. Pyrophosphate phosphohydrolase; inorganic pyrophosphatase; EC 3.6.1.1; 9024-82-2; iphosphate phosphohydrolase. Cat No: NATE-1281. | |
| Lambda Protein Phosphatase, Recombinant | λ Protein Phosphatase (λ-PPase) is a Mn+2-dependent protein phosphatase with activity towards phosphorylated serine, threonine, tyrosine and histidine residues. It is the 221 amino-acid product of ORF221 open reading frame on bacteriophage lambda (1, 2). λ-PPase was expressed as a recombinant protein in E.coli and highly purified (2). This product is an intact enzyme of high quality without tag. Applications: Λ-ppase can be used to release phosphate groups from phosphorylated serine, threonine, tyrosine and histidine residues in proteins (2). it should be noted that different proteins are dephosphorylated at different rates. optimal reaction temperature is 30°c. inclusion of protease inhibitor cocktail and shortest incubation time is desired when assays are done with crude samples. Group: Enzymes. Synonyms: Protein phosphatase 1F; PPM1F; CAMKP; CaMKPase; FEM-2; POPX2; hFEM-2; Lambda Protein. Purity: >98% by SDS-PAGE. λ-PPase. Activity: 400,000 U/mg (400 U/ul). Storage: Store at -80°C. Avoid repeating freeze-thaw cycles. Form: 400 U/ul λ-PPase in 50mM HEPES (pH 7.5), 100mM NaCl, 2mM dithiothreitol, 0.1 mM MnCl2, 0.1mM EDTA, 50% glycerol, 0.01% Brij 35. Source: E. coli. Protein phosphatase 1F; PPM1F; CAMKP; CaMKPase; FEM-2; POPX2; hFEM-2; Lambda Protein Phosphatase; λ-PPase. Cat No: NATE-0990. | |
| L-methionine (S)-S-oxide reductase | Requires NADPH. The reaction occurs in the opposite direction to that given above. Dithiothreitol can replace reduced thioredoxin. L-Methionine (R)-S-oxide is not a substrate [see EC 1.8.4.14, L-methionine (R)-S-oxide reductase]. Group: Enzymes. Synonyms: fSMsr; methyl sulfoxide reductase I and II; acetylmethionine sulfoxide reductase; methionine sulfoxide reductase; L-methionine:oxidized-thioredoxin S-oxidoreductase; methionine-S-oxide reductase; free-methionine (S)-S-oxide reductase. Enzyme Commission Number: EC 1.8.4.13. 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-1668; L-methionine (S)-S-oxide reductase; EC 1.8.4.13; fSMsr; methyl sulfoxide reductase I and II; acetylmethionine sulfoxide reductase; methionine sulfoxide reductase; L-methionine:oxidized-thioredoxin S-oxidoreductase; methionine-S-oxide reductase; free-methionine (S)-S-oxide reductase. Cat No: EXWM-1668. | |
| Luciferase from Photinus pyralis (firefly), Recombinant | Firefly luciferase is an enzyme that catalyzes production of light from luciferin in the presence of Mg2+-ATP and oxygen. The reaction of this enzyme with luciferin, ATP, and O2 results in the emission of light. Luciferase activity can be inhibited by general anesthetics including isoflurane and ketamine/medetomidine thereby affecting the sensitivity of bioluminescence imaging. Applications: The reaction of this enzyme with luciferin, atp, and o2 results in the emission of light. luciferase can be used to detect trace amounts of atp. firefly luciferase is also one of the most commonly utilized reporter genes for the study of gene expression. the bioluminescent rea...pe I , > 5 ,000 ,000 units/mg protein; Type II, 15-30×106 light units/mg protein. Storage: -70°C. Form: Type I, Supplied as a solution in 50 mM Tris HCl pH 8.0, 1 mM dithiothreitol, 1 mM EDTA, and 10% (v/v) glycerol; Type II, Lyophilized powder approximately 20% protein; balance is primarily NaCl, HEPES buffer salts, and carbohydrate. Source: E. coli. Species: Photinus pyralis (firefly). Photinus-luciferin 4-monooxygenase (ATP-hydrolysing); firefly luciferase; luciferase (firefly luciferin); Photinus luciferin 4-monooxygenase (adenosine triphosphate-hydrolyzing); firefly luciferin luciferase; Photinus pyralis luciferase; EC 1.13.12.7; 61970-00-1. Cat No: NATE-0424. | |
