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| Product | Description | |
|---|---|---|
| 4A Molecular Sieve PNMIC0020-1 | Molecular sieve 4A is used as a desiccant in a range of industrial applications. It refers to the adsorption process using molecules with a pore size of 4A0 or 4Å. It simply means that molecules with a pore size greater than 4a cannot be used for adsorption. Typically, they are the sodium form of the A-type structure. Uses: Polyester additives; sewage treatment; metallurgical industry; agriculture: soil amendments; medicine: silver-loaded zeolite antibacterial agent; petrochemical industry: catalysts, desiccants, adsorbents. Group: Microporous molecular sieves. CAS No. Density: ~4Å. Catalog: PNMIC0020-1. |  |
| Calcium chloride anhydrous | Calcium chloride occurs as a white or colorless crystalline powder,granules, or crystalline mass, and is hygroscopic (deliquescent). Synonyms: Calcii chloridum dihydricum; calcii chloridum hexahydricum. CAS No. 10043-52-4. Product ID: PE0385. Molecular formula: CaCl2. Mole weight: 110.98 (for anhydrous). Category: Desiccants; Preservatives; Adsorbentss. Product Keywords: Pharmaceutical Excipients; Other Materials; Desiccants; Calcium chloride anhydrous; PE0385; M4I0D6VV5M; 10043-52-4; 10043-52-4. UNII: M4I0D6VV5M. Chemical Name: Calcium chloride anhydrous. Grade: Pharmceutical Excipients. Administration route: Infiltration, Intramuscular, Intraocular, Intrathecal, Intravenous, Intravitreal, Ophthalmic, oral, Respiratory(Inhalation). Dosage Form: Injection, Soultion, Injectable, Liposomal, Susupension, Drops, Capsule, Concentrate. Stability and Storage Conditions: Calcium chloride is chemically stable; however, it should be protected from moisture. Store in airtight containers in a cool, dry place. Applications: The main applications of calcium chloride as an excipient relate to its dehydrating properties and, therefore, it has been used as an antimicrobial preservative, as a desiccant, and as an astringent in eye lotions. Therapeutically, calcium chloride injection 10% (as the dihydrate form) is used to treat hypocalcemia. Safety: Calcium chloride is used in topical, ophthalmic, and injection preparation |  |
| Calcium chloride dihydrate77% | Calcium chloride occurs as a white or colorless crystalline powder,granules, or crystalline mass, and is hygroscopic (deliquescent). Synonyms: Calcii chloridum dihydricum; calcii chloridum hexahydricum. CAS No. 10035-04-8. Product ID: PE-0673. Molecular formula: CaCl2` 2H2O. Mole weight: 147.0 (for dihydrate). Category: Antimicrobial preservative; therapeutic agent; water-absorbing. agent. Product Keywords: Desiccants; PE-0673; Calcium chloride dihydrate77%; 10035-04-8; Calcii chloridum dihydricum; calcii chloridum hexahydricum. UNII: M4I0D6VV5M. Chemical Name: Calcium chloride dihydrate. Grade: Pharmaceutical grade. Administration route: Infiltration, Intramuscular, Intraocular, Intrathecal, Intravenous, Intravitreal, Ophthalmic, oral, Respiratory(Inhalation). Dosage Form: Injection, Soultion, Injectable, Liposomal, Susupension, Drops, Capsule,Concentrate. Stability and Storage Conditions: Calcium chloride is chemically stable; however, it should be protected from moisture. Store in airtight containers in a cool, dry place. Applications: The main applications of calcium chloride as an excipient relate to its dehydrating properties and, therefore, it has been used as an antimicrobial preservative, as a desiccant, and as an astringent in eye lotions. Therapeutically, calcium chloride injection 11% (as the dihydrate form) is used to treat hypocalcemia. Safety: Calcium chloride is used in topical, ophthalmic, and in | |
| Calcium chloride hexahydrate | Calcium chloride occurs as a white or colorless crystalline powder,granules, or crystalline mass, and is hygroscopic (deliquescent). Synonyms: Calcii chloridum dihydricum; calcii chloridum hexahydricum. CAS No. 7774-34-7. Product ID: PE0387. Molecular formula: CaCl2· 6H2O. Mole weight: 219.1 (for hexahydrate). Category: Desiccants; Preservatives; Adsorbentss. Product Keywords: Pharmaceutical Excipients; Other Materials; Desiccants; Calcium chloride hexahydrate; PE0387; M4I0D6VV5M; 7774-34-7; 7774-34-7. UNII: M4I0D6VV5M. Chemical Name: Calcium chloride hexahydrate. Grade: Pharmceutical Excipients. Administration route: Infiltration, Intramuscular, Intraocular, Intrathecal, Intravenous, Intravitreal, Ophthalmic, oral, Respiratory(Inhalation). Dosage Form: Injection, Soultion, Injectable, Liposomal, Susupension, Drops, Capsule, Concentrate. Stability and Storage Conditions: Calcium chloride is chemically stable; however, it should be protected from moisture. Store in airtight containers in a cool, dry place. Applications: The main applications of calcium chloride as an excipient relate to its dehydrating properties and, therefore, it has been used as an antimicrobial preservative, as a desiccant, and as an astringent in eye lotions. Therapeutically, calcium chloride injection 12% (as the dihydrate form) is used to treat hypocalcemia. Safety: Calcium chloride is used in topical, ophthalmic, and injection p | |
| Calcium sulfate | Calcium sulfate. CAS No. 7778-18-9. Product ID: PE-0226. Molecular formula: CaO4S. Mole weight: 136.141. Category: Desiccants; Filler Excipients; Absorbent. Product Keywords: Pharmaceutical Excipients; Solid Dosage Form; Filler Excipients; Absorbent; Calcium sulfate; PE-0226; CaO4S; 7778-18-9; 7778-18-9. Appearance: White powder or granules. Purity: 0.98. EC Number: 231-900-3. Solubility: water, 1.216e+005 mg/L @ 25 °C (est). Storage: Store at RT. Boiling Point: 333.6ºC at 760 mmHg. Melting Point: 1450 °C. Density: 2.96 g/cm3. | |
| Calcium sulfate dihydrate | Both calcium sulfate and calcium sulfate dihydrate are white or off-white, fine, odorless, and tasteless powder or granules. Synonyms: Calcium sulfate dihydrate alabaster; calcii sulfas dihydricus; Compactrol; Destab; E516; gypsum; light spar; mineral white; native calcium sulfate; precipitated calcium sulfate; satinite; satin spar; selenite; terra alba; USG Terra Alba. CAS No. 10101-41-4. Product ID: PE0384. Molecular formula: CaSO4·2H2O. Mole weight: 172.17. Category: Desiccant; Diluents. Product Keywords: Pharmaceutical Excipients; Other Materials; Desiccants; Calcium sulfate dihydrate; PE0384; WAT0DDB505; 10101-41-4; 10101-41-4. UNII: WAT0DDB505. Chemical Name: Calcium sulfate dihydrate. Grade: Pharmceutical Excipients. Stability and Storage Conditions: Calcium sulfate is chemically stable. Anhydrous calcium sulfate is hygroscopic and may cake on storage. Store in a well-closed container in a dry place, avoiding heat. Safety: Calcium sulfate dihydrate is used as an excipient in oral capsule and tablet formulations. At the levels at which it is used as an excipient, it is generally regarded as nontoxic. However, ingestion of a sufficiently large quantity can result in obstruction of the upper intestinal tract after absorption of moisture. Owing to the limited intestinal absorption of calcium from its salts, hypercalcemia cannot be induced even after the ingestion of massive oral doses. Calcium salts ar | |
| Triethylene Glycol | Triethylene glycol, TEG, or triglycol is a colorless odorless viscous liquid with molecular formula HOCH2CH2OCH2CH2OCH2CH2OH. It is used as a plasticizer for vinyl. It is also used in air sanitizer products, such as Oust or Clean and Pure. When aerosolized it acts as a disinfectant. Glycols are also used as liquid desiccants for natural gas and in air conditioning systems. It is an additive for hydraulic fluids and brake fluids and is used as a base for smoke machine fluid in the entertainment industry. Group: Alcohols. Alternative Names: Triglycol. CAS No. 112-27-6. Molecular formula: C6H14O4. Mole weight: 150.17. Appearance: Clear liquid. IUPACName: 2-[2-(2-Hydroxyethoxy)ethoxy]ethanol. Canonical SMILES: C(COCCOCCO)O. Density: 1.124g/ml. Catalog: ACM112276. | |
| (2S)-3,4-Dihydro-1,2(2H)-pyridinedicarboxylic Acid 1,2-Bis(1,1-dimethylethyl) Ester | (2S)-3,4-Dihydro-1,2(2H)-pyridinedicarboxylic Acid 1,2-Bis(1,1-dimethylethyl) Ester is an intermediate used in the synthesis of Isodesmosine Chloride Hydrate (Synthetic) (I815051), which is a component of elastin and also it is extremely hygroscopic and must be stored over a desiccant such as silica gel. Group: Biochemicals. Grades: Highly Purified. Pack Sizes: 2.5mg, 5mg. Molecular Formula: C15H25NO4. US Biological Life Sciences. |  Worldwide |
