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| Product | Description | |
|---|---|---|
| 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 polymyxa Dispase | Dispase is a protease which cleaves fibronectin, collagen IV, and to a lesser extent collagen I. It is found in some bacteria and can be isolated from culture filtrates of Bacillus polymyxa. It can be extracted, purified, and used in research. It can be particularly useful to separate embryonic epithelia and mesenchyme. Dispase II is specific for the cleavage of Leucine-Phenylalanine bonds. Dispase is often used to digest adhering primary cells in culture, since this treatment turned out to be milder than trypsin digestion. Applications: Dispase is a protease which cleaves fibronectin, collagen iv, and to a lesser extent collagen i. it is found in some bacteria and can be iso...d used in research. it can be particularly useful to separate embryonic epithelia and mesenchyme. dispase ii is specific for the cleavage of leucine-phenylalanine bonds. dispase is often used to digest adhering primary cells in culture, since this treatment turned out to be milder than trypsin digestion (sinclair et al., 2013). a recent article also finds that dispase can digest serine-phenylalanine. Group: Enzymes. Synonyms: Dispase; 42613-33-2; Proteinase; Bacillus polymyxa neutral. CAS No. 42613-33-2. Dispase. Activity: ~0.4 unit/mg solid. Storage: 2-8°C. Form: powder. Source: Bacillus polymyxa. Dispase; 42613-33-2; Proteinase; Bacillus polymyxa neutral. Cat No: NATE-0193. | |
| Native Bacillus polymyxa Dispase I | Dispase I is a rapid, effective, gentle and neutral protease that can separate intact epidermis from the dermis. It can also separate intact epithelial sheets in culture from the substratum. The enzyme preserves the viability of the epithelial cells while cleaving the basement membrane zone region. It can also be used to prevent clumping in suspension cultures. This protease cleaves fibronectin and type IV collagen, but not laminin, type V collagen, serum albumin, or transferrin. It hydrolyzes N-terminal peptide bonds of non-polar amino acid residues. It preferentially attacks denatured and intercellular proteins with exposed hydrophobic amino acid residues. Ca2+, Mg2+, Mn2+...e i has also been used in a study to investigate a dityrosine-based substrate for a protease assay. dispase i has been used in lung digestion and processing for flow staining, as well as for cd4 cell isolation in mice. the enzyme has also been used to digest excised wounds and a small amount of surrounding skin for the detection of gfp+ (green fluorescence protein) cells. this study to investigated the effect of differentiation and angiogenesis of bone marrow-derived mesenchymal stem cells on wound healing. it has also been used to remove the epidermis during the isolation of dermal fibroblasts from mice. Group: Enzymes. Synonyms: Dispase I; Dispase; 42613-33-2; Protease fro | |
| Native Bacillus polymyxa Dispase II | Dispase II is a neutral protease that hydrolyzes the N-terminal peptide bonds of non-polar amino acid residues. It may be used for separating many tissues and cells grown in vitro. The enzyme is very gentle and does not damage cell membranes. It can also be used to prevent clumping in suspension cultures. This protease cleaves fibronectin and type IV collagen, but not laminin, type V collagen, serum albumin, or transferrin. Dispase II is specific for the cleavage of Leucine-Phenylalanine bonds. Ca2+, Mg2+, Mn2+, Fe2+, Fe3+ and Al3+ activate the enzyme. EDTA, EGTA, Hg2+ and other heavy metals inhibit the enzyme activity. The enzyme contains 1g-atom of zinc per g-mol of purif... it has been used in the treatment of rat heart pieces during the isolation of mitochondria from rat heart. it has also been used for the isolation of dental pulp stem cells (dpscs) by enzymatic hydrolysis. these cells have been compared with dpscs isolated by explant method to analyse their stem cell and differentiation properties. Group: Enzymes. Synonyms: Dispase II; Dispase; 42613-33-2; Protease from Bacillus polymyxa. CAS No. 42613-33-2. Dispase. Activity: > 0.5 units/mg solid. Storage: 2-8°C. Form: lyophilized powder containing calcium acetate and milk sugar. Source: Bacillus polymyxa. Dispase II; Dispase; 42613-33-2; Protease from Bacillus polymyxa. Cat No: NATE-0192. | |
| Native Bacillus polymyxa Neutral Protease (Dispase) | Neutral protease (Dispase) is a non-mammalian animal origin free (AOF) metallo, neutral protease. Its mild proteolytic action makes the enzyme especially suitable for the preparation of primary cells and secondary (subcultivation) cell culture, since it is gentle on cell membranes. This protease is also used as a secondary enzyme in cell isolation and tissue dissociation applications, commonly used with collagense. Chromatographically purified. a lyophilized powder. Applications: Tissue disaggregation and subcultivation; prevention of unwanted cell clumping; preparation of cells for culture; separation of intact epidermis from dermis and intact epithelial sheet in c...se; Neutral Protease (Dispase). Enzyme Commission Number: EC 3.4.24.28. CAS No. 9001-92-7. Purity: Chromatographically purified. Neutral Protease. Mole weight: 32.5 kDa. Activity: > 4 units per mg dry weight. Stability: Stable at 2-8°C for 12 months. Aliquot and Store at -20°C after reconstitution with water or commonly used balanced salt solutions or media. Storage: Store at 2-8°C. Form: lyophilized powder. Source: Bacillus polymyxa. Bacillolysin; EC 3.4.24.28; Bacillus metalloendopeptidase; Bacillus subtilis neutral proteinase; anilozyme P 10; Bacillus metalloproteinase; Bacillus neutral proteinase; megateriopeptidase; Neutral Protease (Dispase). Cat No: NATE-0482. | |
| Native Bacillus pumilus Bilirubin Oxidase/Laccase | 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. Group: Enzymes. Synonyms: bilirubin oxidase M-1; EC 1.3.3.5; 80619-01-8; Bilirubin:oxygen oxidoreductase; Bilirubin Oxidase. Purity: ~ 90% (SDS PAGE). Bilirubin Oxidase. Mole weight: 61 kDa. Storage: at -20°C. Form: Lyophilized powder. Source: Bacillus pumilus. bilirubin oxidase M-1; EC 1.3.3.5; 80619-01-8; Bilirubin:oxygen oxidoreductase; Bilirubin Oxidase. Cat No: NATE-1257. | |
| Native Bacillus sp. Amylase, Maltogenic | Glucan 1,4-alpha-maltohydrolase (EC 3.2.1.133, maltogenic alpha-amylase, 1,4-alpha-D-glucan alpha-maltohydrolase) is an enzyme with system name 4-alpha-D-glucan alpha-maltohydrolase. This enzyme catalyses the following chemical reaction:hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the non-reducing ends of the chains. This enzyme acts on starch and related polysaccharides and oligosaccharides. Applications: Maltogenic amylases (mase) are commonly used in the starch industry. they are used to hydrolyze starch, pullulan and cyclodextrin and to make novel carbohydrates. Group: Enzymes. Synonyms: Glucan 1,4-alpha-maltohydrolase; EC 3.2.1.133; maltogenic alpha-amylase; 1,4-alpha-D-glucan alpha-maltohydrolase; Glucan 1,4-α-maltohydrolase, Maltogenic Amylase, Novamyl 1000BG. Enzyme Commission Number: EC 3.2.1.133. CAS No. 160611-47-2. α-Amylase. Storage: 2-8°C. Source: Bacillus sp. Glucan 1,4-alpha-maltohydrolase; EC 3.2.1.133; maltogenic alpha-amylase; 1,4-alpha-D-glucan alpha-maltohydrolase; Glucan 1,4-α-maltohydrolase, Maltogenic Amylase, Novamyl 1000BG. Cat No: NATE-0074. | |
| Native Bacillus sp Chitosanase | Chitosanase is a powdered chitosanase preparation made by submerged fermentation of a selected strain of the bacterium Bacillus sp. The enzyme catalyzes the breakdown of chitosan, a partially or completely de-acetylated derivative of chitin (β-1,4 homopolymer of N-acetyl glucosamine). Applications: Chitosanase can be used for hydrolyzing chitosan(degree of de-acetylatin: 40?100%). especially, it can be used for the production of chitosan oligosaccharides from chitosan, which have a variety of biological activities such as immuno-stimulating activity, anti-tumor activity, anti-microbial activity, etc. Group: Enzymes. Synonyms: Chitosanase; EC 3.2.1.132; 51570-20-8; Chitosan N-acetylglucosaminohydrolase. Enzyme Commission Number: EC 3.2.1.132. CAS No. 51570-20-8. Chitosanase. Mole weight: 45,000Da estimated by SDS-PAGE. Activity: 35,000U/g. Appearance: White or light yellow colored, freeze-dried powder. Storage: The product should be stored in a cool, dry environment with temperatures below 4°C. Source: Bacillus sp. Chitosanase; EC 3.2.1.132; 51570-20-8; Chitosan N-acetylglucosaminohydrolase. Cat No: NATE-1746. | |