| Menoxymycin A | Menoxymycin A is an antibiotic produced by Str. sp. KB10. It has a cytotoxic effect. It inhibits KB and N18-RE-105 cells with IC50 of 0.86 μmol/L and 0.14 μmol/L. Dithiothreitol (DDT) can reduce A and B cytotoxicity effect. Synonyms: [(2R)-2alpha-Methyl-3beta-hydroxy-6alpha-[(3aR)-2,6,11-trioxo-5alpha-methyl-7-hydroxy-3,3aalpha,5,6,11,11balpha-hexahydro-2H-furo[3,2-b]naphtho[2,3-d]pyran-10-yl]tetrahydro-2H-pyran-4alpha-yl]dimethylamine oxide. CAS No. 160492-65-9. Molecular formula: C24H27NO9. Mole weight: 473.47. | |
| Menoxymycin B | Menoxymycin B is an antibiotic produced by Str. sp. KB10. It has a cytotoxic effect. It inhibits KB and N18-RE-105 cells with IC50 of 0.22 μmol/L and 0.023 μmol/L. Dithiothreitol (DDT) can reduce A and B cytotoxicity effect. CAS No. 160523-76-2. Molecular formula: C25H31NO9. Mole weight: 489.51. | |
| Native Baker's yeast (S. cerevisiae) Glutathione Reductase | Glutathione reductase (GR) is a crucial flavoenzyme in the antioxidant defense system. Reduced glutathione (GSH) is used by glutathione peroxidase to detoxify hydrogen peroxide and in the precess is converted to oxidized glutathione (GSSG). The GSSG is then recycled back to GSH by glutathione reductase (GR) using NADPH that is then converted to NADP+. The regenerated GSH is then available to detoxify more hydrogen peroxide. The enzyme uses FAD as a cofactor. GR and glutathione peroxidase may inhibit lipid peroxidation by functioning as antioxidant enzymes in sperm. Glutathione reductase shares a structural motif with a number of other proteins including aspartyl ...reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase. Enzyme Commission Number: EC 1.6.4.2. CAS No. 9001-48-3. GR. Mole weight: mol wt 118 kDa. Activity: 100-300 units/mg protein (biuret). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 3.6 M (NH4)2SO4, pH 7.0, containing 0.1 mM dithiothreitol. Source: Baker's yeast (S. cerevisiae). EC 1.6.4.2; 9001-48-3; Glutathione Reductase; GR; glutathione reductase; glutathione reductase (NADPH); NADPH-glutathione reductase; GSH reductase; GSSG reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase. Cat No: NATE-0317. | |
| Native Barley β-Amylase | β-Amylase hydrolyzes the α-(1,4) glucan linkages in polysaccharides of three or more α-(1,4) linked D-glucose units. Natural substrates such as starch and glycogen are broken down into glucose and maltose. Pure, crystalline β-amylase preparation consists of four isoenzymes with different isoelectric points. The enzyme polymerizes very rapidly through the sulfhydryl groups in the absence of reducing agents. p-Chloromercuribenzoate inhibits the polymerization and the enzymatic activity. The reducing agents mercaptoethanol or dithiothreitol can completely restore the activity. Applications: Β-amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. β-amylase, has been used in various plant studies, such as carbon starvation studies in populus tremuloides. β-amylase, from barley, has been used to study how pressure and temperature affect catalytic activity. Group: Enzymes. Synonyms: saccharogen amylase; glycogenase; β amylase, β-amylase; 1,4-α-D-glucan maltohydrola. Enzyme Commission Number: EC 3.2.1.2. CAS No. 9000-91-3. β-Amylase. Activity: 20-80 units/mg protein (biuret). Storage: 2-8°C. Source: Barley. saccharogen amylase; glycogenase; β amylase, β-amylase; 1,4-α-D-glucan maltohydrolase; EC 3.2.1.2; 9000-91-3. Cat No: NATE-0761. | |