| (2S) -[Bis[ (1, 1-dimethylethoxy) carbonyl]amino]-5-hexenoic Acid 1,1-Dimethylethyl Ester | (2S) -[Bis[ (1, 1-dimethylethoxy) carbonyl]amino]-5-hexenoic Acid 1,1-Dimethylethyl Ester is an intermediate in the synthesis of Isodesmosine Chloride Hydrate which is a component of elastin. It is extremely hygroscopic and must be stored over a desiccant such as silica gel. Group: Biochemicals. Grades: Highly Purified. CAS No. 226985-05-3. Pack Sizes: 5mg, 10mg. Molecular Formula: C20H35NO6. US Biological Life Sciences. | Worldwide |
| Acetyl-Coenzyme A acetyltransferase 2 from Human, Recombinant | ACAT2 enzyme participates in lipid metabolism. ACAT2 takes part in lipoprotein assembly, catalyzing cholesterol esterification in mammalian cells. ACAT2 is an integral membrane protein that localizes to the endoplasmic reticulum of human intestinal cells. ACAT2 deficiency contributes to severe mental retardation and hypotonus. Acat2 recombinant human produced in e. coli is a single, non-glycosylated polypeptide chain containing 433 amino acids (1-397 a.a.) and having a molecular mass of 45.4 kda. the acat2 is fused to 36 amino acid his-tag at n-terminus and purified by proprietary chromatographic techniques. Group: Enzymes. Synonyms: Acetyl-CoA acetyltransferase cytosolic; Cytosolic acetoacetyl-CoA thiolase; ACAT2; Acetyl CoA transferase-like protein; ACAT-2. Purity: Greater than 95.0% as determined by SDS-PAGE. ACAT-2. Mole weight: 45.4 kDa. Stability: ACAT2 Human although stable at 4°C for 1 week, should be stored desiccated below -18°C. Please prevent freeze thaw cycles. Appearance: Sterile Filtered clear solution. Source: E. coli. Species: Human. Acetyl-CoA acetyltransferase cytosolic; Cytosolic acetoacetyl-CoA thiolase; ACAT2; Acetyl CoA transferase-like protein; ACAT-2. Cat No: NATE-0798. |  |
| Acyl-Coenzyme A Dehydrogenase 8 from Human, Recombinant | Acyl CoA dehydrogenase is the enzymeused to catalyzethe first step of β-oxidationin Fatty acid metabolism. Acyl-coenzyme A (CoA) dehydrogenases (ACADs) are a family of mitochondrial enzymes that catalyze the first dehydrogenation step in the bets-oxidation of fatty acyl-CoA derivatives. Several human ACADs exist and all ACADs catalyze the same initial dehydrogenation of the substrate at the beta-carbon atom and require electron transfer flavoprotein as an alectron acceptor. The predicted 415-amino acid ACAD8 protein contains many of the residues conserved in most other ACADs, including an active site glutamic acid residue and residues important for tetramer f...mber 8 mitochondrial; ACAD-8; Isobutyryl-CoA dehydrogenase; Activator-recruited cofactor 42 kDa component; ARC42; FLJ22590. Purity: Greater than 95.0% as determined by SDS-PAGE. ACAD-8. Mole weight: 47.7 kDa. Stability: ACAD8 although stable at 4°C for 1 week, should be stored desiccated 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 clear solution. Source: E. coli. Species: Human. Acyl-CoA dehydrogenase family member 8 mitochondrial; ACAD-8; Isobutyryl-CoA dehydrogenase; Activator-recruited cofactor 42 kDa component; ARC42; FLJ22590. Cat No: NATE-0801. | |
| Alanine Aminotransferase from Human, Recombinant | Alanine transaminase (ALT) is a transaminase enzyme. It is also called alanine aminotransferase (ALAT) and was formerly called serum glutamate-pyruvate transaminase (SGPT) or serum glutamic-pyruvic transaminase (SGPT). ALT is found in plasma and in various body tissues, but is most common in the liver. It catalyzes the two parts of the alanine cycle. Serum ALT level, serum AST (aspartate transaminase) level, and their ratio (AST/ALT ratio) are commonly measured clinically as biomarkers for liver health. The tests are part of blood panels. Alanine aminotransferase human recombinant produced in e. coli is a homodimer, nonglycosylated, polypeptide chain containing 495a.a...inotransferase; pyruvate transaminase; pyruvate-alanine aminotransferase; pyruvate-glutamate transaminase. CAS No. 9000-86-6. Purity: Greater than 95.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. ALT. Mole weight: 54,479 Da. Activity: 1,000 U/mg. Stability: AAT1 although stable at 10°C for 5 days, should be stored desiccated below -18°C. Please prevent freeze-thaw cycles. Appearance: Sterile liquid formulation. Source: E. coli. Species: Human. ALT1; Glutamic-pyruvic transaminase 1; GPT 1; Glutamic-alanine transaminase 1; AAT1; ALT; ALAT; SGPT; Alanine transaminase; alanine aminotransferase; GPT; β-alanine aminotransferase; alanine-α | |
| Beta Lactamase from E.coli, Recombinant | Beta-lactamase is a type of enzyme (EC 3.5.2.6) produced by some bacteria that is responsible for their resistance to beta-lactam antibiotics like penicillins, cephalosporins, cephamycins and carbapenems. These antibiotics have a common element in their molecular structure: a four-atom ring known as a beta-lactam. The lactamase enzyme breaks that ring open, deactivating the molecule's antibacterial properties. Group: Enzymes. Synonyms: b-Lactamase; EC 3.5.2.6; TEM precursor; β-lactamase. Enzyme Commission Number: EC 3.5.2.6. Purity: Greater than 90.0% as determined by: (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. β-Lactamase. Mole weight: 29 kDa. Activity: 700IU/mg. Stability: Lyophilized Beta Lactamase although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Beta Lactamase Recombinant 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. Form: Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM Phosphate buffer pH-7. Source: E. coli. Species: E. coli. b-Lactamase; EC 3.5.2.6; TEM precursor; β-lactamase. Cat No: NATE-1886. | |
| Calcium Chloride | CALCIUM CHLORIDE, ANHYDROUS, DESICCANT, ACS Reagent, granular, Formula: CaCl2. CAS No. 10043-52-4. Noah Chemicals San Antonio, Texas. ISO 9001:2015 Certified. Request a Quote Today! |  Texas TX |
| Calcium Chloride Anhydrous, ACS | Calcium chloride is highly hygroscopic and is often used as a desiccant. Group: Biochemicals. Alternative Names: Calcium (II) chloride. Grades: ACS Grade. CAS No. 10043-52-4. Pack Sizes: 100g, 500g, 1Kg, 2.5Kg. Molecular Formula: CaCl2, Molecular Weight: 110.98. US Biological Life Sciences. | Worldwide |
| Calcium Chloride Desiccant | Calcium Chloride Desiccant. CAS No. 10043-52-4. Molecular Formula CaCl2. Chemical Reagents |  Cater Chemicals Corp. Illinois IL |
| Calcium Chloride Dihydrate | Hygroscopic flakes or pellets. Uses: food additive, desiccant. Group: halide salt. CAS No. 10035-04-8. |  |
| Calcium chloride hexahydrate | Calcium chloride are inorganic compounds with the chemical formula CaCl2(H2O)x, where x = 0, 1, 2, 4, and 6. All of these salts are a highly soluble in water. They are mainly used for deicing and dust control. Because the anhydrous salt is hygroscopic, it is used as a desiccant. Group: Electrolytes. Alternative Names: Calcium chloride 6-hydrate. CAS No. 7774-34-7. Product ID: calcium; dichloride; hexahydrate. Molecular formula: 219.08. Mole weight: H12CaCl2O6. O.O.O.O.O.O.Cl[Ca]Cl. InChI=1S/Ca.2ClH.6H2O/h; 2*1H; 6*1H2/q+2; /p-2. QHFQAJHNDKBRBO-UHFFFAOYSA-L. 99%+. |  |
| Calcium chloride hexahydrate | Calcium chloride are inorganic compounds with the chemical formula CaCl2(H2O)x, where x = 0, 1, 2, 4, and 6. All of these salts are a highly soluble in water. They are mainly used for deicing and dust control. Because the anhydrous salt is hygroscopic, it is used as a desiccant. Group: Metal & ceramic materials. Alternative Names: Calcium chloride 6-hydrate. CAS No. 7774-34-7. Molecular formula: H12CaCl2O6. Mole weight: 219.08. Appearance: Colorless solid. Purity: 99%+. IUPACName: calcium; dichloride; hexahydrate. Canonical SMILES: O.O.O.O.O.O.Cl[Ca]Cl. Density: 1.71 g/mL at 25 °C (lit.). ECNumber: 233-140-8. Catalog: ACM7774347. | |
| Calcium Chloride Tech Grade | Calcium Chloride tech grade finds extensive use across a range of applications, including ice melting, dust suppression, accelerating concrete setting, acting as a desiccant, and aiding in wastewater treatment. It is a cost-effective chemical with numerous versatile applications. Uses: Concrete Set Time Accelerator, Ice Melt, Dust Control, Wastewater Treatment. Alternative Names: CaCl2, CalChlor, 94-97% Mini Pellets. CAS No. 10043-52-4. Pack Sizes: 50lb. |  USA |