| 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 sphaericus 12α-Hydroxysteroid Dehydrogenase | In enzymology, a 12alpha-hydroxysteroid dehydrogenase (EC 1.1.1.176) is an enzyme that catalyzes the chemical reaction:3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + NADP+<-> 3alpha,7alpha-dihydroxy-12-oxo-5beta-cholanate + NADPH + H+. Thus, the two substrates of this enzyme are 3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate and NADP+, whereas its 3 products are 3alpha,7alpha-dihydroxy-12-oxo-5beta-cholanate, NADPH, 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 is involved in a metabolic pathway that degrades bile acids into cholesterol. Group: Enzymes. Synonyms: EC 1.1.1.176; 61642-40-8; 12α Hydroxysteroid Dehydrogenase; 12alpha-hydroxy steroid dehydrogenase; NAD+-dependent. Enzyme Commission Number: EC 1.1.1.176. CAS No. 61642-40-8. 12α-Hydroxysteroid Dehydrogenase. Activity: 150-350 units/mg protein (Lowry). Storage: -20°C. Form: lyophilized powder. Source: Bacillus sphaericus. EC 1.1.1.176; 61642-40-8; 12α Hydroxysteroid Dehydrogenase; 12alpha-hydroxy steroid dehydrogenase; NAD+-dependent 12alpha-hydroxysteroid dehydrogenase; NADP+-12alpha-hydroxysteroid dehydrogenase; 12-α-Hydroxysteroid Dehydrogenase; 12alpha-hydroxysteroid:NADP+ 12-oxidoreductase. Cat No: NATE-0001. | |
| 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. Leucine dehydrogenase | In enzymology, a leucine dehydrogenase (EC 1.4.1.9) is an enzyme that catalyzes the chemical reaction: L-leucine + H2O + NAD+ <-> 4-methyl-2-oxopentanoate + NH3 + NADH + H+. The 3 substrates of this enzyme are L-leucine, H2O, and NAD+, whereas its 4 products are 4-methyl-2-oxopentanoate, NH3, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. This enzyme participates in valine, leucine and isoleucine degradation and valine, leucine and isoleucine biosynthesis. Applications: This enzyme is useful for enzyme determination of l-leucine and the activity of leucine amino-peptidase. Group: Enzymes. Synonyms: EC 1.4.1.9; Leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); L-leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); LeuDH. Enzyme Commission Number: EC 1.4.1.9. CAS No. 9082-71-7. Leucine dehydrogenase. Mole weight: 245 kDa. Activity: Grade? 20U/mg-solid or more (containing approx. 70% of stabilizers). Stability: Stable at-20°C for at least one year. Appearance: White amorphous powder, lyophilized. Source: Bacillus sp. EC 1.4.1.9; Leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); L-leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); LeuDH. Cat No: DIA-209. | |
| 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 sp. Purine Nucleoside Phosphorylase | Purine nucleoside phosphorylase (also known as PNPase) is an enzyme (EC 2.4.2.1) involved in purine metabolism. PNP metabolizes adenosine into adenine, inosine into hypoxanthine, and guanosine into guanine, in each case creating ribose phosphate. NP encodes the enzyme purine nucleoside phosphorylase that together with adenosine deaminase (ADA) serves a key role in purine catabolism, referred to as the salvage pathway. Mutations in either enzyme result in a severe combined immunodeficiency (SCID). Confusingly, the same abbreviation (PNPase), is also used for another, otherwise unrelated, enzyme, namely Polynucleotide Phosphorylase. Purine nucleoside phosphorylase produced in microorganism has a molecular mass of 32 kda. Applications: Useful for enzymatic determination of inorganic phosphate. Group: Enzymes. Synonyms: inos. Enzyme Commission Number: EC 2.4.2.1. CAS No. 9030-21-1. PNPase. Activity: > 500U/mL. Appearance: Colourless to light brown solution. Storage: -20°C. Form: Liquid. Source: Bacillus sp. inosine phosphorylase; PNPase; PUNPI; PUNPII; inosine-guanosine phosphorylase; nucleotide phosphatase; purine deoxynucleoside phosphorylase; purine deoxyribonucleoside phosphorylase; purine nucleoside phosphorylase; purine ribonucleoside phosphorylase; purine-nucleoside: phosphate ribosyltransferase; EC 2.4.2.1. Cat No: DIA-164. | |
| Native Bacillus sp. Pyroglutamate Aminopeptidase | Pyroglutamate aminopetidase is an enzyme that digests proteins. Applications: Pyroglutamate aminopetidase is used to digest proteins for subsequent analysis, such as amino acid sequencing. pyroglutamate aminopeptidase is used to hydrolyze and activate various prodrugs. Group: Enzymes. Synonyms: pyroglutamyl-peptidase I; Pyroglutamate aminopeptidase; EC 3.4.19.3; 5-oxoprolyl-peptidase; pyrase; pyroglutamate aminopeptidase; pyroglutamyl aminopeptidase; L-pyroglutamyl peptide hydrolase; pyrrolidone-carboxyl peptidase; pyrrolidone-carboxylate peptidase; pyrrolidonyl peptidase; L-pyrrolidonecarboxylate peptidase; pyroglutamidase; pyrrolidonecarboxylyl peptidase; 9075-21-2. Enzyme Commission Number: EC 3.4.19.3. CAS No. 9075-21-2. Pyrase. Activity: > 0.11 units/mg protein. Storage: -20°C. Source: Bacillus sp. pyroglutamyl-peptidase I; Pyroglutamate aminopeptidase; EC 3.4.19.3; 5-oxoprolyl-peptidase; pyrase; pyroglutamate aminopeptidase; pyroglutamyl aminopeptidase; L-pyroglutamyl peptide hydrolase; pyrrolidone-carboxyl peptidase; pyrrolidone-carboxylate peptidase; pyrrolidonyl peptidase; L-pyrrolidonecarboxylate peptidase; pyroglutamidase; pyrrolidonecarboxylyl peptidase; 9075-21-2. Cat No: NATE-0647. | |
| Native Bacillus sp. Sarcosine Oxidase | Sarcosine oxidase is an enzyme (EC 1.5.3.1) that catalyzes the oxidative demethylation of sarcosine to yield glycine, H2O2, 5,10-CH2-tetrahydrofolate in a reaction requiring H4-tetrahydrofolate and oxygen. Corynebacterial sarcosine oxidase is a heterotetramer and is produced as an inducible enzyme when Corynebacterium sp.is grown with sarcosine as source of carbon and energy. Monomeric sarcosine oxidase (msox) is a flavoenzyme that catalyzes the oxidative demethylation of sarcosine (n-methylglycine) to yield glycine, formaldehyde, and hydrogen peroxide. monomeric sarcosine oxidase can oxidize other secondary amino acids such as n-methyl-l-alanine, n-ethylglycine, and l-proline. Applications: Sarcosine oxidase has been used in a study as part of a multienzyme cascade, that when immobilized constructed amperometric biosensors. sarcosine oxidase has also been used in a study to investigate oxidation of amines by flavoproteins. Group: Enzymes. Synonyms: Sarcosine oxidase; EC 1.5.3.1; 9029-22-5; sarcosine:oxygen oxidoreductase (demethylating). Enzyme Commission Number: EC 1.5.3.1. CAS No. 9029-22-5. SAO. Activity: 25-50 units/mg solid. Storage: -20°C. Form: lyophilized powder; No stabilizers added. Source: Bacillus sp. Sarcosine oxidase; EC 1.5.3.1; 9029-22-5; sarcosine:oxygen oxidoreductase (demethylating). Cat No: NATE-0664. | |
| Native Bacillus sp. Uricase | The enzyme urate oxidase (UO), or uricase or factor-independent urate hydroxylase, absent in humans, catalyzes the oxidation of uric acid to 5-hydroxyisourate: Uric acid + O2 + H2O ? 5-hydroxyisourate + H2O2 ? allantoin + CO2. Applications: This enzyme is useful for enzymatic determination of uric acid in clinical analysis. Group: Enzymes. Synonyms: urate oxidase; uric acid oxidase; uricase; uricase; urate: oxygen oxidoreductase; EC 1.7.3.3; uricase II. UO. Mole weight: approx.150,000. Activity: Grade? 1.5U/mg-solid or more. Stability: Stable at -20°C for at least 6 months. Appearance: White amorphous powder, lyophilized. Source: Bacillus sp. urate oxidase; uric acid oxidase; uricase; uricase; urate: oxygen oxidoreductase; EC 1.7.3.3; uricase II. Cat No: DIA-276. | |
| 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 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, ... acetate kinase from creative enzymes. this [32p]-acetyl phosphate was used to label bldm, bldm d-54n or bldm d-54a loci during the study of the effect of bldm gene on streptomyces coelicolor development. Group: Enzymes. Synonyms: Acetate kinase (phosphorylating); Acetic kinase; Acetokinase; 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: 400-1,200 units/mg solid. Storage: 2-8°C. Form: lyophilized powder. Contains potassium phosphate buffer. Source: Bacillus stearothermophilus. Acetate kinase (phosphorylating); Acetic kinase; Acetokinase; EC 2.7.2.1; 9027-42-3; Acetate kinase. Cat No: NATE-0016. | |