| Native Bovine Glutathione Peroxidase | Glutathione peroxidase is an enzyme which reduced lipid hydroperoxides into their corresponding alcohols. It also reduces free hydrogen peroxide in to water. In vivo it is responsible for protecting hemoglobin from oxidative breakdown. Applications: Glutathione peroxidase from bovine erythr ocytes was used as a positive control in cloning and characterization of full-length cdnas encoding two glutathione peroxidases (gpxs) from globodera rost ochiensis. it was used for the determination of glutathione peroxidase activity in human milk. Group: Enzymes. Synonyms: EC 1.11.1.9; GSH peroxidase; selenium-glutathione peroxidase; reduced glutathione peroxidase; 9013-66-5; GSH-Px, Glutathione:hydrogen-peroxide oxido-reductase; Glutathione Peroxidase. Enzyme Commission Number: EC 1.11.1.9. CAS No. 9013-66-5. Mole weight: mol wt 84.5 kDa. Activity: > 300 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing 25% sucrose and 2.5% dithiothreitol with sodium phosphate buffer salts. Source: Bovine erythr ocytes. Species: Bovine. EC 1.11.1.9; GSH peroxidase; selenium-glutathione peroxidase; reduced glutathione peroxidase; 9013-66-5; GSH-Px, Glutathione:hydrogen-peroxide oxido-reductase; Glutathione Peroxidase. Cat No: NATE-0322. | |
| Native Corn Phospho (enol)pyruvate Carboxylase | Phospho (enol)pyruvate carboxylase is a ubiquitous, highly regulated oligomeric, cytosolic enzyme in plants. Phospho (enol)pyruvate Carboxylase from corn was found to be highly susceptible to trypsin digestion. Phospho (enol)pyruvate carboxylase is a ubiquitous, highly regulated oligomeric, cytosolic enzyme in plants. Applications: Phospho (enol)pyruvate carboxylase has been used in a study to assess activity of carbon metabolism enzymes in wheat plants treated with kartolin-4 and exposed to water stress. it has also been used in a study to investigate the specific density of leaf as a characteristic of the photosynthetic apparatus. Group: Enzymes. Synonyms: phosphopyruvate (phosphate) carboxylase; PEP carboxylase; phosphoenolpyruvic carboxylase; PEPC; PEPCase; phosphate:oxaloacetate carboxy-lyase (phosphorylating); EC 4.. Enzyme Commission Number: EC 4.1.1.31. CAS No. 9067-77-0. PEPC. Activity: > 1 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 2.4 M (NH4)2SO4 solution containing 10 mM phosphate buffer, pH 7.0, 1 mM biotin, 5 mM dithiothreitol and 1 mM phenylmethylsulfonyl fluoride. Source: Corn. phosphopyruvate (phosphate) carboxylase; PEP carboxylase; phosphoenolpyruvic carboxylase; PEPC; PEPCase; phosphate:oxaloacetate carboxy-lyase (phosphorylating); EC 4.1.1.31; 9067-77-0. Cat No: NATE-0543. | |
| Native E. coli Inorganic Pyrophosphatase | Pyrophosphatase (or inorganic pyrophosphatase) is an enzyme (EC 3.6.1.1) that catalyzes the conversion of one molecule of pyrophosphate to two phosphate ions. This is a highly exergonic reaction, and therefore can be coupled to unfavorable biochemical transformations in order to drive these transformations to completion. The functionality of this enzyme plays a critical role in lipid metabolism (including lipid synthesis and degradation), calcium absorption and bone formation, and DNA synthesis,as well as