| Calcium sulfate hemihydrate | Calcium sulfate (or calcium sulphate) is the inorganic compound with the formula CaSO4 and related hydrates. In the form of γ-anhydrite (the anhydrous form), it is used as a desiccant. One particular hydrate is better known as plaster of Paris, and another occurs naturally as the mineral gypsum. It has many uses in industry. All forms are White solids that are poorly soluble in water. Calcium sulfate causes permanent hardness in water. Alternative Names: CALCIUM SULFATE CALCINED;CALCINED GYPSUM;Calcium sulfate hemihydrate;CALCIUM SULPHATE 1/2 H2O;CalciumSulphateDriedBp. CAS No. 10034-76-1. Molecular formula: CaH2O5S. Mole weight: 290.3. Appearance: White powder. Purity: 99%+. IUPACName: calcium sulfate hemihydrate. Canonical SMILES: O. [O-]S(=O)(=O)[O-]. [O-]S(=O)(=O)[O-]. [Ca+2]. [Ca+2]. ECNumber: 231-900-3. Catalog: ACM10034761-1. | |
| Calcium Sulphate Anhydrous | White powder, insoluble in water. Uses: desiccant, construction (drywall). Group: sulfate compound. Alternative Names: Anhydrite. CAS No. 7778-18-9. | |
| Dimethylglycine oxidase from Arthrobacter globifomis, Recombinant | Dimethylglycine oxidase (DMGO) is a covalent flavoenzyme from Arthrobacter globiformis that catalyzes the oxidative demethylation of dimethylglycine to yield sarcosine, formaldehyde, and hydrogen peroxide. The N-terminal region binds FAD covalently so it is yellowish. Dimethylglycine oxidase recombinant originated from arthrobacter globifomis fused to his tag at n-terminal produced in e. coli is a single, non-glycosylated, polypeptide chain containing 850 amino acids and having a molecular mass of 92.1 kda. the dmgo is purified by proprietary chromatographic techniques. Group: Enzymes. Synonyms: DMGO; Dimethylglycine Oxidase. CAS No. 74870-79-4. Purity: Greater than 95.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. DMGO. Mole weight: 92.1 kDa. Stability: Dimethylglycine Oxidase Recombinant although stable at 4°C for 30 days, should be stored desiccated below -20°C for periods greater than 30 days. Please prevent freeze-thaw cycles. Appearance: Sterile filtered liquid formulation 1 mg/ml. Source: E. coli. Species: Arthrobacter globifomis. DMGO; Dimethylglycine Oxidase. Cat No: NATE-0826. | |
| Diquat-d4 Dibromide | Contact herbicide used also to produce desiccation and defoliation. Group: Biochemicals. Alternative Names: 6,7-Dihydrodipyrido[1,2-a:2,1-c]pyrazinediium Dibromide Monohydrate; 1,1-Ethylene-2,2-dipyridylium Dibromide Monohydrate; FB/2; Reglone. Grades: Highly Purified. Pack Sizes: 5mg. US Biological Life Sciences. | Worldwide |
| Diquat Dibromide Monohydrate | Contact herbicide used also to produce desiccation and defoliation. Group: Biochemicals. Alternative Names: 6,7-Dihydrodipyrido[1,2-a:2,1-c]pyrazinediium Dibromide Monohydrate; 1,1-Ethylene-2,2-dipyridylium Dibromide Monohydrate; FB/2; Reglone. Grades: Highly Purified. CAS No. 6385-62-2. Pack Sizes: 1g. US Biological Life Sciences. | Worldwide |
| 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. | |
| Drierite®, Indicating (8 mesh) Granules, Laboratory Grade, 454 g | Notes: Blue granules turn pink when wet; contains calcium sulfate, anhydrous, as the desiccant and cobalt chloride as the indicator; to recharge, spread in a 1-granule-deep layer and heat for 1 hour at 210° C (425° F). Storage Code: Blue; toxic. Grades: chem-grade laboratory. Product ID: 858963. -- SOLD FOR EDUCATIONAL USE ONLY -- |  |
| D-(+)-Trehalose | D-(+)-Trehalose (α,α-Trehalose) is an orally active disaccharide, showing anti-desiccant and cryopreservative activities. D-(+)-Trehalose acts as an osmolyte, and stress protectant and helps in the storage and transport of carbon. D-(+)-Trehalose can be used as a food ingredient and pharmaceutical excipient [1] [2] [3] [4]. Uses: Scientific research. Group: Natural products. Alternative Names: D-Trehalose; α,α-Trehalose. CAS No. 99-20-7. Pack Sizes: 10 mM * 1 mL; 100 mg. Product ID: HY-N1132. |  |
| Ethylene glycol | Ethylene glycol is used as a precursor for the syntheses of polymers like polyester fibers, resins and polyethylene terephthalate, which finds application in making plastic bottles. It acts as an intermediate in the synthesis of 1,4-dioxane. It plays an important role in organic synthesis as a protecting group for carbonyl groups. It is a useful desiccant due to its high boiling point and affinity towards water. It plays an important role to remove water vapor from natural gas before proceeding for further processes. Its major application is as a medium for convective heat transfer in automobiles and liquid cooled computers. Group: Solvents. Alternative Names: 1,2-Ethanediol. CAS No. 107-21-1. Molecular formula: C2H6O2. Mole weight: 62.07. IUPACName: ethane-1,2-diol. Canonical SMILES: OCCO. Density: 1.1±0.1 g/cm3. ECNumber: 203-473-3. Catalog: ACM107211. | |
| Exoenzyme C3 from Clostridium botulinum, Recombinant | Exoenzyme C3 transferase is an ADP ribosyl transferase that selectively ribosylates RhoA, RhoB and RhoC proteins on asparagine residue 41, rendering them inactive. It has extremely low affinity for other members of the Rho family such as Cdc42 and Rac1 and does therefore not affect these GTPases. Hence, C3 transferase is a very potent and useful reagent to specifically block RhoA/B/C signaling. Applications: Inhibition of rho activity in vivo by microinjection or pinocyctic uptake into cells. inhibition of rho activity in vitro. Group: Enzymes. Synonyms: Clostridium botulinum Exoenzyme C3; Exoenzyme C3; Exoenzyme C3 transferase; C3 transferase. Purity: >80% by SDS-P...2, 200 mM NaCl, 5% sucrose and 1% dextran. In order to maintain high biological activity of the protein, it is recommended that the protein solution be supplemented with DTT to 1 mM, aliquoted into "experiment sized" amounts, snap frozen in liquid nitrogen and stored at -70°C. The protein is stable for 6 months if stored at -70° C. Storage: The protein should not be exposed to repeated freeze-thaw cycles. The lyophilized protein is stable at 4°C desiccated (<10% humidity) for 1 year. Form: Lyophilized powder. Source: E. coli. Species: Clostridium botulinum. Clostridium botulinum Exoenzyme C3; Exoenzyme C3; Exoenzyme C3 transferase; C3 transferase. Cat No: NATE-0874. | |
| Gefarnate | Gefarnate is a drug used for the treatment of gastritis and gastric ulcer, in vivo, the instillation of gefarnate reduced corneal epithelial damage from desiccation in a dose-dependent fashion. Besides Gefarnate has been proposed for use in the treatment of dry eye syndrome. Synonyms: [(2E)-3,7-dimethylocta-2,6-dienyl] (4E,8E)-5,9,13-trimethyltetradeca-4,8,12-trienoate; Farnesylacetate, Geranyl; Gefarnate; Gefarnil; Gepharnate; Geranyl Farnesylacetate; Ulco. CAS No. 51-77-4. Molecular formula: C27H44O2. Mole weight: 400.64. |  |
| Glucose-6-Phosphate Isomerase from Human, Recombinant | Glucose-6-phosphate isomerase (GPI) is a part of the GPI family whose members encode multifunctional phosphoglucose isomerase proteins involved in energy pathways. GPI is a dimeric enzyme which catalyzes the reversible isomerization of glucose-6-phosphate and fructose-6-phosphate. Mammalian GPI also functions as a tumor-secreted cytokine and an angiogenic factor (AMF) which stimulates endothelial cell motility. In addition, GPI is a neurotrophic factor (Neuroleukin) for spinal and sensory neurons. GPI performs in different capacities inside and outside the cell. In the cytoplasm, GPI is involved in glycolysis and gluconeogenesis, while outside the cell it acts as a...somerase; Autocrine motility factor; Neuroleukin; Sperm antigen 36; GPI; PGI; PHI; AMF; NLK; SA-36; GNPI. Purity: Greater than 95.0% as determined by SDS-PAGE. PGI. Mole weight: 65.3 kDa. Stability: GPI although stable 4°C for 4 weeks, should be stored desiccated 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 colorless solution. Source: E. coli. Species: Human. Glucose-6-phosphate isomerase; Phosphoglucose isomerase; Phosphohexose isomerase; Autocrine motility factor; Neuroleukin; Sperm antigen 36; GPI; PGI; PHI; AMF; NLK; SA-36; GNPI. Cat No: NATE-0841. | |