| Native Bacillus stearothermophilus Alanine Dehydrogenase | L-Alanine dehydrogenase is a stereospecific dehydrogenase that catalyzes the reversible deamination of L-alanine to pyruvate and ammonium. It is important for the generation of pyruvate during sporulation. Applications: The enzyme is useful for determination of l-alanine. Group: Enzymes. Synonyms: L-Alanine Dehydrogenase; Alanine dehydrogenase; EC 1.4.1.1; 9029-06-5; AlaDH; NAD+-linked alanine dehydrogenase; alpha-alanine dehydrogenase; NAD+-dependent alanine dehydrogenase; alanine oxidoreductase; NADH-dependent alanine dehydrogenase. Enzyme Commission Number: EC 1.4.1.1. CAS No. 9029-6-5. AlaDH. Mole weight: ca. 230,000; Subunit molecular weight : ca. 38,000. Appearance: Lyophilized. Storage: Stable at -20 °C for at least one year. Source: Bacillus stearothermophilus. L-Alanine Dehydrogenase; Alanine dehydrogenase; EC 1.4.1.1; 9029-06-5; AlaDH; NAD+-linked alanine dehydrogenase; alpha-alanine dehydrogenase; NAD+-dependent alanine dehydrogenase; alanine oxidoreductase; NADH-dependent alanine dehydrogenase. Cat No: NATE-1899. | |
| Native Bacillus stearothermophilus Alanine Racemase | Alanine racemase is involved in alanine, aspartate and D-alanine metabolism. 3-Fluoro-D-alanine and D-Cycloserine are known to inhibit alanine racemase. Alanine racemase monomer is composed of two domains, an eight-stranded α/β barrel at the N-terminus and a C-terminal domain. The N-terminus includes residues 1-240, whereas the C-terminal comprises of the β-strand (residues 241-388). One molecule of pyridoxalphosphate (PLP) is present as the cofactor in each subunit. Applications: Alanine racemase is used to convert l-alanine into d-alanine. alanine racemase, from creative enzymes, has been used to isomerize l-[u-14c]alanine to a racemic mixture of l/d-[14c]alanine. Group: Enzymes. Synonyms: Alanine Racemase; EC 5.1.1.1; 9024-06-0; L-alanine racemase. Enzyme Commission Number: EC 5.1.1.1. CAS No. 9024-06-0. Alanine Racemase. Mole weight: Mr 78 kDa (2 subunits 39 kDa each). Activity: > 10 Iunits/mg solid. Storage: -20°C. Form: lyophilized powder. Lyophilized from 50 mM phosphate buffer, pH 7.5. Source: Bacillus stearothermophilus. Alanine Racemase; EC 5.1.1.1; 9024-06-0; L-alanine racemase. Cat No: NATE-0045. | |
| Native Bacillus stearothermophilus Diaphorase 1 | Diaphorase catalyzes the reaction of a reduced di- or tri-phosphopyridine nucleotide hydrogen donor with a hydrogen acceptor, usually a dye in the leucoform. Applications: The enzyme is useful for the measurement of various dehydrogenase reactions in visible spectral range. Group: Enzymes. Synonyms: Diaphorase 1; Di-1; EC 1.6.99 -. Enzyme Commission Number: EC 1.6.99.-. Diaphorase. Mole weight: ca. 30,000. Appearance: Lyophilized. Storage: Stable at -20 to 5 °C for at least one year. Source: Bacillus stearothermophilus. Diaphorase 1; Di-1; EC 1.6.99 -. Cat No: NATE-1901. | |
| Native Bacillus stearothermophilus Esterase | An esterase is a hydrolase that splits esters into acids and alcohols. Applications: The compound is commonly used for the synthesis of biodiesel and biopolymers, as well as in the production of pharmaceuticals, agr ochemicals and flavor compounds. Group: Enzymes. Synonyms: EC 3.1.1.1; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyRate esterase; triacetin esterase; carboxyl ester hydrolase; butyRate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; esterase A; se. Enzyme Commission Number: EC 3.1.1.1. CAS No. 9016-18-6. Esterase. Activity: > 0.2 units/mg. Storage: 2-8°C. Source: Bacillus stearothermophilus. EC 3.1.1.1; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyRate esterase; triacetin esterase; carboxyl ester hydrolase; butyRate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; esterase A; serine esterase; carboxylic acid esterase; cocaine esterase; 9016-18-6. Cat No: NATE-0234. | |
| Native Bacillus stearothermophilus Fructose-6-phosphate Kinase | Fructose-1,6-bisphosphatase (FBP) is an important enzyme in glucose metabolism. It catalyzes the hydrolysis of fructose-1,6-bisphosphate to fructose-6-phosphate and inorganic phosphate. Fructose-6-phosphate kinase converts fructose-6-phosphate into fructose 1,6-bisphophate in the rate limiting step of the glycolysis cycle. Bacillus stearothermophilus phosphofructokinase (bspfk) is a homotetramer that is allosterically inhibited by phosphoenolpyruvate (pep), which binds along one dimer-dimer interface. Applications: Fructose-6-phosphate kinase from bacillus stearothermophilus was shown to interact with neuronal nitric oxide synthase (nnos) causing a defect in glycolytic metabolism and increased fatigability in dystrophic muscle. Group: Enzymes. Sy. Enzyme Commission Number: EC 2.7.1.11. CAS No. 9001-80-3. FBP. Activity: > 50 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing phosphate buffer salt. Source: Bacillus stearothermophilus. EC 2.7.1.11; phosphohexokinase; phosphofructokinase I; phosphofructokinase (phosphorylating); 6-phosphofructose 1-kinase; ATP-dependent phosphofructokinase; D-fructose-6-phosphate 1-phosphotransferase; fructose 6-phosphate kinase; fructose 6-phosphokinase; nucleotide triphosphate-dependent phosphofructokinase; phospho-1,6-fructokinase; PFK; 9001-80-3. Cat No: NATE-0252. | |
| Native Bacillus stearothermophilus Glucokinase | Glucokinase (EC 2.7.1.2) is an enzyme that facilitates phosphorylation of glucose to glucose-6-phosphate. Glucokinase occurs in cells in the liver, pancreas, gut, and brain of humans and most other vertebrates. In each of these organs it plays an important role in the regulation of carbohydrate metabolism by acting as a glucose sensor, triggering shifts in metabolism or cell function in response to rising or falling levels of glucose, such as occur after a meal or when fasting. Mutations of the gene for this enzyme can cause unusual forms of diabetes or hypoglycemia. Group: Enzymes. Synonyms: EC 2.7.1.2; glucokinase; glucokinase (phosphorylating); 9001-36-9; GCK; FGQTL3; GK; GLK; HHF3; HK4; HKIV; HXKP; LGLK; MODY2. Enzyme Commission Number: EC 2.7.1.2. CAS No. 9001-36-9. GCK. Activity: > 300 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Tris buffer salts. Source: Bacillus stearothermophilus. EC 2.7.1.2; glucokinase; glucokinase (phosphorylating); 9001-36-9; GCK; FGQTL3; GK; GLK; HHF3; HK4; HKIV; HXKP; LGLK; MODY2. Cat No: NATE-0282. | |
| Native Bacillus stearothermophilus Glycerokinase | Glycerol kinase is a phosphotransferase enzyme involved in triglycerides and glycerophospholipids synthesis. Glycerol kinase catalyzes tge MgATP-dependent phosphorylation of glycerol to produce sn-glycerol-3-phosphate and is the rate limiting enzyme in the utilization of glycerol. It is also subject to feedback regulation by fructose-1,6-bisphosphate. Group: Enzymes. Synonyms: EC 2.7.1.30; glycerokinase; GK; ATP:glycerol-3-phosphotransferase; glycerol kinase (phosphorylating); glyceric kinase; 9030-66-4. Enzyme Commission Number: EC 2.7.1.30. CAS No. 9030-66-4. GK. Activity: > 75 units/mg protein (biuret). Storage: 2-8°C. Form: buffered aqueous solution; Stabilized solution in Tris buffer, pH 7.3. Source: Bacillus stearothermophilus. EC 2.7.1.30; glycerokinase; GK; ATP:glycerol-3-phosphotransferase; glycerol kinase (phosphorylating); glyceric kinase; 9030-66-4. Cat No: NATE-0286. | |
| Native Bacillus stearothermophilus 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: Inorganic pyrophosphatase (ppase) is a ubiquitous enzyme catalyzing the reaction ppi + h2o ? 2pi. it plays an important role in protein, rna, and dna synthesis. Group: Enzymes. Synonyms: Pyrophosphate phosphohydrolase; inorganic pyrophosphatase; EC 3.6.1.1; 9024-82-2; iphosphate phosphohydrolase. Enzyme Commission Number: EC 3.6.1.1. CAS No. 9024-82-2. Inorganic pyrophosphatase. Activity: 15-25 units/mg protein (biuret). Storage: 2-8°C. Form: lyophilized powder. Source: Bacillus stearothermophilus. Pyrophosphate phosphohydrolase; inorganic pyrophosphatase; EC 3.6.1.1; 9024-82-2; iphosphate phosphohydrolase. Cat No: NATE-0353. | |