other biochemical transformations. Applications: Increasing rna yield in transcription reaction; enhancing dna replication. Group: Enzymes. Synonyms: Pyrophosphate phosphohydrolase; inorganic pyrophosphatase; EC 3.6.1.1; 9024-82-2; iphosphate phosphohydrolase. CAS No. 9024-82-2. Inorganic pyrophosphatase. Form: 20 mM Tris-HCl, 100 mM NaCl, 1 mM Dithiothreitol, 0.1 mM EDTA, 50% Glycerol, pH 8.0 25°C. Store at -20°C. Source: E. coli. Pyrophosphate phosphohydrolase; inorganic pyrophosphatase; EC 3.6.1.1; 9024-82-2; iphosphate phosphohydrolase. Cat No: NATE-1272. | |
| Native E. coli RNA Polymerase, Holoenzyme | E. coli RNA Polymerase, Holoenzyme is the core enzyme saturated with sigma factor 70. The Holoenzyme initiates RNA synthesis from sigma 70 specific bacterial and phage promoters. E. coli RNA Polymerase, Core Enzyme consists of 5 subunits designated α, α, β?, β, and &omega. The enzyme is free of sigma factor and does not recognize any specific bacterial or phage DNA promoters. The enzyme retains the ability to transcribe RNA from nonspecific initiation sequences. Addition of sigma factors will allow the enzyme to initiate RNA synthesis from specific bacterial and phage promoters. Applications: Rna synthesis from e. coli promoter transcription initiation studies in vitro translation with purexpress. Group: Enzymes. Synonyms: E. coli RNA Polymerase, Holoenzyme; E. coli RNA Polymerase; RNA Polymerase; RNAP; RNApol; DNA-dependent RNA polymerase. RNAP. Mole weight: 400 kDa. Storage: at -20°C. Form: 20 mM Tris-HCl, pH 7.5, 100 mM NaCl, 0.1 mM EDTA, 1 mM dithiothreitol (DTT) and 50% glycerol. Source: E. coli. E. coli RNA Polymerase, Holoenzyme; E. coli RNA Polymerase; RNA Polymerase; RNAP; RNApol; DNA-dependent RNA polymerase. Cat No: NATE-1262. | |
| Native Escherichia coli Acetate Kinase | In molecular biology, acetate kinase (EC 2.7.2.1), which is predominantly found in micro-organisms, facilitates the production of acetyl-CoA by phosphorylating acetate in the presence of ATP and a divalent cation. Short-chain fatty acids (SCFAs) play a major role in carbon cycle and can be utilized as a source of carbon and energy by bacteria. The enzyme is important in the process of glycolysis, enzyme levels being increased in the presence of excess glucose. The growth of a bacterial mutant lacking acetate kinase has been shown to be inhibited by glucose, suggesting that the enzyme is involved in excretion of excess carbohydRate. A related enzyme, butyRate kinase, facili...rom escherichia coli has been used as part of an atp-regenerating system to study the kinetics of agonist-stimulated transphosphatidylatio. Group: Enzymes. Synonyms: Acetate kinase (phosphorylating); Acetic kinase; Acetokinase; AK; EC 2.7.2.1; 9027-42-3; Acetate kinase. Enzyme Commission Number: EC 2.7.2.1. CAS No. 9027-42-3. Acetate kinase. Activity: > 150 units/mg protein (biuret). Storage: -20°C. Form: Lyophilized powder containing trehalose with small amounts of potassium phosphate, magnesium chloride, and dithiothreitol. Source: Escherichia coli. Acetate kinase (phosphorylating); Acetic kinase; Acetokinase; AK; EC 2.7.2.1; 9027-42-3; Acetate kinase. Cat No: NATE-0017. | |