| Glycerol-3-phosphate oxidase from Pediococcus sp. | In enzymology, a glycerol-3-phosphate oxidase (EC 1.1.3.21) is an enzyme that catalyzes the chemical reaction: sn-glycerol 3-phosphate + O2 ? glycerone phosphate + H2O2. Thus, the two substrates of this enzyme are sn-glycerol 3-phosphate and O2, whereas its two products are glycerone phosphate and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. This enzyme participates in glycerophospholipid metabolism. It employs one cofactor, FAD. Native glycerol-3-phosphate oxidase (ec 1.1.3.21) was purified from streptococcus sp. Group: Enzymes. Synonyms: glycerol-3-phosphate oxidase; EC 1.1.3.21; sn-glycerol-3-phosphate: oxygen 2-oxidoreductase; glycerol phosphat. Enzyme Commission Number: EC 1.1.3.21. CAS No. 9046-28-0. Activity: 40 U/mg-solid or more (containing approx. 60% of stabilizers). Appearance: Yellowish powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Pediococcus sp. glycerol-3-phosphate oxidase; EC 1.1.3.21; sn-glycerol-3-phosphate: oxygen 2-oxidoreductase; glycerol phosphate oxidase; glycerol-1-phosphate oxidase; glycerol phosphate oxidase; L-alpha-glycerophosphate oxidase; alpha-glycerophosphate oxidase; L-alpha-glycerol-3-phosphate oxidase. Cat No: DIA-154. | |
| Glycogen Phosphorylase from Human, Recombinant | Glycogen phosphorylase is one of the phosphorylaseenzymes (EC 2.4.1.1). It breaks up glycogeninto glucosesubunits. Glycogenis left with one less glucosemolecule, and the free glucosemolecule is in the form of glucose-1-phosphate. In order to be used for metabolism, it must be converted to glucose-6-phosphateby the enzyme phosphoglucomutase. Glycogen phosphorylase can only act on linearchainsof glycogen (a 1-4 glycosidic linkage). Its work will immediately come to a halt four residues away from a 1-6 branch (which are exceedingly common in glycogen). In these situations, a debranching enzymeis necessary, which will straighten out the chain in that area. Additionally, an...e; amylopectin phosphorylase; glucan phosphorylase; α-glucan phosphorylase; 1,4-α-glucan phosphorylase; glucosan phosphorylase; granulose phosphorylase; maltodextrin phosphorylase; muscle phosphorylase; myophosphorylase; potato phosphorylase; starch phosphorylase; 1,4-α-D-glucan:phosphate α-D-glucosyltransferase; phosphorylase; EC 2.4.1.1; GPBB. CAS No. 9035-74-9. Purity: Greater than 85.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. GPBB. Stability: GPBB although stable at 10°C for 7 days, should be stored desiccated below -18°C. Please prevent freeze-thaw cycles. Appearance: Sterile Filtered colourless liquid formualtio | |
| Glyoxalase I from Human, Recombinant | Glyoxalase I is universally expressed and involved in the protection against cellular damage due to cytotoxic metabolites such as advanced glycation end products (AGEs). It is an integral component of the detoxification system, catalyzing the conversion of reactive, acyclic a-oxoaldehydes into the corresponding a-hydroxyacids in a glutathione-dependent manner. Group: Enzymes. Synonyms: lactoylglutathione lyase; EC 4.4.1.5; methylglyoxalase; aldoketomutase; ketone-aldehyde mutase; glyoxylase I; (R)-S-lactoylglutathione methylglyoxal-lyase (isomerizing); 9033-12-9. Enzyme Commission Number: EC 4.4.1.5. Purity: > 90% by SDS-PAGE. Glyoxalase I. Mole weight: 20.7 kDa. Activity: >0.4 units/mg. Storage: Glyoxalase-I Human Recombinant although stable at 4 °C for weeks, should be stored desiccated below -18 °C. Please prevent freeze/thaw cycles. Form: Glyoxalase-1 solution containing 20 mM Tris pH-8, 1mM DTT and 10% glycerol. Source: E. coli. Species: Human. lactoylglutathione lyase; EC 4.4.1.5; methylglyoxalase; aldoketomutase; ketone-aldehyde mutase; glyoxylase I; (R)-S-lactoylglutathione methylglyoxal-lyase (isomerizing); 9033-12-9. Cat No: NATE-1651. | |
| Histidyl-tRNA Synthetase from Human, Recombinant | Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene is a cytoplasmic enzyme which belongs to the class II family of aminoacyl-tRNA synthetases. The enzyme is responsible for the synthesis of histidyl-transfer RNA, which is essential for the incorporation of histidine into proteins. The gene is located in a head-to-head orientation with HARSL on chromosome five, where the homologous genes share a bidirectional promoter. The gene product is a frequent target of autoantibodies in the human autoimmune disease polymyositis/dermatomyositis. Histidyl-trna synthetase human recombinant produced in...thetase is purified by proprietary chromatographic techniques. Group: Enzymes. Synonyms: Histidyl-tRNA synthetase; EC 6.1.1.21; Histidine-tRNA ligase; HisRS; HRS; FLJ20491; JO-1. Enzyme Commission Number: EC 6.1.1.21. CAS No. 9068-78-4. Purity: Greater than 90.0% as determined by both (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. HRS. Stability: Histidyl-tRNA Synthetase although stable at 4°C for 3 weeks, should be stored desiccated below -18°C. Please prevent freeze-thaw cycles. Appearance: Sterile Filtered clear solution. Source: E. coli. Species: Human. Histidyl-tRNA synthetase; EC 6.1.1.21; Histidine-tRNA ligase; HisRS; HRS; FLJ20491; JO-1. Cat No: NATE-0848. | |
| Immobilized Lipase-A from Serratia marcescens, Recombinant | Lipase (EC 3.1.1.3) is a ubiquitous enzyme that catalyzes the hydrolysis of fats and oil. The Serratia marcescens lipase is recognized for its excellent enantioselectivity in biocatalytic hydrolysis of trans-3-(4-methoxyphynyl) glycidic acid methyl ester [(±)-MPGM] to produce (2R, 3S)-3-(4-methoxyphenyl) glycidic acid methyl ester [(-)-MPGM], an important intermediate for the synthesis of diltiazem hydrochlorid. Group: Enzymes. Synonyms: Lipase. Enzyme Commission Number: EC 3.1.1.3. CAS No. 9001-62-1. Purity: >90%. Lipase. Mole weight: 65 kDa. Stability: Lipase-A although stable at room temp for 1 week, should be stored desiccated 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. Form: Sterile Filtered lyophilized powder. Source: E. Coli. Species: Serratia marcescens. Lipase; Lipase-A; Lipase A; EC 3.1.1.3; Immobilized Lipase-A. Cat No: NATE-1621. | |
| Kallikrein-1 from Human, Recombinant | Kallikreins are serine protease enzymes having various physiological functions. Kallikreins are implicated in carcinogenesis and have potenital as novel cancer disease biomarkers. KLK1 is one of the fifteen kallikrein subfamily members located in a cluster on chromosome 19. KLK1 is functionally conserved in its ability to release the vasoactive peptide, Lys-bradykinin, from low molecular weight kininogen. Human Kallikrein-1, also called as Kallidinogenase, Kininogenase or Kininogenin, is an active protein enzyme present in saliva, pancreatic juices, and urine that catalyzes the proteolysis of bradykininogen to bradykinin. Kallikrein-1, which derived from human or porcine, h...ysis by RP-HPLC. (b) Analysis by SDS-PAGE. Kallikrein. Mole weight: 28-32 kDa. Activity: 5 Units/mg. Stability: Lyophilized KLK1although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution KLK1 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 powder. Source: Pichia Pastoris. Species: Human. KLK1; KLK-1; HK1; HK-1; KLKR; KLK6; Tissue Kallikrein; Hklk1; EC 3.4.21.35; Kidney/pancreas/salivary gland kallikrein; Kallikrein-1. Cat No: NATE-0851. | |
| KBP-Type Peptidyl-Prolyl Cis-Trans Isomerase, Recombinant | SlyD is a putative folding helper protein from the Escherichia coli cytosol, which has N-terminal prolyl isomerase domain of the FKBP type and a most likely unstructured C-terminal tail. SlyD is an important factor in the biosynthesis of the metal cluster in the [NiFe]-hydrogenase enzymes, and exhibits several activities including that of a peptidyl-prolyl isomerase. Slyd recombinant produced in e. coli is a single, non-glycosylated polypeptide chain containing 196 amino acids and having a molecular mass of 21 kda. Group: Enzymes. Synonyms: FKBP-Type Peptidyl-Prolyl Cis-Trans Isomerase; SlyD. Purity: Greater than 95.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. SlyD. Mole weight: 21 kDa. Activity: > 66 nmoles/min/ug. Stability: SlyD although stable 4°C for 4 weeks, should be stored desiccated 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 colorless solution. Source: E. coli. FKBP-Type Peptidyl-Prolyl Cis-Trans Isomerase; SlyD. Cat No: NATE-0852. | |