| Native Bacillus stearothermophilus Leucine Dehydrogenase | In enzymology, a leucine dehydrogenase (EC 1.4.1.9) is an enzyme that catalyzes the chemical reaction: L-leucine + H2O + NAD+ <-> 4-methyl-2-oxopentanoate + NH3 + NADH + H+. The 3 substrates of this enzyme are L-leucine, H2O, and NAD+, whereas its 4 products are 4-methyl-2-oxopentanoate, NH3, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. This enzyme participates in valine, leucine and isoleucine degradation and valine, leucine and isoleucine biosynthesis. Applications: The enzyme is useful for determination of l-leucine, l-valine or l-isoleucine. Group: Enzymes. Synonyms: EC 1.4.1.9; Leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); L-leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); LeuDH. Enzyme Commission Number: EC 1.4.1.9. CAS No. 9082-71-7. Leucine dehydrogenase. Mole weight: ca. 300,000; Subunit molecular weight : ca. 49,000. Appearance: Lyophilized. Storage: Stable at -20 °C for at least one year. Source: Bacillus stearothermophilus. EC 1.4.1.9; Leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); L-leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); LeuDH. Cat No: NATE-1905. | |
| Native Bacillus stearothermophilus Myokinase | Adenylate kinase (EC 2.7.4.3) (also known as ADK or myokinase) is a phosphotransferase enzyme that catalyzes the interconversion of adenine nucleotides, and plays an important role in cellular energy homeostasis. Myokinase is an enzyme that can be found in skeletal muscle and acts as a phosphotransferase agitator. Applications: Myokinase from bacillus stearothermophilus has been used in a study to assess its thermostability grown in a temperature range from 37 oc to 60 oc. Group: Enzymes. Synonyms: Adenylate kinase; EC 2.7.4.3; ADK; myokinase; 9013-02-9; Adenylic kinase; Adenylokinase. Enzyme Commission Number: EC 2.7.4.3. CAS No. 9013-2-9. Myokinase. Activity: > 150 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Tris buffer salts, pH 8.5. Source: Bacillus stearothermophilus. Adenylate kinase; EC 2.7.4.3; ADK; myokinase; 9013-02-9; Adenylic kinase; Adenylokinase. Cat No: NATE-0036. | |
| 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 stearothermophilus Phosphotransacetylase | Phosphotransacetylase converts CoA to acetyl CoA. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. This enzyme participates in 3 metabolic pathways:taurine and hypotaurine metabolism, pyruvate metabolism, and propanoate metabolism. Applications: Phosphotransacetylase, from bacillus stearothermophilus, is used to convert coa to acetyl coa. phosphotransacetylase (pta) is used to study transport systems for acetate. it is used to study metabolic pathways in various bacterium. Group: Enzymes. Synonyms: phosphate acetyltransferase; phosphotransacetylase; phosphoacylase; PTA; EC 2.3.1.8; 9029-91-8. Enzyme Commission Number: EC 2.3.1.8. CAS No. 9029-91-8. PTA. Activity: > 3,000 units/mg protein (biuret). Storage: -20°C. Form: Lyophilized powder containing potassium phosphate. Source: Bacillus stearothermophilus. phosphate acetyltransferase; phosphotransacetylase; phosphoacylase; PTA; EC 2.3.1.8; 9029-91-8. Cat No: NATE-0641. | |
| Native Bacillus stearothermophilus Polynucleotide Phosphorylase | Polynucleotide phosphorylase (PNPase) is a bifunctional enzyme with a phosphorolytic 3' to 5' exoribonuclease activity and a 3'-terminal oligonucleotide polymerase activity. It is also involved in mRNA processing and degradation in bacteria, plants, and humans. Applications: The enzyme is useful for the preparation of polyribonucleotide. Group: Enzymes. Synonyms: PNPase; nucleoside diphosphate:polynucleotidyl transferase; polyribonucleotide nucleotidyltransferase; polynucleotide phosphorylase; polyribonucleotide phosphorylase; EC 2.7.7.8; 9014-12-4. Enzyme Commission Number: EC 2.7.7.8. CAS No. 9014-12-4. Polynucleotide phosphorylase. Mole weight: 300,000 - 340,000; Subunit molecular weight : ca. 85,000. Appearance: Lyophilized. Storage: Stable at -20 °C for at least one year. Source: Bacillus stearothermophilus. PNPase; nucleoside diphosphate:polynucleotidyl transferase; polyribonucleotide nucleotidyltransferase; polynucleotide phosphorylase; polyribonucleotide phosphorylase; EC 2.7.7.8; 9014-12-4. Cat No: NATE-1908. | |
| Native Bacillus stearothermophilus Pyruvate Kinase | Pyruvate kinase is an enzyme involved in glycolysis. It catalyzes the transfer of a phosphate group from phosphoenolpyruvate (PEP) to ADP, yielding one molecule of pyruvate and one molecule of ATP. Applications: Pyruvate kinase from bacillus stearothermophilus has been used in a study to assess evidence that the genes for phosphofructokinase and pyruvate kinase constitute an operon. 1 it has also been used in a study to investigate the importance of the lys221 active site for pyruvate kinase activity. Group: Enzymes. Synonyms: Pyruvate kinase; EC 2.7.1.40; 9001-59-6; phosphoenolpyruvate kinase; phosphoenol transphosphorylase; pyruvate kinase (phosphorylating); fluorokinase; fluorokinase (phosphorylating); pyruvic kinase; pyruvate phosphotransferase; ATP:pyruvate 2-O-phosphotransferase. Enzyme Commission Number: EC 2.7.1.40. CAS No. 9001-59-6. Pyruvate Kinase. Activity: 100-300 units/mg protein. Stability: 2-8°C. Form: lyophilized powder. Source: Bacillus stearothermophilus. EC 2.7.1.40; 9001-59-6; Pyruvate kinase. Cat No: NATE-0649. | |
| Native Bacillus stearothermophilus Superoxide Dismutase | Superoxide dismutase (SOD) catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. SOD plays a critical role in the defense of cells against the toxic effects of oxygen radicals. SOD competes with nitric oxide (NO) for superoxide anion (which reacts with NO to form peroxynitrite), thereby SOD promotes the activity of NO. SOD has also been shown to suppress apoptosis in cultured rat ovarian follicles, neural cell lines, and transgenic mice by preventing the conversion of NO to peroxynitrate, an inducer of apoptosis. Applications: The enzyme is useful for medicine, cosmetic material and nutrition or antioxidant. Group: Enzymes. Synonyms: Superoxide dismutases; EC 1.15.1.1; superoxidase dismutase;. Enzyme Commission Number: EC 1.15.1.1. CAS No. 9054-89-1. SOD. Mole weight: ca. 50,000; Subunit molecular weight : ca. 25,000. Appearance: Lyophilized. Storage: Stable at -20 °C for at least one year. Source: Bacillus stearothermophilus. Superoxide dismutases; EC 1.15.1.1; superoxidase dismutase; copper-zinc superoxide dismutase; Cu-Zn superoxide dismutase; ferrisuperoxide dismutase; superoxide dismutase I; superoxide dismutase II; SOD; Cu,Zn-SOD; Mn-SOD; Fe-SOD; SODF; SODS; SOD-1; SOD-2; SOD-3; SOD-4; hemocuprein; erythrocuprein; cytocuprein; cuprein ; hepatocuprein; 9054-89-1. Cat No: NATE-1910. | |
| 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 Bacillus subtilis Diacetinase | Native Bacillus subtilis Diacetinase. Applications: Used in the formulation of lipase testing reagents. Group: Enzymes. Synonyms: Diacetinase; EC 3.1.1-. Enzyme Commission Number: E.C.3.1.1-. Diacetinase. Activity: 0.228 U/mg-0.633 U/mg liquid. Appearance: Colourless to Yellowish solution. Form: Liquid. Source: Bacillus subtilis. Diacetinase; EC 3.1.1-. Cat No: NATE-0187. | |
| Native Bacillus subtilis L-Alanine Dehydrogenase | L-Alanine dehydrogenase is an A-stereospecific dehydrogenase that catalyzes the reversible deamination of L-alanine to pyruvate and ammonium. It is important for the geneRation of pyruvate during sporulation. L-Alanine dehydrogenase from Bacillus subtilis has a predominately ordered kinetic mechanism in which NAD binds before L-alanine. Subsequently, ammonia, pyruvate, and NADH are released in that specific order. Optimal pH for the amination reaction is 8.8-9.0, whereas it is 10-10.5 for the deamination reaction. The enzyme is inactivated by divalent metal ions and p-chloromercuribenzoate, mercuric ion being most effective. The inactivation may be reversed by L-or D-...genase. Enzyme Commission Number: EC 1.4.1.1. CAS No. 9029-6-5. AlaDH. Activity: Type I, ~30 units/mg protein (Lowry); Type II, > 20 units/mg protein (Lowry). Storage: -20°C. Form: Type I, buffered aqueous glycerol solution, Solution in 50% glycerol containing 10 mM potassium phosphate buffer, pH 7.7; Type II, ammonium sulfate suspension, Suspension in 2.4 M (NH4)2SO4 solution, pH 7.0. Source: Bacillus subtilis. L-Alanine Dehydrogenase; Alanine dehydrogenase; EC 1.4.1.1; 9029-06-5; AlaDH; NAD+-linked alanine dehydrogenase; alpha-alanine dehydrogenase; NAD+-dependent alanine dehydrogenase; alanine oxidoreductase; NADH-dependent alanine dehydrogenase. Cat No: NATE-0043. | |