| Native Human Glutathione Peroxidase | Glutathione peroxidase is an enzyme which reduced lipid hydroperoxides into their corresponding alcohols. It also reduces free hydrogen peroxide in to water. In vivo it is responsible for protecting hemoglobin from oxidative breakdown. At the reported ph optimum of 8.8, we have found the activity to be approx. 10 times that at ph 7.0. however, to remain consistent with literature and avoid complications arising from non-enzymatic oxidation of gsh, our unit is defined at ph 7.0. Group: Enzymes. Synonyms: EC 1.11.1.9; GSH peroxidase; selenium-glutathione peroxidase; reduced glutathione peroxidase; 9013-66-5; GSH-Px, Glutathione:hydrogen-peroxide oxido-reductase; Glutathione Peroxidase. Enzyme Commission Number: EC 1.11.1.9. CAS No. 9013-66-5. GSH-Px. Activity: > 30 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing 25% sucrose, 3% dithiothreitol, and sodium phosphate buffer salts. Source: Human erythr ocytes. Species: Human. EC 1.11.1.9; GSH peroxidase; selenium-glutathione peroxidase; reduced glutathione peroxidase; 9013-66-5; GSH-Px, Glutathione:hydrogen-peroxide oxido-reductase; Glutathione Peroxidase. Cat No: NATE-0323. | |
| Native Leuconostoc mesenteroides Mannitol Dehydrogenase | In enzymology, a mannitol 2-dehydrogenase (EC 1.1.1.67) is an enzyme that catalyzes the chemical reaction:D-mannitol + NAD+<-> D-fructose + NADH + H+. Thus, the two substrates of this enzyme are D-mannitol and NAD+, whereas its 3 products are D-fructose, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in fructose and mannose metabolism. Applications: This preparation is useful in the determination of mannitol in urine. can be used for the production of d-mannitol. it has been used in a study to assess glucosylglycerol and glucosylglycerate as enzyme stabilizers. Group: Enzymes. Synonyms: mannitol dehydrogenase; D-mannitol dehydrogenase; mannitol dehydrogenase; mannitol 2-dehydrogenase; EC 1.1.1.67; 9001-65-4. Enzyme Commission Number: EC 1.1.1.67. CAS No. 9001-65-4. Mannitol Dehydrogenase. Mole weight: 136 kDa. Activity: > 60 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing buffer salts, potassium phosphate, and dithiothreitol. Source: Leuconostoc mesenteroides. mannitol dehydrogenase; D-mannitol dehydrogenase; mannitol dehydrogenase; mannitol 2-dehydrogenase; EC 1.1.1.67; 9001-65-4. Cat No: NATE-0435. | |
| Native Pigeon Carnitine Acetyltransferase | Carnitine acetyltransferase maintains the cellular and mitochondrial levels of acetyl-CoA, a key cofactor required for oxidative metabolism, by catalyzing an equilibrium between acetyl-CoA and acetyl-L-carnitine, a storage form of activated acetate. Carnitine acetyltransferase also maintains the pool of acetyl-CoA required for neuronal and nonneuronal acetylcholine production. Protein determined by biuret. Group: Enzymes. Synonyms: acetyl-CoA-carnitine O-acetyltransferase; acetylcarnitine transferase; carnitine acetyl coenzyme A transferase; carnitine acetylase; carnitine acetyltransferase; carnitine-acetyl-CoA transferase; CATC; 9029-90-7; carnitine O-acetyltransferase; EC 2.3.1.7; CRAT; CAT. Enzyme Commission Number: EC 2.3.1.7. CAS No. 9029-90-7. CRAT. Activity: > 70 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension. Crystalline suspension in 3.2 M (NH4)2SO4 solution, 50 mM potassium phosphate, 1 mM dithiothreitol, pH 7.0. Source: Pigeon breast muscle. Species: Pigeon. acetyl-CoA-carnitine O-acetyltransferase; acetylcarnitine transferase; carnitine acetyl coenzyme A transferase; carnitine acetylase; carnitine acetyltransferase; carnitine-acetyl-CoA transferase; CATC; 9029-90-7; carnitine O-acetyltransferase; EC 2.3.1.7; CRAT; CAT. Cat No: NATE-0159. | |