| Magnesium Sulphate Dried | White powder. Uses: desiccant, fertilizer. Group: sulfate salt. CAS No. 22189-08-8. | |
| Matrix Metalloproteinase-8 from Human, Recombinant | Full-length recombinant human neutrophil pro-collagenase (MMP-8), latent form. Matrix metalloproteinase 8 (MMP-8), or neutrophil collagenase, degrades interstitial collagens, acting preferentially on collagen type I. Increased full-length MMP-8 protein was associated with infiltration into the skin of neutrophils, which are the major cell type that expresses MMP-8. MMP-8 is synthesized and stored in specific granules in neutrophil leukocytes. MMP-8 activity is therefore regulated by factors such as surface-bound ligands (IgG or complement components) that release it through degranulation.Once released and activated through proteolytic or oxidative mechanisms, MMP-8 p...ollagenase activity. Group: Enzymes. Synonyms: Neutrophil collagenase; EC 3.4.24.34; Matrix metalloproteinase-8; MMP-8; PMNL collagenase; PMNL-CL; HNC; CLG1. Enzyme Commission Number: EC 3.4.24.34. CAS No. 9001-12-1. Purity: Greater than 90% as determined by SDS-PAGE. Matrix Metalloproteinase. Mole weight: 75 kDa. Activity: 100 units/ml. Stability: MMP-8 although stable at 4°C for 1 week, should be stored desiccated below -18°C. Please prevent freeze-thaw cycles. Appearance: Sterile Filtered clear solution. Source: E. coli. Species: Human. Neutrophil collagenase; EC 3.4.24.34; Matrix metalloproteinase-8; MMP-8; PMNL collagenase; PMNL-CL; HNC; CLG1. Cat No: NATE-0862. | |
| Native Acremonium sp. Ascorbate Oxidase | In enzymology, a L-ascorbate oxidase (EC 1.10.3.3) is an enzyme that catalyzes the chemical reaction:2 L-ascorbate + O2<-> 2 dehydroascorbate + 2 H2O. Thus, the two substRates of this enzyme are L-ascorbate and O2, whereas its two products are dehydroascorbate and H2O. This enzyme belongs to the family of oxidoreductases, specifically those acting on diphenols and related substances as donor with oxygen as acceptor. This enzyme participates in ascorbate metabolism. It employs one cofactor, copper. Applications: This enzyme is useful for avoidance from interference of ascorbic acid on diagnostic assay such as blood, uric acid, tg, tc and creatinine. Group: Enzymes. Synonyms: ascorbase; ascorbic acid oxidase; ascorbate oxidase; ascorbic oxidase; ascorbate dehydrogenase; L-ascorbic acid oxidase; AAO; L-ascorbate:O2 oxidoreductase;. Enzyme Commission Number: EC 1.10.3.3. CAS No. 9029-44-1. AAO. Mole weight: 80 kDa?gel filtration?. Activity: > 200 U/mg. Appearance: Light blue amorphous powder, lyophilized. Storage: Storage at ?20°C in the presence of a desiccant is recommended. Form: Freeze dried powder. Source: Acremonium sp. ascorbase; ascorbic acid oxidase; ascorbate oxidase; ascorbic oxidase; ascorbate dehydrogenase; L-ascorbic acid oxidase; AAO; L-ascorbate:O2 oxidoreductase; AA oxidase; EC 1.10.3.3; L-ascorbate oxidase. Cat No: NATE-0864. | |
| Native Aerococcuss viridans Lactate Oxidase | Native Aerococcuss viridans Lactate Oxidase. Native lactate oxidase (ec 1.13.12.4) was purified from aerococcuss viridans. Group: Enzymes. Synonyms: lactate 2-monooxygenase; EC 1.13.12.4; (S)-lactate: oxygen 2-oxidoreductase (decarboxylating); lactate oxidative decarboxylase; lactate oxidase; lactic oxygenase; lactate oxygenase; lactic oxidase; L-lactate monooxygenase; lactate monooxygenase; L-lactate-2-monooxygenase. Enzyme Commission Number: EC 1.13.12.4. CAS No. 9028-72-2. Lactate oxidase. Activity: > 20 U/mg. Appearance: Yellowish powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Aerococcuss viridans. lactate 2-monooxygenase; EC 1.13.12.4; (S)-lactate: oxygen 2-oxidoreductase (decarboxylating); lactate oxidative decarboxylase; lactate oxidase; lactic oxygenase; lactate oxygenase; lactic oxidase; L-lactate monooxygenase; lactate monooxygenase; L-lactate-2-monooxygenase. Cat No: DIA-156. | |
| Native Aerococcuss viridans Pyruvate oxidase | In enzymology, a pyruvate oxidase (EC 1.2.3.3) is an enzyme that catalyzes the chemical reaction: pyruvate + phosphate + O2 <-> acetyl phosphate + CO2 + H2O2. The 3 substrates of this enzyme are pyruvate, phosphate, and O2, whereas its 3 products are acetyl phosphate, CO2, and H2O2. Native pyruvate oxidase (ec 1.2.3.3) was purified from aerococcuss viridans. Applications: Useful for enzymatic determination of ast and alt. Group: Enzymes. Synonyms: pyruvate oxidase; EC 1.2.3.3; pyruvate: oxygen 2-oxidoreductase (phosphorylating); pyruvic oxidase; phosphate-dependent pyruvate oxidase. Enzyme Commission Number: EC 1.2.3.3. CAS No. 9001-96-1. Pyruvate oxidase. Activity: > 25 U/mg. Appearance: Yellowish powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Aerococcuss viridans. pyruvate oxidase; EC 1.2.3.3; pyruvate: oxygen 2-oxidoreductase (phosphorylating); pyruvic oxidase; phosphate-dependent pyruvate oxidase. Cat No: DIA-169. | |
| Native Arthrobacter globiformis Choline oxidase | In enzymology, a choline oxidase (EC 1.1.3.17) is an enzyme that catalyzes the chemical reaction choline + O2<-> betaine aldehyde + H2O2. Thus, the two substrates of this enzyme are choline and O2, whereas its two products are betaine aldehyde and H2O2. Native choline oxidase (ec 1.1.3.17) was purified from arthrobacter globiformis. Group: Enzymes. Synonyms: choline oxidase; EC 1.1.3.17; choline: oxygen 1-oxidoreductase. Enzyme Commission Number: EC 1.1.3.17. CAS No. 9028-67-5. Choline Oxidase. Activity: 8-20 U/mg. Appearance: Yellow amorphous powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Arthrobacter globiformis. choline oxidase; EC 1.1.3.17; choline: oxygen 1-oxidoreductase. Cat No: DIA-139. | |
| Native Arthrobacter sp. acyl-CoA oxidase | In enzymology, an acyl-CoA oxidase (EC 1.3.3.6) is an enzyme that catalyzes the chemical reaction acyl-CoA + O2<-> trans-2, 3-dehydroacyl-CoA + H2O2. Thus, the two substrates of this enzyme are acyl-CoA and O2, whereas its two products are trans-2, 3-dehydroacyl-CoA and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with oxygen as acceptor. This enzyme participates in 3 metabolic pathways: fatty acid metabolism, polyunsaturated fatty acid biosynthesis, and ppar signaling pathway. It employs one cofactor, FAD. Native acyl-coa oxidase (ec 1.3.3.6) was purified from arthrobacter sp. Group: Enzymes. Synonyms: acyl-CoA oxidase; EC 1.3.3.6; fatty acyl-CoA oxidase; acyl coenzyme A oxidase; and fatty acyl-coenzyme A oxidase. Enzyme Commission Number: EC 1.3.3.6. CAS No. 61116-22-1. Acyl-CoA oxidase. Activity: > 20 U/mg. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Yellowish Freeze dried powder. Source: Arthrobacter sp. acyl-CoA oxidase; EC 1.3.3.6; fatty acyl-CoA oxidase; acyl coenzyme A oxidase; and fatty acyl-coenzyme A oxidase. Cat No: DIA-121. | |
| Native Arthrobacter sp. Tyramine Oxidase | Amine oxidases (AO) are enzymes that catalyze the oxidation of a wide range of biogenic amines including many neurotransmitters, histamine and xenobiotic amines. There are two classes of amine oxidases: flavin-containing (EC 1.4.3.4) and copper-containing (EC 1.4.3.6). Copper-containing AO act as a disulphide-linked homodimer. They catalyse the oxidation of primary amines to aldehydes, with the subsequent release of ammonia and hydrogen peroxide, which requires one copper ion per subunit and topaquinone as cofactor: RCH2NH2 + H2O + O2 <-> RCHO + NH3 + H2O2. The 3 substrates of this enzyme are primary amines (RCH2NH2), H2O, and O2, whereas its 3 products are RCHO, NH3, and H2O2. Native tyramine oxidase (ec 1.4.3.4) was purified from arthrobacter sp. Applications: Useful for enzymatic determiantion of leucine aminopeptidase. Group: Enzymes. Synonyms: Tyramine Oxidase; TOD; EC 1.4.3.6. Enzyme Commission Number: EC 1.4.3.6. CAS No. 9001-53-0. Tyramine Oxidase. Activity: > 3 U/mg. Appearance: White to light brown powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Arthrobacter sp. Tyramine Oxidase; TOD; EC 1.4.3.6. Cat No: DIA-158. | |