| Native Bacillus Subtilis Sutilains (industry grade) | Sutilain, a proteolytic enzyme isolated from Bacillus subtilis, has been used for the treatment of burns. Group: Enzymes. Synonyms: Proteinase; Bacillus subtilis; sutilain. CAS No. 12211-28-8. Purity: > 90%. Source: Bacillus subtilis. Proteinase; Bacillus subtilis; sutilain. Cat No: NATE-1631. | |
| Native Bacillus subtilis Xylanase Enzyme (Food Grade) | Xylanase is the name given to a class of enzymes which degrade the linear polysaccharide beta-1,4-xylan into xylose, thus breaking down hemicellulose, one of the major components of plant cell walls. As such, it plays a major role in micro-organisms thriving on plant sources for the degradation of plant matter into usable nutrients. Xylanases are produced by fungi, bacteria, yeast, marine algae, protozoans, snails, crustaceans, insect, seeds, etc., (mammals do not produce xylanases). Xylanase which made from the best strain of bacillus subtilis. it is a kind of purified endo-bacteria-xylanase. it can be applied in the flour treatment for bread powder and steam brea...and chewy. 2) in the storage of bread, the appropriate xylanase can retrad bread staling, improve the water holding capacity of the bread and optimize the gluten network, thereby, preventing water loss and re-allocate, stabilize the organizational structure of the bread. Group: Enzymes. Synonyms: EC 3.2.1.8; endo-(1?4)-β-xylan 4-xylanohydrolase; endo-1,4-xylanase; xylanase; β-1,4-xylanase; endo-1,4-xylanase; endo-β-1,4-xylanase; endo-1,4-β-D-xylanase; 1,4-β-xylan xylanohydrolase; β-xylanase; β-1,4-xylan xylanohydrolase; endo-1,4-β-xylanase; β-D-xylanase; endo-1,4-β-xylanase. Enzyme Commission Number: EC 3.2.1.8. CAS | |
| Native Bacillus thermoglucosidasius Esterase | An esterase is a hydrolase that splits esters into acids and alcohols. Group: Enzymes. Synonyms: EC 3.1.1.1; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyRate esterase; triacetin esterase; carboxyl ester hydrolase; butyRate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; esterase A; serine esterase; carboxylic acid esterase; cocaine esterase; 9016-18-6. Enzyme Commission Number: EC 3.1.1.1. CAS No. 9016-18-6. Esterase. Activity: ~0.1 units/mg. Storage: 2-8°C. Form: lyophilized powder. Source: Bacillus thermoglucosidasius. EC 3.1.1.1; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyRate esterase; triacetin esterase; carboxyl ester hydrolase; butyRate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; esterase A; serine esterase; carboxylic acid esterase; cocaine esterase; 9016-18-6. Cat No: NATE-0235. | |
| Native Bacillus thermoproteolyticus Thermolysin | Thermolysin is a thermostable neutral metalloproteinase enzyme produced by the Gram-positive bacteria Bacillus thermoproteolyticus. It requires one zinc ion for enzyme activity and four calcium ions for structural stability. Thermolysin specifically catalyzes the hydrolysis of peptide bonds containing hydrophobic amino acids. However thermolysin is also widely used for peptide bond formation through the reverse reaction of hydrolysis. Thermolysin is the most stable member of a family of metalloproteinases produced by various Bacillus species. These enzymes are also termed 'neutral' proteinases or thermolysin-like proteinases (TLPs). Group: Enzymes. Synonyms: thermolysin; Bacillus thermoproteolyticus neutral proteinase; thermoase; thermoase Y10; TLN; EC 3.4.24.27. Enzyme Commission Number: EC 3.4.24.27. CAS No. 9073-78-3. TLN. Mole weight: 36.2kDa. Activity: Reverse-phase HPLC analysis shows <30% of undigested insulin after 10 minutes of incubation with Thermolysin at 75°C using a 1:20 thermolysin:insulin ratio. Form: Lyophilized. Source: Bacillus thermoproteolyticus. thermolysin; Bacillus thermoproteolyticus neutral proteinase; thermoase; thermoase Y10; TLN; EC 3.4.24.27. Cat No: NATE-0705. | |
| Native Bacteria Achromopeptidase | Lysyl endopeptidase (EC 3.4.21.50, Achromobacter proteinase I, Achromobacter lyticus alkaline proteinase I, protease I, achromopeptidase, lysyl bond specific proteinase) is an enzyme. This enzyme catalyses the following chemical reaction:Preferential cleavage:Lys-, including-Lys-Pro-. This enzyme is isolated from Achromobacter lyticus. Hemolysins are lipids and proteins that cause lysis of red blood cells by destroying their cell membrane. although the lytic activity of some microbe-derived hemolysins on red blood cells may be of great importance for nutrient acquisition, many hemolysins produced by pathogens do not cause significant destruction of red blood cells during infe...and the effect of ciprofloxacin on biofilm formation. Group: Enzymes. Synonyms: Achromobacter proteinase I; Achromobacter lyticus alkaline proteinase I; protease I; achromopeptidase; lysyl bond specific proteinase; EC 3.4.21.50; 123175-82-6; Lysyl endopeptidase. Enzyme Commission Number: EC 3.4.21.50. CAS No. 123175-82-6. Achromopeptidase. Mole weight: ~27 kDa. Activity: > 1,000 units/mg solid; > 20,000 units/mg solid. Storage: 2-8°C. Form: lyophilized powder. Source: Bacteria. Achromobacter proteinase I; Achromobacter lyticus alkaline proteinase I; protease I; achromopeptidase; lysyl bond specific proteinase; EC 3.4.21.50; 123175-82-6; Lysyl endopeptidase. Cat No: NATE-0022. | |
| Native Bacterial Environmental DNA Glucan elongation enzyme | A thermostable 4-α-glucanotransferase that elongates linear alpha-glucan chains in starch and amylose by catalyzing the transfer of one glucose unit from the non-reducing end to a new position in an acceptor, which may be triose or larger. The enzyme can be used various applications, such as for modifications of alpha-polysaccharides and is ideal for making clear size ladders of oligosaccharides larger than maltose. The enzyme was developed from metagenome DNA obtained from environmental sample from a geothermal environment. The enzyme catalyzes the formation of the alpha-1,4-glucosidic linkages. the enzyme transfers a segment of a (1->4)-alpha-d-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-d-glucan. Group: Enzymes. Synonyms: Glucan elongation enzyme. Glucan elongation enzyme. Source: Bacterial Environmental DNA. Glucan elongation enzyme. Cat No: NATE-0302. | |
| Native Bacteria Maltose phosphorylase | Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes maltose and inorganic phosphate into β-D-glucose-1-phosphate and glucose. Group: Enzymes. Synonyms: maltose phosphorylase; maltose:phosphate 1-β-D-glucosyltransferase; EC 2.4.1.8; 9030-19-7; MP. Enzyme Commission Number: EC 2.4.1.8. CAS No. 9030-19-7. MP. Activity: > 5 units/mg protein (at 25°C and pH 7.5). Storage: 0 -5°C. Form: Ammonium sulfate suspension. Source: Bacteria. maltose phosphorylase; maltose:phosphate 1-β-D-glucosyltransferase; EC 2.4.1.8; 9030-19-7; MP. Cat No: NATE-1031. | |
| Native Bacterium cadaveris L-Lysine Decarboxylase | Lysine decarboxylase is an enzyme that converts lysine to cadaverine. Group: Enzymes. Synonyms: Lysine decarboxylase; EC 4.1.1.18; 9024-76-4; L-lysine carboxy-lyase; L-Lysine Decarboxylase. Enzyme Commission Number: EC 4.1.1.18. CAS No. 9024-76-4. Lysine decarboxylase. Activity: ~0.01 unit/mg solid. Storage: -20°C. Source: Bacterium cadaveris. Lysine decarboxylase; EC 4.1.1.18; 9024-76-4; L-lysine carboxy-lyase; L-Lysine Decarboxylase. Cat No: NATE-0425. | |
| Native Baker's yeast (S. cerevisiae) 3-Phosphoglyceric Phosphokinase | PhosphoglyceRate kinase (EC 2.7.2.3) (PGK) is an enzyme that catalyzes the reversible transfer of a phosphate group from 1,3-bisphosphoglyceRate (1,3-BPG) to ADP producing 3-phosphoglyceRate (3-PG) and ATP. Like all kinases it is a transferase. PGK is a major enzyme used in glycolysis, in the first ATP-geneRating step of the glycolytic pathway. In gluconeogenesis, the reaction catalyzed by PGK proceeds in the opposite direction, geneRating ADP and 1,3-BPG. Applications: 3-phosphoglyceric phosphokinase generates atp by catalyzing the transfer of a phosphate group from 1,3-diphosphoglycerate to adp. 3-phosphoglycerate phosphokinase is used to study glycolysis ...phoglyceric kinase; phosphoglycerokinase; EC 2.7.2.3. Enzyme Commission Number: EC 2.7.2.3. CAS No. 9001-83-6. 3-PGK. Activity: > 1000 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension. Source: Baker's yeast (S. cerevisiae). PGK; 3-PGK; ATP-3-phospho-D-glyceRate-1-phosphotransferase; ATP:D-3-phosphoglyceRate 1-phosphotransferase; 3-phosphoglyceRate kinase; 3-phosphoglyceRate phosphokinase; 3-phosphoglyceric acid kinase; 3-phosphoglyceric acid phosphokinase; 3-phosphoglyceric kinase; glyceRate 3-phosphate kinase; glycerophosphate kinase; phosphoglyceric acid kinase; phosphoglyceric kinase; phosphoglycerokinase; EC 2.7.2.3. Cat No: NATE-0006. | |