| Native Porcine Catechol-O-methyl Transferase | Catechol-O-methyltransferase (COMT; EC 2.1.1.6) is one of several enzymes that degrade catecholamines such as dopamine, epinephrine, and norepinephrine. In Humans, catechol-O-methyltransferase protein is encoded by the COMT gene. As the regulation of catecholamines is impaired in a number of medical conditions, several pharmaceutical drugs target COMT to alter its activity and therefore the availability of catecholamines. COMT was first discovered by the biochemist Julius Axelrod in 1957. Group: Enzymes. Synonyms: catechol O-methyltransferase; COMT; COMT I; COMT II; S-COMT (soluble form of catechol-O-methyltransferase); MB-COMT (membrane-bound form of catechol-O-methyltransferase); catechol methyltransferase; catecholamine O-methyltransferase; EC 2.1.1.6; 9012-25-3; Py. Enzyme Commission Number: EC 2.1.1.6. CAS No. 9012-25-3. COMT. Activity: > 150 units/mg protein. Form: Lyophilized powder containing phosphate buffer and dithiothreitol. Source: Porcine liver. Species: Porcine. catechol O-methyltransferase; COMT; COMT I; COMT II; S-COMT (soluble form of catechol-O-methyltransferase); MB-COMT (membrane-bound form of catechol-O-methyltransferase); catechol methyltransferase; catecholamine O-methyltransferase; EC 2.1.1.6; 9012-25-3; Pyrocatechol-O-methyl Transferase; S-Adenosyl-L-methionine:catechol O-methyltransferase. Cat No: NATE-0148. | |
| Native Rabbit S-(5'-Adenosyl)-L-homocysteine Hydrolase | Enzyme in vertebrates which catabolizes S-adenosyl-L-homocysteine. Group: Enzymes. Synonyms: Adenosylhomocysteinase; EC 3.3.1.1; S-adenosylhomocysteine synthase; S-adenosylhomocysteine hydrolase; adenosylhomocysteine hydrolase (ambiguous); S-adenosylhomocysteinase; SAHase; AdoHcyase; 9025-54-1. Enzyme Commission Number: EC 3.3.1.1. CAS No. 9025-54-1. AHCY. Activity: > 10 units/mg protein (Lowry). Storage: -70°C. Form: buffered aqueous glycerol solution; Solution in 25 mM Tris, pH 7.4, containing 1 mM dithiothreitol, 1 mM EDTA, and 20% glycerol. Source: Rabbit erythrocytes. Species: Rabbit. Adenosylhomocysteinase; EC 3.3.1.1; S-adenosylhomocysteine synthase; S-adenosylhomocysteine hydrolase; adenosylhomocysteine hydrolase (ambiguous); S-adenosylhomocysteinase; SAHase; AdoHcyase; 9025-54-1. Cat No: NATE-0662. | |
| Native Sweet potato β-Amylase | β-Amylase hydrolyzes the α-(1,4) glucan linkages in polysaccharides of three or more α-(1,4) linked D-glucose units. Natural substrates such as starch and glycogen are broken down into glucose and maltose. Pure, crystalline β-amylase preparation consists of four isoenzymes with different isoelectric points. The enzyme polymerizes very rapidly through the sulfhydryl groups in the absence of reducing agents. p-Chloromercuribenzoate inhibits the polymerization and the enzymatic activity. The reducing agents mercaptoethanol or dithiothreitol can completely restore the activity. Applications: Β-amylase is used to hydrolyze α bonds of α-linke...ng and removing staphylococcus aureus biofilms. the enzyme has also been used to prepare β-limit dextrin from waxy maize starch. Group: Enzymes. Synonyms: saccharogen amylase; glycogenase; β amylase, β-amylase; 1,4-α-D-glucan maltohydrolase; EC 3.2.1.2; 9000-91-3. Enzyme Commission Number: EC 3.2.1.2. CAS No. 9000-91-3. β-Amylase. Mole weight: 127.5. Activity: > 750 units/mg protein (E1%/280). Storage: 2-8°C. Form: ammonium sulfate suspension. Crystalline suspension in 2.3 M (NH4)2SO4. Source: Sweet potato. saccharogen amylase; glycogenase; β amylase, β-amylase; 1,4-α-D-glucan maltohydrolase; EC 3.2.1.2; 9000-91-3. Cat No: NATE-0762. | |