| Native Bacillus cereus Phospholipase C | Phospholipase C is an enzyme with system name phosphatidylcholine cholinephosphohydrolase. This enzyme catalyses the following chemical reaction: a phosphatidylcholine + H2O<-> 1, 2-diacyl-sn-glycerol + phosphocholine. The bacterial enzyme is a zinc protein. It also acts on sphingomyelin and phosphatidylinositol. Native phospholipase c (ec 3.1.4.3) was purified from bacillus cereus. Applications: Useful for enzymatic determination of lecithin. Group: Enzymes. Synonyms: Phospholipase C; EC 3.1.4.3; lipophosphodiesterase I; Clostridium welchii alpha-toxin; Clostridium oedematiens beta-and gamma-toxins; lipophosphodiesterase C; phosphatidase C; heat-labile hemolysin; alpha-toxin. Enzyme Commission Number: EC 3.1.4.3. CAS No. 9001-86-9. Phospholipase C. Activity: > 30 U/mg. Appearance: White to brownish powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Bacillus cereus. Phospholipase C; EC 3.1.4.3; lipophosphodiesterase I; Clostridium welchii alpha-toxin; Clostridium oedematiens beta-and gamma-toxins; lipophosphodiesterase C; phosphatidase C; heat-labile hemolysin; alpha-toxin. Cat No: DIA-163. | |
| Native Bacillus megaterium Diaphorase (NADH) | In enzymology, a NADPH dehydrogenase is an enzyme that catalyzes In enzymology, a NAD (P)H dehydrogenase (quinone) (EC 1.6.5.2) is an enzyme that catalyzes the chemical reaction NAD (P)H + H+ + a quinone<-> NAD (P)+ + a hydroquinone. The 4 substrates of this enzyme are NADH, NADPH, H+, and quinone, whereas its 3 products are NAD+, NADP+, and hydroquinone. Native diaphorase (ec 1.6.5.2) was purified from bacillus megaterium. Applications: Useful for enzymatic determination of reduced nad. Group: Enzymes. Synonyms: EC 1.6.99.3; cytochrome c reductase; type 1 dehydrogenase; beta-NADH dehydrogenase dinucleotide; diaphorase; dihydrocodehydr. Enzyme Commission Number: EC 1.6.99.3. CAS No. 9079-67-8. Diaphorase. Activity: 30-60 U/mg. Appearance: Yellow dried powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Bacillus megaterium. EC 1.6.99.3; cytochrome c reductase; type 1 dehydrogenase; beta-NADH dehydrogenase dinucleotide; diaphorase; dihydrocodehydrogenase I dehydrogenase; dihydronicotinamide adenine dinucleotide dehydrogenase; diphosphopyridine diaphorase; DPNH diaphorase; NADH diaphorase; NADH hydrogenase; NADH oxidoreductase; NADH-menadione oxidoreductase; reduced diphosphopyridine nucleotide diaphorase; Beta-NADH dehydrogenase dinucleotide. Cat No: DIA-142. | |
| Native Bacillus sp. Glucose-6-phosphate dehydrogenase | Glucose-6-phosphate dehydrogenase (G6PD or G6PDH) (EC 1.1.1.49) is a cytosolic enzyme that catalyzes the chemical reaction:D-glucose 6-phosphate + NADP+ <-> 6-phospho-D-glucono-1,5-lactone + NADPH + H+. This enzyme is in the pentose phosphate pathway, a metabolic pathway that supplies reducing energy to cells (such as erythrocytes) by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH). Native glucose-6-phosphate dehydrogenase (ec 1.1.1.49) was purified from bacillus sp. Applications: Useful for enzymatic determination of glucose or atp when coupled with hexokinase. Group: Enzymes. Synonyms: Glucose-6-phosphate dehydrogenase; G6PD; G6PDH; Glucose-6-phosphate dehydrogenase (NADP(+)); EC 1.1.1.49; Glucose-6-phosphate 1-dehydrogenase; Glucose-6-phosph. Enzyme Commission Number: EC 1.1.1.49. CAS No. 9001-40-5. Glucose-6-phosphate dehydrogenase. Mole weight: 104 kDa dalton (two subunits of approx. 55 kDa). Activity: > 200 U/mg. Appearance: White/off white powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Bacillus sp. Glucose-6-phosphate dehydrogenase; G6PD; G6PDH; Glucose-6-phosphate dehydrogenase (NADP(+)); EC 1.1.1.49; Glucose-6-phosphate 1-dehydrogenase; Glucose-6-phosphate dehydrogenase; GPD. Cat No: DIA-143. | |
| Native Bacillus sp. Glutamine synthetase | Glutamine synthetase (GS) (EC 6.3.1.2) is an enzyme that plays an essential role in the metabolism of nitrogen by catalyzing the condensation of glutamate and ammonia to form glutamine: Glutamate + ATP + NH3 ? Glutamine + ADP + phosphate. Glutamine Synthetase uses ammonia produced by nitrate reduction, amino acid degradation, and photorespiration. The amide group of glutamate is a nitrogen source for the synthesis of glutamine pathway metabolites. Native glutamine synthetase (ec 6.3.1.2) was purified from bacillus sp. Applications: Useful for the determination of ammonia and atp in clinical analysis. Group: Enzymes. Synonyms: Glutamine synthetase; GS; EC 6.3.1.2; Glutamate-ammonia ligase. Enzyme Commission Number: EC 6.3.1.2. CAS No. 9023-70-5. GS. Activity: > 15 U/mg. Appearance: White to pale brown powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Bacillus sp. Glutamine synthetase; GS; EC 6.3.1.2; Glutamate-ammonia ligase. Cat No: DIA-155. | |
| Native Bacillus sp. Hexokinase | A hexokinase is an enzyme that phosphorylates hexoses (six-carbon sugars), forming hexose phosphate. In most organisms, glucose is the most important substrate of hexokinases, and glucose-6-phosphate the most important product. Hexokinase can transfer an inorganic phosphate group from ATP to a substrate. Hexokinases should not be confused with glucokinase, which is a specific isoform of hexokinase. While other hexokinases are capable of phosphorylating several hexoses, glucokinase acts with a 50-fold lower substrate affinity and its only hexose substrate is glucose. Applications: This enzyme is useful for enzymatic determination of glucose or creatinine kinase activity when coupled with glucose-6-phosphate dehydrogenase. Group: Enzymes. Synonyms: hexokinase (phosphorylating); ATP-dependent hexokinase; glucose ATP phosphotransferase; hexokinase; ATP:D-hexose 6-phosphotransferase. Enzyme Commission Number: EC 2.7.1.1. CAS No. 9001-51-8. Hexokinase. Mole weight: 68 kDa (gel filtration). Activity: More than 250 U/mg solid. Appearance: White amorphous powder, lyophilized. Storage: Storage at -20°C in the presence of a desiccant is recommended. Form: Freeze dried powder. Source: Bacillus sp. hexokinase (phosphorylating); ATP-dependent hexokinase; glucose ATP phosphotransferase; hexokinase; ATP:D-hexose 6-phosphotransferase; EC 2.7.1.1. Cat No: NATE-1157. | |
| Native Bacillus sp. Monoglyceride Lipase | In enzymology, an acylglycerol lipase (EC 3.1.1.23) is an enzyme that catalyzes a chemical reaction that uses water molecules to break the glycerol monoesters of long-chain fatty acids. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. This enzyme participates in glycerolipid metabolism. Is an enzyme produced by microorganisms. this product shall be used for a diagnostics reagent. Applications: Useful for enzymatic determiantion of triglyceride. Group: Enzymes. Synonyms: EC 3.1.1.23; acylglycerol lipase; glycerol-ester acylhydrolase; monoacylglycerol lipase; monoacylglycerolipase; monoglyceride lipase; monoglyceride hydrolase; fatty acyl monoester lipase; monoacylglycerol hydrolase; monoglyceridyllipase; monoglyceridase. Enzyme Commission Number: EC 3.1.1.23. CAS No. 9040-75-9. Monoglyceride lipase. Mole weight: 20 kDa (gel filtration). Activity: > 20 U/mg. Appearance: White powder. Storage: Storage at-20°C in the presence of a desiccant is recommended. Form: Freeze dried powder. Source: Bacillus sp. EC 3.1.1.23; acylglycerol lipase; glycerol-ester acylhydrolase; monoacylglycerol lipase; monoacylglycerolipase; monoglyceride lipase; monoglyceride hydrolase; fatty acyl monoester lipase; monoacylglycerol hydrolase; monoglyceridyllipase; monoglyceridase. Cat No: NATE-0455. | |
| Native Bacillus stearothermophilius NAD Synthetase | In enzymology, a NAD+ synthase (EC 6.3.1.5) is an enzyme that catalyzes the chemical reaction:ATP + deamido-NAD+ + NH3<-> AMP + diphosphate + NAD+. The 3 substrates of this enzyme are ATP, deamido-NAD+, and NH3, whereas its 3 products are AMP, diphosphate, and NAD+. This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ligases (amide synthases). This enzyme participates in nicotinate and nicotinamide metabolism and nitrogen metabolism. Is an enzyme produced by microorganisms. this product shall be used for a diagnostics reagent. Applications: Useful for enzymatic determination of atp, ammonia, urea or creatinine. it is also suitable for enzymatic cycling method. Group: Enzymes. Synonyms: EC 6.3.1.5; 9032-69-3; NAD+ synthetase; NAD+ synthase; nicotinamide adenine dinucleotide synthetase; diphosp. Enzyme Commission Number: EC 6.3.1.5. CAS No. 9032-69-3. NAD Synthetase. Mole weight: 50 kDa (gel filtration); 25 kDa (SDS-PAGE). Activity: > 1 U/mg. Appearance: White powder. Storage: Storage at-20°C in the presence of a desiccant is recommended. Form: Freeze dried powder. Source: Bacillus stearothermophilius. EC 6.3.1.5; 9032-69-3; NAD+ synthetase; NAD+ synthase; nicotinamide adenine dinucleotide synthetase; diphosphopyridine nucleotide synthetase. Cat No: NATE-0471. | |