| Native Baker's yeast (S. cerevisiae) D-Ribulose-5-phosphate 3-Epimerase | RPE is a metalloenzyme and has been shown to use the divalent Zn2+ ion predominantly for catalysis. Human D-ribulose-5-phosphate 3-epimerase (hRPE) has been shown to use Fe2+ for catalysis. Applications: D-ribulose-5-phosphate 3-epimerase is an enzyme that converts the reversible conversion of d-ribulose 5-phosphate into d-xylulose 5-phosphate, which is important for the cellular response against oxidative stress. d-ribulose-5-phosphate 3-epimerase is involved in the pentose phosphate pathway, pentose and glucuronate interconversions and carbon fixation. this product is from bakers yeast and is provided as a lyophilized powder. it is useful in enzyme syste...EC 5.1.3.1. CAS No. 9024-20-8. RPE. Activity: 50-100 units/mg protein (modified Warburg-Christian). Storage: -20°C. Form: lyophilized powder. Lyophilized and essentially sulfate-free; contains approx. 35% Citrate buffer salts. Source: Baker's yeast (S. cerevisiae). EC 5.1.3.1; RPE; phosphoribulose epimerase; erythrose-4-phosphate isomerase; phosphoketopentose 3-epimerase; xylulose phosphate 3-epimerase; phosphoketopentose epimerase; ribulose 5-phosphate 3-epimerase; D-ribulose phosphate-3-epimerase; D-ribulose 5-phosphate epimerase; D-ribulose-5-P 3-epimerase; D-xylulose-5-phosphate 3-epimerase; pentose-5-phosphate 3-epimerase; 9024-20-8. Cat No: NATE-0659. | |
| Native Baker's yeast (S. cerevisiae) Enolase | Enolase is a metalloenzyme that catalyzes the interconversion of 2-phosphoglycerate to phosphoenolpyruvate. Enolase is essential for both glycolysis and gluconeogenesis. Enolase from bakers yeast is a homodimer containing two bound Mg2+ ions. The molecular weight is 93.069 kDa.The peptide consists of 436 amino acids and contains a single cysteine residue. Two of the active site components include His191 and Arg414. The phosphorylated tyrosine residue present in yeast enolase forms a substrate for phosphorylation by tyrosine protein kinase. Apart from Mg2+, the enzyme can be activated by Zn2+, Mn2+, and Cd2+. Applications: Enolase from baker?s yeast has been used in a st...d spectroscopy. it has also been used along with other proteins to study gradient chromatof ocusing-mass spectrometry; a new technique for protein analysis. Group: Enzymes. Synonyms: EC 4.2.1.11; enolase; 2-phosphoglyceRate dehydRatase; 14-3-2-protein; nervous-system specific enolase; phosphoenolpyruvate hydRatase; 2-phosphoglyceRate dehydRatase; 2-phosphoglyceric dehydRatase; 2-phosphoglyceRate enolase; γ-enolase; 2-phospho-D-glyceRate hydro-lyase; 9014-08-8. Enzyme Commission Number: EC 4.2.1.11. CAS No. 9014-8-8. Enolase. Activity: > 50 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Tris buffer salts. Source: Baker's yeast (S. cerevisiae) | |
| Native baker's yeast (S. cerevisiae) 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). Applications: Glucose-6-phosphate dehydrogenase is used to test ketose reductase activity in developing maize endosperm. 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-phosphate dehydrogenase; GPD. Enzyme Commission Number: EC 1.1.1.49. CAS No. 9001-40-5. Glucose-6-phosphate dehydrogenase. Storage: -20°C. Form: lyophilized powder. Source: Baker's yeast (S. cerevisiae). 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-219. | |
| 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 Baker's yeast (S. cerevisiae) Glyceraldehyde-3-phosphate Dehydrogenase | Glyceraldehyde-3-phosphate dehydrogenase catalyzes the conversion of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate as part of glycolysis. It has also been shown to have roles in initiation of apoptosis, transcription activation and the shuttling of ER to Golgi vesicles. Group: Enzymes. Synonyms: EC 1.2.1.12; GAPDH; glyceraldehyde-3-phosphate dehydrogenase (phosphorylating); triosephosphate dehydrogenase; dehydrogenase, glyceraldehyde phosphate; phosphoglyceraldehyde dehydrogenase; 3-phosphoglyceraldehyde . Enzyme Commission Number: EC 1.2.1.12. CAS No. 9001-50-7. Glyceraldehyde-3-phosphate Dehydrogenase. Activity: 70-140 units/mg protein. Storage: -20°C. Form: Lyophilized, sulfate-free powder stabilized with trehalose, Citrate, and DTT. Useful for systems requiring low sulfate. Source: Baker's yeast (S. cerevisiae). EC 1.2.1.12; GAPDH; glyceraldehyde-3-phosphate dehydrogenase (phosphorylating); triosephosphate dehydrogenase; dehydrogenase, glyceraldehyde phosphate; phosphoglyceraldehyde dehydrogenase; 3-phosphoglyceraldehyde dehydrogenase; NAD+-dependent glyceraldehyde phosphate dehydrogenase; glyceraldehyde phosphate dehydrogenase (NAD+); glyceraldehyde-3-phosphate dehydrogenase (NAD+); NADH-glyceraldehyde phosphate dehydrogenase; glyceraldehyde-3-P-dehydrogenase; 9001-50-7. Cat No: NATE-0278. | |
| Native Baker's yeast (S. cerevisiae) 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. This ubiquitous enzyme serves to drive metabolic reactions that produce pyrophosphate, since these reactions typically have...phohydrolase; inorganic pyrophosphatase; EC 3.6.1.1; 9024-82-2; iphosphate phosphohydrolase. Enzyme Commission Number: EC 3.6.1.1. CAS No. 9024-82-2. Inorganic pyrophosphatase. Mole weight: 71 kDa (homodimer consisting of two equal subunits of molecular weight 32-35 kDa). Activity: Type I, > 1,000 units/mg protein (BCA); Type II, > 500 units/mg protein (E1%/280). Storage: -20°C. Form: Type I, lyophilized powder containing 90% buffer salts; Type II, Lyophilized powder containing 85% buffer salts. Source: Baker's yeast (S. cerevisiae). Pyrophosphate phosphohydrolase; inorganic pyrophosphatase; EC 3.6.1.1; 9024-82-2; iphosphate phosphohydrolase. Cat No: NATE-0354. | |
| Native Baker's yeast (S. cerevisiae) Invertase | Invertase is an enzyme that catalyzes the hydrolysis (breakdown) of sucrose (table sugar). The resulting mixture of fructose and glucose is called inverted sugar syrup. Related to invertases are sucrases. Invertases and sucrases hydrolyze sucrose to give the same mixture of glucose and fructose. Invertases cleave the O-C (fructose) bond, whereas the sucrases cleave the O-C (glucose) bond. Typically used in manufacturing confectionaries, dietary supplements, and other food grade applications. Applications: Used in the production of confectionary foods and artificial honey. Group: Enzymes. Synonyms: EC 3.2.1.26; invertase; saccharase; glucosucrase; β-h-fructosidase; β-fructosidase; invertin; sucrase; maxinvert L 1000; fructosylinvertase; alkaline invertase; acid invertase; β-fructofuranosidase; β-D-fructofuranoside fructohydrolase; 9001-57. Enzyme Commission Number: EC 3.2.1.26. CAS No. 9001-57-4. Invertase. Activity: Type I, 200-300 units/mg solid; Type II, > 300 units/mg solid. Storage: -20°C. Source: Baker's yeast (S. cerevisiae). EC 3.2.1.26; invertase; saccharase; glucosucrase; β-h-fructosidase; β-fructosidase; invertin; sucrase; maxinvert L 1000; fructosylinvertase; alkaline invertase; acid invertase; β-fructofuranosidase; β-D-fructofuranoside fructohydrolase; 9001-57-4. Cat No: NATE-0357. | |
| Native Baker's yeast (S. cerevisiae) Nucleoside 5'-Diphosphate Kinase | Nucleoside 5'-diphosphate kinase is a cytosolic enzyme. Nucleoside 5'-diphosphate kinase from Saccharomyces cerevisiae is found highly expressed in the cytoplasm. It affects DNA synthesis, in part, by binding to Cdc8p. Nucleoside 5?-diphosphate kinase is a cytosolic enzyme. Applications: Nucleoside 5?-diphosphate kinase has been used in a study to examine a possible intracellular activity of the drug disodium cromoglycate in mast cells. it has also been used in a study to investigate protein synthesis in rabbit reticul ocytes. Group: Enzymes. Synonyms: nucleoside 5'-diphosphate kinase; nucleoside diphosphate (UDP) kinase; nucleoside diphosphokinase; nucleotide phosphate kinase; UDP kinase; uridine diphosphate kinase; nucleoside-diphosphate kinase; EC 2.7.4.6; 9026-51-1; NDPK. Enzyme Commission Number: EC 2.7.4.6. CAS No. 9026-51-1. NDPK. Storage: -20°C. Form: lyophilized powder; essentially sulfate-free powder. Contains sodium Citrate with a trace of magnesium and EDTA salts. Source: Baker's yeast (S. cerevisiae). nucleoside 5'-diphosphate kinase; nucleoside diphosphate (UDP) kinase; nucleoside diphosphokinase; nucleotide phosphate kinase; UDP kinase; uridine diphosphate kinase; nucleoside-diphosphate kinase; EC 2.7.4.6; 9026-51-1; NDPK. Cat No: NATE-0476. | |