| 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. | |
| Protein Kinase A Catalytic Subunit from Bovine, Recombinant | Protein Kinase A (PKA) catalyzes the transfer of the terminal phosphate of ATP to threonine or serine residues in a variety of protein substrates. The enzyme is composed of two subunit types: a catalytic subunit and a regulatory subunit. In the absence of cAMP, the two subunits are bound to each other and no catalysis can take place. In the presence of cAMP, the regulatory subunit binds cAMP, thus releasing the catalytic subunit. In the presence of cAMP, the catalytic subunit exists as a monomer of 40,862 Da (amino acid sequence), but on SDS-PAGE the apparent molecular mass is 43,000 Da. Group: Enzymes. Synonyms: PKA; cAMP-dependent protein kinase; ATP:protein phosphotransferase (cAMP-dependent); Protein K. Enzyme Commission Number: EC 2.7.11.11. Activity: >9 units/μg protein. Storage: Store at -20°C. Form: Lyophilized from a solution containing approximately: 80% sucrose, 19% potassium phosphate buffer, pH 6.7, 0.0625% 2-mercaptoethanol(2-ME), 0.002% EDTA, 0.016% dithiothreitol (DTT), and ≤1% protein. The lyophilized product may contain traces of DTT or 2-ME. Source: Bovine Heart. Species: Bovine. PKA; cAMP-dependent protein kinase; ATP:protein phosphotransferase (cAMP-dependent); Protein Kinase A catalytic subunit; Protein kinase A; PKAC; cAMP-dependent protein kinase catalytic subunit; PRKAC. Cat No: NATE-1889. | |
| selenocysteine lyase | A pyridoxal-phosphate protein. Dithiothreitol or 2-mercaptoethanol can act as the reducing agent in the reaction. The enzyme from animals does not act on cysteine, serine or chloroalanine, while the enzyme from bacteria shows activity with cysteine (cf. EC 2.8.1.7, cysteine desulfurase). Group: Enzymes. Synonyms: selenocysteine reductase; selenocysteine β-lyase. Enzyme Commission Number: EC 4.4.1.16. CAS No. 82047-76-5. 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-5318; selenocysteine lyase; EC 4.4.1.16; 82047-76-5; selenocysteine reductase; selenocysteine β-lyase. Cat No: EXWM-5318. | |
| [Skp1-protein]-hydroxyproline N-acetylglucosaminyltransferase | Skp1 is a cytoplasmic and nuclear protein required for the ubiquitination of cell cycle regulatory proteins and transcriptional factors. In Dictyostelium Skp1 is modified by the linear pentasaccharide Galα1-6Galα1-L-Fucα1-2Galβ1-3GlcNAc, which is attached to a hydroxyproline residue at position 143. This enzyme catalyses the first step in the building up of the pentasaccharide by attaching an N-acetylglucosaminyl group to the hydroxyproline residue. It requires dithiothreitol and a divalent cation for activity. Group: Enzymes. Synonyms: Skp1-HyPro GlcNAc-transferase; UDP-N-acetylglucosamine (GlcNAc):hydroxyproline polypeptide GlcNAc-transferase; UDP-GlcNAc:Skp1-hydroxyproline GlcNAc. Enzyme Commission Number: EC 2.4.1.229. CAS No. 256531-81-4. 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-2458; [Skp1-protein]-hydroxyproline N-acetylglucosaminyltransferase; EC 2.4.1.229; 256531-81-4; Skp1-HyPro GlcNAc-transferase; UDP-N-acetylglucosamine (GlcNAc):hydroxyproline polypeptide GlcNAc-transferase; UDP-GlcNAc:Skp1-hydroxyproline GlcNAc-transferase; UDP-GlcNAc:hydroxyproline polypeptide GlcNAc-transferase; UDP-N-acetyl-D-glucosamine:[Skp1-protein]-hydroxyproline N-acetyl-D-glucosaminyl-transferase. Cat No: EXWM-2458. | |
| 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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