| Native Bacillus stearothermophilus Phosphofructokinase | Phosphofructokinase is a kinase enzyme that phosphorylates fructose 6-phosphate in glycolysis. The enzyme-catalysed transfer of a phosphoryl group from ATP is an important reaction in a wide variety of biological processes. One enzyme that utilizes this reaction is phosphofructokinase (PFK), which catalyses the phosphorylation of fructose-6-phosphate to fructose-1,6-bisphosphate, a key regulatory step in the glycolytic pathway. PFK exists as a homotetramer in bacteria and mammals (where each monomer possesses 2 similar domains) and as an octomer in yeast (where there are 4 alpha-(PFK1) and 4 beta-chains (PFK2), the latter, like the mammalian monomers, possessing 2 ...cs reagent. Applications: Useful for enzymatic determiantion of fructose-6-phosphate. Group: Enzymes. Synonyms: PFKWII; EC 2.7.1.11; PFK; phosphofructokinase; 6-phosphofructokinase; Phosphofructokinase I; Phosphohexokinase. Enzyme Commission Number: EC 2.7.1.11. CAS No. 9001-80-3. PFK. Mole weight: 72 kDa (gel filtration); 35 kDa (SDS-PAGE). Activity: > 250 U/mg. Appearance: White to pale yellow powder. Storage: Storage at-20°C in the presence of a desiccant is recommended. Form: Freeze dried powder. Source: Bacillus stearothermophilus. PFKWII; EC 2.7.1.11; PFK; phosphofructokinase; 6-phosphofructokinase; Phosphofructokinase I; Phosphohexokinase. Cat No: NATE-0551. | |
| Native Bacillus stearothermophilus Phosphoglucose isomerase | Glucose-6-phosphate isomerase is an enzyme that catalyzes the conversion of glucose-6-phosphate into fructose 6-phosphate in the second step of glycolysis. The human variant of this enzyme is encoded by the GPI gene. Native glucose-6-phosphate isomerase (ec 5.3.1.9) was purified from bacillus stearothermophilus. Group: Enzymes. Synonyms: Glucose-6-phosphate isomerase; phosphoglucose isomerase; phosphohexose isomerase; EC 5.3.1.9; phosphohexomutase; oxoisomerase; hexosephosphate isomerase; phosphosaccharomutase; phosphoglucoisomerase; phosphohexoisomerase; glucose phosphate isomerase; hexose phosphate isomerase; D-glucose-6-phosphate ketol-isomerase. Enzyme Commission Number: EC 5.3.1.9. CAS No. 9001-41-6. PGI. Activity: > 250 U/mg. Appearance: White powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Bacillus stearothermophilus. Glucose-6-phosphate isomerase; phosphoglucose isomerase; phosphohexose isomerase; EC 5.3.1.9; phosphohexomutase; oxoisomerase; hexosephosphate isomerase; phosphosaccharomutase; phosphoglucoisomerase; phosphohexoisomerase; glucose phosphate isomerase; hexose phosphate isomerase; D-glucose-6-phosphate ketol-isomerase. Cat No: DIA-162. | |
| Native Bacillus subtilis Bilirubin oxidase | In enzymology, a bilirubin oxidase (EC 1.3.3.5) is an enzyme that catalyzes the chemical reaction 2 bilirubin + O2<-> 2 biliverdin + 2 H2O. Thus, the two substrates of this enzyme are bilirubin and O2, whereas its two products are biliverdin and H2O. This enzyme belongs to the family of oxidoreductases, to be specific those acting on the CH-CH group of donor with oxygen as acceptor. This enzyme participates in porphyrin and chlorophyll metabolism. Native bilirubin oxidase (ec 1.3.3.5) was purified from bacillus subtilis. Applications: Useful for enzymatic determination of bilirubin and for eliminating the interference of bilirubin in diagnostic assays. Group: Enzymes. Synonyms: bilirubin oxidase M-1; bilirubin oxidase; EC 1.3.3.5; bilirubin: oxygen oxidoreductase. Enzyme Commission Number: EC 1.3.3.5. CAS No. 80619-01-8. Bilirubin Oxidase. Activity: > 1.2 U/mg. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Bacillus subtilis. bilirubin oxidase M-1; bilirubin oxidase; EC 1.3.3.5; bilirubin: oxygen oxidoreductase. Cat No: DIA-129. | |
| Native Bovine Protein Kinase A | 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. Group: Enzymes. Synonyms: Protein kinase A; PKA; Protein Kinase; 3',5'-cyclic-AMP-dependent Protein Kinase. Enzyme Commission Number: EC 2.7.11.11. CAS No. 9026-43-1. PKAC. Activity: >0.4 units/μg protein. Storage: Store the product at -20 °C. The dry solid is shipped at ambient temperature with minimal loss in activity. When stored at -20 °C with desiccant, the protein will lose <10% activity per year. Form: Lyophilized from a solution containing: 5-10% potassium phosphate buffer, pH 7.5, 5-10% EDTA, and 80-90% protein (biuret assay). Source: Bovine heart. Species: Bovine. Protein kinase A; PKA; Protein Kinase; 3',5'-cyclic-AMP-dependent Protein Kinase. Cat No: NATE-1944. | |
| Native Candida sp. Alcohol oxidase | In enzymology, an alcohol oxidase (EC 1.1.3.13) is an enzyme that catalyzes the chemical reaction a primary alcohol + O2 <-> an aldehyde + H2O2. Thus, the two substrates of this enzyme are primary alcohol and O2, whereas its two products are aldehyde and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. Native alcohol oxidase (ec 1.1.3.13) was purified from candida sp. Applications: Useful for enzymatic determination of blood alcohol. Group: Enzymes. Synonyms: ethanol oxidase; alcohol oxidase; EC 1.1.3.13; Methanol oxidase; 9073-63-6. Enzyme Commission Number: EC 1.1.3.13. CAS No. 9073-63-6. Alcohol Oxidase. Activity: 7~20 U/mg. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Light yellow powder. Source: Candida sp. ethanol oxidase; alcohol oxidase; EC 1.1.3.13; Methanol oxidase; 9073-63-6. Cat No: DIA-123. | |
| Native Cucurbita sp. L-ascorbate oxidase | In enzymology, a L-ascorbate oxidase (EC 1.10.3.3) is an enzyme that catalyzes the chemical reaction2 L-ascorbate + O2 ? 2 dehydroascorbate + 2 H2O. Thus, the two substrates of this enzyme are L-ascorbate and O2, whereas its two products are dehydroascorbate and H2O. Native l-ascorbate oxidase (ec 1.10.3.3) was purified from acremonium sp. Applications: This enzyme is useful for enzymatic determination of ascorbic acid and for eliminating the interference of ascorbic acid in clinical analysis. Group: Enzymes. Synonyms: ascorbase; ascorbic acid oxidase; ascorbate oxidase; ascorbic oxidase; ascorbate dehydrogenase; L-ascorbic acid oxidase; AAO; L-ascorbate: O2 oxidoreductase; AA oxidase; EC 1.10.3.3; 9029-44-1; L-ascorbate oxidase. Enzyme Commission Number: EC 1.10.3.3. CAS No. 9029-44-1. Activity: 200U/mg. Appearance: Light blue amorphous powder, lyophilized. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Light blue lyophilized powder. Source: Cucurbita sp. ascorbase; ascorbic acid oxidase; ascorbate oxidase; ascorbic oxidase; ascorbate dehydrogenase; L-ascorbic acid oxidase; AAO; L-ascorbate: O2 oxidoreductase; AA oxidase; EC 1.10.3.3; 9029-44-1; L-ascorbate oxidase. Cat No: DIA-124. | |
| Native E. coli 1-5-Anhydroglucitol-6-Phosphate Dehydrogenase | Native E. coli 1-5-Anhydroglucitol-6-Phosphate Dehydrogenase. Ag6pdhii is an enzyme produced by microorganisms. this product shall be used for a diagnostics reagent. Applications: Useful for enzymatic determination of 1,5-ag. Group: Enzymes. Synonyms: AG6PDHII; EC 1.1.1.140; 1-5-Anhydroglucitol-6-Phosphate Dehydrogenase. Enzyme Commission Number: EC 1.1.1.140. CAS No. 37250-69-4. AG6PDHII. Mole weight: 78 kDa (TSK gel G 3000 SWXL gel filtration); 40 kDa (SDS-PAGE). Activity: > 20 U/mg. Stability: Stable for 1 years under the freezing condition (-80°C). Appearance: White powder. Storage: Storage at-80°C in the presence of a desiccant is recommended. Form: Freeze dried powder. Source: Escherichia coli. AG6PDHII; EC 1.1.1.140; 1-5-Anhydroglucitol-6-Phosphate Dehydrogenase. Cat No: NATE-0039. | |