| Native Baker's yeast (S. cerevisiae) Phosphoglucose Isomerase | Phosphoglucose Isomerase (PGI) is an enzyme crucial for the interconversion of D-glucose 6-phosphate and D-fructose 6-phosphate. PGI is responsible for the second step of glycolysis and is involved in glucogenesis. It is highly conserved in bacteria and eukaryotes. Applications: Isomerization of ketoses to aldoses. Group: Enzymes. Synonyms: Glucose-6-phosphate isomerase; EC 5.3.1.9; phosphohexose isomerase; phosphohexomutase; oxoisomerase; hexosephosphate isomerase; phosphosaccharomutase; phosphoglucoisomerase; phosphohexoisomerase; phosphoglucose isomerase; glucose phosphate isomerase; hexose phosphate isomerase; D-glucose-6-phosphate ketol-isomerase; 9001-41-6; PGI. Enzyme Commission Number: EC 5.3.1.9. CAS No. 9001-41-6. PGI. Mole weight: 145 kDa. Activity: 350 U/mg at +25°C with F6P as substrate. Storage: Stable at +2 to +8°C. Source: Baker's yeast (S. cerevisiae). Glucose-6-phosphate isomerase; EC 5.3.1.9; phosphohexose isomerase; phosphohexomutase; oxoisomerase; hexosephosphate isomerase; phosphosaccharomutase; phosphoglucoisomerase; phosphohexoisomerase; phosphoglucose isomerase; glucose phosphate isomerase; hexose phosphate isomerase; D-glucose-6-phosphate ketol-isomerase; 9001-41-6; PGI. Cat No: NATE-0554. | |
| Native baker's yeast (S. cerevisiae) Proteinase A | Saccharopepsin is an enzyme. This enzyme catalyses the following chemical reaction:Hydrolysis of proteins with broad specificity for peptide bonds. Cleaves-Leu-Leu-Val-Tyr bond in a synthetic substrate. This enzyme is present in baker's yeast (Saccharomyces cerevisiae). Applications: Possibly useful for producing overlap peptides in sequence studies. Group: Enzymes. Synonyms: Endopeptidase; Proteinase A; EC 3.4.23.25; yeast endopeptidase A; Saccharomyces aspartic proteinase; aspartic proteinase yscA; proteinase yscA; yeast proteinase A; Saccharomyces cerevisiae aspartic proteinase A. Enzyme Commission Number: EC 3.4.23.25. Proteinase A. Activity: 15-50 units/mg protein. Storage: -20°C. Form: Lyophilized solids containing sodium Citrate, pH 5.0. Source: S. cerevisiae. Species: baker's yeast. Endopeptidase; Proteinase A; EC 3.4.23.25; yeast endopeptidase A; Saccharomyces aspartic proteinase; aspartic proteinase yscA; proteinase yscA; yeast proteinase A; Saccharomyces cerevisiae aspartic proteinase A. Pack: Package size based on protein content. Cat No: NATE-0636. | |
| Native Baker's yeast (S. cerevisiae) Pyruvate Decarboxylase | Pyruvate decarboxylase (PDC) is a homotetrameric enzyme that catalyses the decarboxylation of pyruvic acid to acetaldehyde and carbon dioxide in the cytoplasm. Pyruvate decarboxylase depends on cofactors thiamine pyrophosphate (TPP) and magnesium. PDC contains a β-α-β structure, yielding parallel β-sheets. Applications: Pyruvate decarboxylase (pdc) is used to study residues involved in thiamine pyrophosphate (tpp) binding. it is used to study the regulation of fermentation pathways in plant species. Group: Enzymes. Synonyms: Pyruvate decarboxylase; EC 4.1.1.1; α-carboxylase (ambiguous); pyruvic decarboxylase; α-ketoacid carboxylase; 2-oxo-acid carboxy-lyase; 9001-04-1; 2-Oxo-acid carboxy-lyase; PDC. Enzyme Commission Number: EC 4.1.1.1. CAS No. 9001-4-1. PDC. Activity: 5.0-20.0 units/mg protein (biuret). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 3.2 M (NH4)2SO4 pH 6.5, stabilized with 5% glycerol, 5 mM potassium phosphate, 1 mM magnesium acetate, 0.5 mM EDTA, and 25 μM c ocarboxylase. Source: Baker's yeast (S. cerevisiae). Pyruvate decarboxylase; EC 4.1.1.1; α-carboxylase (ambiguous); pyruvic decarboxylase; α-ketoacid carboxylase; 2-oxo-acid carboxy-lyase; 9001-04-1; 2-Oxo-acid carboxy-lyase; PDC. Cat No: NATE-0510. | |
| Native Baker's yeast (S. cerevisiae) S-Acetyl-coenzyme A synthetase | Acetyl-coenzyme A synthetase catalyzes the production of acetyl-CoA. It is involved in histone acetylation in the nucleus. It may be involved in the growth of nonfermentable carbon sources such as glycerol. Acetyl-coenzyme A synthetase is induced by acetate, acetaldehyde and ethanol. Applications: S-acetyl-coenzyme a synthetase may be used to study various metabolic pathways, such as glycolysis, gluconeogenesis, pyruvate metabolism and co fixation. it may also be used in gene expression studies. Group: Enzymes. Synonyms: acetyl-CoA synthetase; acetyl activating enzyme; acetate thiokinase; acyl-activating enzyme; acetyl coenzyme A synthetase; acetic thiokinase; acetyl CoA ligase; acetyl C. Enzyme Commission Number: EC 6.2.1.1. CAS No. 9012-31-1. ACS. Activity: > 3 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing stabilizers as potassium phosphate, sucrose, and reduced glutathione. Source: Baker's yeast (S. cerevisiae). acetyl-CoA synthetase; acetyl activating enzyme; acetate thiokinase; acyl-activating enzyme; acetyl coenzyme A synthetase; acetic thiokinase; acetyl CoA ligase; acetyl CoA synthase; acetyl-coenzyme A synthase; short chain fatty acyl-CoA synthetase; short-chain acyl-coenzyme A synthetase; ACS; EC 6.2.1.1; 9012-31-1. Pack: Package size based on protein content. Cat No: NATE-0026. | |
| Native Baker's yeast (S. cerevisiae) Transaldolase | Transaldolase is an enzyme (EC 2.2.1.2) of the non-oxidative phase of the pentose phosphate pathway. In humans, transaldolase is encoded by the TALDO1 gene. The following chemical reaction is catalyzed by transaldolase:sedoheptulose 7-phosphate + glyceraldehyde 3-phosphate<-> erythrose 4-phosphate + fructose 6-phosphate. Applications: Useful in systems requiring low sulfate concentrations. Group: Enzymes. Synonyms: Transaldolase; EC 2.2.1.2; 9014-46-4; dihydroxyacetonetransferase; dihydroxyacetone synthase; formaldehyde transketolase; D-Sedoheptulose-7-phosphate:D-Glyceraldehyde-3-phosphate dihydroxyacetonetransferase. Enzyme Commission Number: EC 2.2.1.2. CAS No. 9014-46-4. Transaldolase. Activity: 10-30 units/mg protein (biuret). Storage: -20°C. Form: Lyophilized, essentially sulfate-free; contains approx. 5% Citrate buffer salts. Source: Baker's yeast (S. cerevisiae). Transaldolase; EC 2.2.1.2; 9014-46-4; dihydroxyacetonetransferase; dihydroxyacetone synthase; formaldehyde transketolase; D-Sedoheptulose-7-phosphate:D-Glyceraldehyde-3-phosphate dihydroxyacetonetransferase. Cat No: NATE-0714. | |
| Native Baker's yeast (S. cerevisiae) Triosephosphate Isomerase | Triose-phosphate isomerase (TPI or TIM) is an enzyme (EC 5.3.1.1) that catalyzes the reversible interconversion of the triose phosphate isomers dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate. TPI plays an important role in glycolysis and is essential for efficient energy production. TPI has been found in nearly every organism searched for the enzyme, including animals such as mammals and insects as well as in fungi, plants, and bacteria. However, some bacteria that do not perform glycolysis, like ureaplasmas, lack TPI. Applications: Triosephosphate isomerase has been used in a study to assess differential expression of fourteen proteins of uveal melanoma. triosephosphate isomerase has also been used in a study to investigate the use of sigmoid ph gradients in free-flow isoelectric f ocusing of human endothelial cell proteins. Group: Enzymes. Synonyms: Triose-. Enzyme Commission Number: EC 5.3.1.1. CAS No. 9023-78-3. TPI. Activity: ~10,000 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension; Crystalline suspension in 2.7 M (NH4)2SO4, 0.5 mM EDTA, pH 6.5. Source: Baker's yeast (S. cerevisiae). Triose-phosphate isomerase; phosphotriose isomerase; triose phosphoisomerase; triose phosphate mutase; D-glyceraldehyde-3-phosphate ketol-isomerase; TPI; TIM; EC 5.3.1.1; 9023-78-3. Cat No: NATE-0711. | |