| Native Flavobacterium meningosepticum Glycerol kinase | The activity of glycerol kinase is found widely in nature. In microorganisms GK makes possible the utilization of glycerol as a carbon source. In mammals the enzyme represents a juncture of sugar and fat metabolism; The enzyme is important to the clinical chemist in the determination of glycerol. GK is also useful in the assay of glyceraldehydes and dihydroxyacetone following their quantitative reduction to glycerol with sodium borohydride. Applications: Useful for the measurement of triglyceride. Group: Enzymes. Synonyms: glycerokinase; GK; ATP: glycerol-3-phosphotransferase; glycerol kinase phosphorylating; glyceric kinase; EC 2.7.1.30. Enzyme Commission Number: EC 2.7.1.30. GK. Mole weight: 150 kDa (TSK G3000SWXL) 50 kDa (SDS-PAGE). Activity: More than 70 U/mg solid. Appearance: White to light grayish white amorphous powder, lyophilized. Storage: Storage at -20°C in the presence of a desiccant is recommended. Form: Freeze dried powder. Source: Flavobacterium meningosepticum. glycerokinase; GK; ATP: glycerol-3-phosphotransferase; glycerol kinase phosphorylating; glyceric kinase; EC 2.7.1.30. Cat No: NATE-1155. | |
| Native Gliocladium roseum Glycerophosphocholine phosphodiesterase | In enzymology, a glycerophosphocholine phosphodiesterase (EC 3.1.4.2) is an enzyme that catalyzes the chemical reaction: sn-glycero-3-phosphocholine + H2O<-> choline + sn-glycerol 3-phosphate. Thus, the two substrates of this enzyme are sn-glycero-3-phosphocholine and H2O, whereas its two products are choline and sn-glycerol 3-phosphate. Native glycerophosphocholine phosphodiesterase (ec 3.1.4.2) was purified from gliocladium roseum. Group: Enzymes. Synonyms: glycerophosphocholine phosphodiesterase; EC 3.1.4.2; sn-glycero-3-phosphocholine glycerophosphohydrolase; glycerophosphinicocholine diesterase; glycerylphosphorylcholinediesterase; sn-glycero-3-phosphorylcholine diesterase; glycerolphosphorylcholine phospho. Enzyme Commission Number: EC 3.1.4.2. CAS No. 9025-85-8. Glycerophosphocholine phosphodiesterase. Activity: > 10.0 U/mg. Appearance: White to brownish powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Gliocladium roseum. glycerophosphocholine phosphodiesterase; EC 3.1.4.2; sn-glycero-3-phosphocholine glycerophosphohydrolase; glycerophosphinicocholine diesterase; glycerylphosphorylcholinediesterase; sn-glycero-3-phosphorylcholine diesterase; glycerolphosphorylcholine phosphodiesterase; glycerophosphohydrolase. Cat No: DIA-153. | |
| Native Hexokinase (ADP-Dependent) from Pyrococcus furiosus | In enzymology, a ADP-Dependent Hexokinase (EC 2.7.1.147) is an enzyme that catalyzes the chemical reaction: D-Glucose + ADP ? D-Glucose-6-phosphate + AMP. Applications: Useful for the enzymatic determination of adp. Group: Enzymes. Synonyms: ADP-dependent glucokinase; ADP-specific glucokinase; ADP:D-glucose 6-phosphotransferase; EC 2.7.1.147. Enzyme Commission Number: EC 2.7.1.147. CAS No. 173585-07-4. Hexokinase (ADP-Dependent). Mole weight: 100 kDa (gel filtration) 51 kDa (SDS-PAGE). Activity: More than 30 U/mg solid. Appearance: White amorphous powder, lyophilized. Storage: Storage at ?20°C in the presence of a desiccant is recommended. Source: Pyrococcus furiosus. ADP-dependent glucokinase; ADP-specific glucokinase; ADP:D-glucose 6-phosphotransferase; EC 2.7.1.147. Cat No: NATE-1135. | |
| Native Hexokinase (ADP-Dependent) from Thermococcus litoralis | In enzymology, a ADP-Dependent Hexokinase (EC 2.7.1.147) is an enzyme that catalyzes the chemical reaction: D-Glucose + ADP ? D-Glucose-6-phosphate + AMP. Applications: Useful for the enzymatic determination of 1,5 anhydroglucitol. Group: Enzymes. Synonyms: ADP-dependent glucokinase; ADP-specific glucokinase; ADP:D-glucose 6-phosphotransferase; EC 2.7.1.147. Enzyme Commission Number: EC 2.7.1.147. CAS No. 173585-07-4. Hexokinase (ADP-Dependent). Mole weight: 50 kDa (gel filtration) 50 kDa (SDS-PAGE). Activity: More than 25 U/mg solid. Appearance: White amorphous powder, lyophilized. Storage: Storage at ?20°C in the presence of a desiccant is recommended. Source: Thermococcus litoralis. ADP-dependent glucokinase; ADP-specific glucokinase; ADP:D-glucose 6-phosphotransferase; EC 2.7.1.147. Cat No: NATE-1136. | |
| Native Microorganism Glucose Dehydrogenase (FAD-dependent) | FAD-GDH catalyses the oxidation of glucose in the presence of an electron acceptor, such as 2,6-dichlorophenolindophenol or potassium ferricyanide. Applications: Blood glucose monitoring (biosensors) biosensors. Group: Enzymes. Synonyms: D-glucose:acceptor 1-oxidoreductase; glucose dehydrogenase (Aspergillus); glucose dehydrogenase (decarboxylating); D-glucose: (acceptor) 1-oxidoreductase; Glucose Dehydrogenase (FAD-dependent); FAD-GDH; EC 1.1.99.10; 9035-82-9. Enzyme Commission Number: EC 1.1.99.10. CAS No. 9035-82-9. Activity: ≥ 800U/mg protein. Storage: Store desiccated at-15°C or below. Allow to come to room temperature before opening. Before returning to storage, re-desiccate under vacuum over silica gel for a minimum of four hours. Form: A yellow freeze dried material. Source: Microorganism. D-glucose:acceptor 1-oxidoreductase; glucose dehydrogenase (Aspergillus); glucose dehydrogenase (decarboxylating); D-glucose: (acceptor) 1-oxidoreductase; Glucose Dehydrogenase (FAD-dependent); FAD-GDH; EC 1.1.99.10; 9035-82-9. Cat No: NATE-0251. | |
| Native Pediococcus sp. Glycerol-3-phosphate oxidase | In enzymology, a glycerol-3-phosphate oxidase (EC 1.1.3.21) is an enzyme that catalyzes the chemical reaction: sn-glycerol 3-phosphate + O2<-> glycerone phosphate + H2O2. Thus, the two substrates of this enzyme are sn-glycerol 3-phosphate and O2, whereas its two products are glycerone phosphate and H2O2. Native glycerol-3-phosphate oxidase (ec 1.1.3.21) was purified from streptococcus sp. Group: Enzymes. Synonyms: glycerol-3-phosphate oxidase; EC 1.1.3.21; sn-glycerol-3-phosphate: oxygen 2-oxidoreductase; glycerol phosphate oxidase; glycerol-1-phosphate oxidase; glycerol phosphate oxidase; L-alpha-glycerophosphate oxidase; alpha-glycerophosphate oxidase; L-alpha-glycerol-3-phosphate oxidase. Enzyme Commission Number: EC 1.1.3.21. CAS No. 9046-28-0. Glycerol-3-phosphate oxidase. Activity: > 40 U/mg. Appearance: Yellowish powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Pediococcus sp. glycerol-3-phosphate oxidase; EC 1.1.3.21; sn-glycerol-3-phosphate: oxygen 2-oxidoreductase; glycerol phosphate oxidase; glycerol-1-phosphate oxidase; glycerol phosphate oxidase; L-alpha-glycerophosphate oxidase; alpha-glycerophosphate oxidase; L-alpha-glycerol-3-phosphate oxidase. Cat No: DIA-154. | |
| Native Porcine Mutarotase | In enzymology, an aldose 1-epimerase (EC 5.1.3.3) is an enzyme that catalyzes the chemical reaction:alpha-D-glucose<-> beta-D-glucose. Hence, this enzyme has one substrate, alpha-D-glucose, and one product, beta-D-glucose. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. This enzyme participates in glycolysis and gluconeogenesis. Applications: Clinical chemistry. Group: Enzymes. Synonyms: mutarotase; aldose mutarotase; galactose mutarotase; galactose 1-epimerase; D-galactose 1-epimerase; aldose 1-epimerase; EC 5.1.3.3. Enzyme Commission Number: EC 5.1.3.3. CAS No. 9031-76-9. Mutarotase. Storage: Store desiccated at-15°C or below. Allow to come to room temperature before opening. Before returning to storage, redesiccate under vacuum over silica gel for a minimum of four hours. Re-seal before returning to-15°C or below. Form: A freeze-dried material. Source: Porcine kidney. Species: Porcine. mutarotase; aldose mutarotase; galactose mutarotase; galactose 1-epimerase; D-galactose 1-epimerase; aldose 1-epimerase; EC 5.1.3.3. Cat No: NATE-0465. | |
| Native Pseudomonas sp. Oxaloacetate decarboxylase | Oxaloacetate decarboxylase is a carboxy-lyase involved in the conversion of oxaloacetate into pyruvate. It is categorized under EC 4.1.1.3. In some bacteria this enzyme is a trimer, composed of alpha, beta and gamma subunits. The beta and gamma subunits are integral membrane proteins. Native oxaloacetate decarboxylase (ec 4.1.1.3) was purified from pseudomonas sp. Applications: Useful for enzymatic determination of ast. Group: Enzymes. Synonyms: EC 4.1.1.3; Oxaloacetate decarboxylase; Oxalate beta-decarboxylase; Oxaloacetate carboxy-lyase. Enzyme Commission Number: EC 7.2.4.2 (Formerly EC 4.1.1.3). CAS No. 9024-98-0. Oxaloacetate decarboxylase. Activity: > 100 U/mg. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Pseudomonas sp. EC 4.1.1.3; Oxaloacetate decarboxylase; Oxalate beta-decarboxylase; Oxaloacetate carboxy-lyase. Cat No: DIA-161. | |
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