| Native Baker's yeast Uridine-5'-diphosphoglucose pyrophosphorylase | UTP-glucose-1-phosphate uridylyltransferase is an enzyme associated with glycogenesis. It synthesizes UDP-glucose from glucose-1-phosphate and UTP; i.e., glucose-1-phosphate + UTP<-> UDP-glucose + pyrophosphate. Applications: Uridine-5?-diphosphoglucose pyrophosphorylase has been used in assays to determine the concentration of pyrophosphate in human urine samples. Group: Enzymes. Synonyms: UDP glucose pyrophosphorylase; glucose-1-phosphate uridylyltransferase; UDPG phosphorylase; UDPG pyrophosphorylase; uridine 5'-diphosphoglucose pyrophosphorylase; uridine diphosphoglucose pyrophosphorylase; uridine diphosphate-D-glucose pyrophosphorylase; uridine-diphosphate glucose pyrophosphorylase; EC 2.7.7.9; 9026-22-6. Enzyme Commission Number: EC 2.7.7.9. CAS No. 9026-22-6. UDPG pyrophosphorylase. Activity: > 50 units/mg protein. Storage: -20°C. Form: Lyophilized, sulfate-free powder containing Citrate buffer salt. Source: Baker's yeast. UDP glucose pyrophosphorylase; glucose-1-phosphate uridylyltransferase; UDPG phosphorylase; UDPG pyrophosphorylase; uridine 5'-diphosphoglucose pyrophosphorylase; uridine diphosphoglucose pyrophosphorylase; uridine diphosphate-D-glucose pyrophosphorylase; uridine-diphosphate glucose pyrophosphorylase; EC 2.7.7.9; 9026-22-6. Cat No: NATE-0728. | |
| 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 Basidiomycetes sp. Driselase | Driselase is a cell wall degrading enzyme that contains cellulase, hemicellulase, pectinase etc. Therefore, it is very effective in removing plant cell walls to make protoplasts. Applications: Driselase from basidiomycetes has been used in a study to assess the digestion by fungal glycanases of arabinoxylans with different feruloylated side-chains. driselase from basidiomycetes has also been used in a study to investigate the purification, characterization, and mode of action of a rhamnogalacturonan hydrolase. the enzyme from creative enzymes has been used as a control while testing the ability of p-coumaroyl esterase to release p-coumaroyl and feruloyl groups from intact cell walls. it has also been used in the protoplast preparation from mycelia during a study to investigate the pathogenicity of cochliobolus carbonum on maize. Group: Enzymes. Synonyms: Driselase; 85186-71-6. CAS No. 85186-71-6. Driselase. Storage: 2-8°C. Source: Basidiomycetes sp. Driselase; 85186-71-6. Cat No: NATE-0207. | |
| Native β-hemolytic Streptococcus Streptokinase | Streptokinase (SK) is an enzyme secreted by several species of streptococci that can bind and activate human plasminogen. SK is used as an effective and inexpensive thrombolysis medication in some cases of myocardial infarction (heart attack) and pulmonary embolism. Streptokinase belongs to a group of medications known as fibrinolytics, and complexes of streptokinase with human plasminogen can hydrolytically activate other unbound plasminogen by activating through bond cleavage to produce plasmin. There are three domains to Streptokinase, denoted α (residues 1-150), β (residues 151-287), and γ (residues 288-414). Each domain binds plasminogen, altho...bral hemorrhage. streptokinase is also used in the treatment of complicated parapneumonic effusions and empyema where adverse reactions, allergic type, are rare. streptokinase has been used in a study to compare primary coronary intervention and thrombolytic therapy in my ocardial infarction patients. Group: Enzymes. Synonyms: Streptokinase; SK; EC 3.4.99.0; 9002-01-1. Enzyme Commission Number: EC 3.4.99.0. CAS No. 9002-1-1. SK. Activity: > 3,500 units/mg solid. Storage: -20°C. Form: Lyophilized powder containing ~50% total protein by biuret and sodium glutamate. Total protein composed of enzyme protein and human serum albumin. Source: β-hemolytic Streptococcus | |
| Native Bjerkandera adusta Peroxidase | The transformation of industrial dyes by manganese peroxidases from Bjerkandera adusta is a manganese-independent reaction. Applications: Peroxidase is isolated from bjerkandera adusta. peroxidases from b. adusta, a white rot fungus, is used to degrade synthetic dyes. peroxidase is used in bi ochemistry applications such as western blots, elisa and immunohist ochemistry. peroxidases are used to amplify a weak signal and increase detectability of a target molecule, such as a protein2. peroxidase is commonly used to determine amounts of glucose and peroxides in solution. Group: Enzymes. Synonyms: Peroxidases; lactoperoxidase; guaiacol peroxidase; plant peroxidase; Japanese radish peroxidase; horseradish peroxidase (HRP); soybean peroxidase (SBP); extensin peroxi. Enzyme Commission Number: EC 1.11.1.7. CAS No. 9003-99-0. Peroxidase. Activity: > 2.8 units/mg. Storage: -20°C. Source: Bjerkandera adusta. Peroxidases; lactoperoxidase; guaiacol peroxidase; plant peroxidase; Japanese radish peroxidase; horseradish peroxidase (HRP); soybean peroxidase (SBP); extensin peroxidase; heme peroxidase; oxyperoxidase; protoheme peroxidase; pyrocatechol peroxidase; scopoletin peroxidase; Coprinus cinereus peroxidase; Arthromyces ramosus peroxidase; EC 1.11.1.7; 9003-99-0. Pack: Bottomless glass bottle. Contents are inside inserted fused cone. Cat No: NATE-0549. | |
| Native Bothrops atrox Phosphodiesterase I | Phosphodiesterase I breaks phosphodiester bonds and catalyzes the hydrolysis of various nucleotide polyphosphates. Phosphodiesterase I is released from eucaryotic plasma membranes by phosphatidylinositol-specific phospholipase C. Group: Enzymes. Synonyms: Phosphodiesterase I; EC 3.1.4.1; 5'-exonuclease; 5'-phosphodiesterase; 5'-nucleotide phosphodiesterase; oligonucleate 5'-nucleotidohydrolase; 5' nucleotide phosphodiesterase/alkaline phosphodiesterase I; 5'-NPDase; 5'-PDase; 5'-PDE; 5'NPDE; alkaline phosphodiesterase; nucleotide pyrophosphatase/phosphodiesterase I; orthophosphoric diester phosphohydrolase; PDE I; phosphodiesterase; exonuclease I. Enzyme Commission Number: EC 3.1.4.1. CAS No. 9025-82-5. PDE. Activity: > 0.01 unit/mg solid. Storage: -20°C. Form: crude dried venom. Source: Bothrops atrox. Phosphodiesterase I; EC 3.1.4.1; 5'-exonuclease; 5'-phosphodiesterase; 5'-nucleotide phosphodiesterase; oligonucleate 5'-nucleotidohydrolase; 5' nucleotide phosphodiesterase/alkaline phosphodiesterase I; 5'-NPDase; 5'-PDase; 5'-PDE; 5'NPDE; alkaline phosphodiesterase; nucleotide pyrophosphatase/phosphodiesterase I; orthophosphoric diester phosphohydrolase; PDE I; phosphodiesterase; exonuclease I. Cat No: NATE-0511. | |
| Native Bothrops atrox snake Defibrase | The medicine Defibrase is the trade name given to batroxobin and is isolated from the venom of Bothrops moojeni. It functions as an defibrinogenating agent and is used for patients with thrombosis. The batroxobin from the snake Bothrops atrox is patented as Reptilase and used as a hemostatic drug. Group: Enzymes. Synonyms: Defibrase; batroxobin; reptilase. Purity: Purity (SDS-PAGE): No band other than 31000-41000 Purity (HPLC): > 90.0%. Defibrase. Activity: pecific activity(CP): > 1,200 units / mg protein. Appearance: White lyophilized powder. Storage: Store in an airtight container, protect from light, at a temperature of < 10°C. Form: Freeze dried powder. Source: Bothrops atrox snake. Defibrase; batroxobin; reptilase. Cat No: PHAM-176. | |
| Native Bovine Acid Phosphatase, Prostatic | Acid phosphatases (APase) are a family of enzymes that non-specifically catalyze the hydrolysis of monoesters and anhydrides of phosphoric acid to produce inorganic phosphate at an optimum pH of 4 to 7. Acid phosphatase from potatoes is a 111 kDa diner consisting of two subunits at 41 and 35 kDa. This phosphatase has also been shown to cleave DNA. Group: Enzymes. Synonyms: acid phosphatase; 9001-77-8; acid phosphomonoesterase; phosphomonoesterase; glycerophosphatase; acid monophosphatase; acid phosphohydrolase; acid phosphomonoester hydrolase; uteroferrin; acid nucleoside diphosphate phosphatase; orthophosphoric-monoester phosphohydrolase (acid optimum); EC 3.1.3.2; APase. Enzyme Commission Number: EC 3.1.3.2. CAS No. 9001-77-8. Apase. Activity: ~10 units/g solid. Storage: -20°C. Form: Partially purified, lyophilized powder. Source: Bovine prostate. Species: Bovine. acid phosphatase; 9001-77-8; acid phosphomonoesterase; phosphomonoesterase; glycerophosphatase; acid monophosphatase; acid phosphohydrolase; acid phosphomonoester hydrolase; uteroferrin; acid nucleoside diphosphate phosphatase; orthophosphoric-monoester phosphohydrolase (acid optimum); EC 3.1.3.2; APase. Cat No: NATE-0081. | |
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