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| Product | Description | |
|---|---|---|
| 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 Cystathionine-β-synthase | Cystathionine-β-synthase, also known as CBS, is an enzyme (EC 4.2.1.22) that in humans is encoded by the CBS gene. CBS uses the cofactor pyridoxal-phosphate (PLP) and can be allosterically regulated by effectors such as the ubiquitous cofactor S-adenosyl-L-methionine (adoMet). This enzyme belongs to the family of lyases, to be specific, the hydro-lyases, which cleave carbon-oxygen bonds. CBS is a multidomain enzyme composed of an N-terminal enzymatic domain and two CBS domains. The CBS gene is the most common locus for mutations associated with homocystinuria. Human cbs performs a crucial step in the biosynthetic pathway of cysteine by providing a regulatory control po...nates methyl groups to a variety of substrates, e.g., neurotransmitters, proteins, and nucleic acids. in mammals, cbs is a highly regulated enzyme, which contains a heme cofactor that functions as a redox sensor, that can modulate its activity in response to changes in the redox potential. if the resting form of cbs in the cell has ferrous heme, the potential exists for activating the enzyme under oxidizing conditions by conversion to the ferric state. Group: Enzymes. Synonyms: Cystathionine-β-synthase; CBS; EC 4.2.1.22; 9023-99-8. Enzyme Commission Number: EC 4.2.1.22. CAS No. 9023-99-8. CBS. Cystathionine-β-synthase; CBS; EC 4.2.1.22; 9023-99-8. Cat No: DIA-272. | |
| Native Dactylium dendroides Galactose Oxidase | Galactose oxidase is an extracellular copper-containing enzyme, secreted by the deuteromycete fungus Dactylium dendroides. It catalyzes the oxidation of a range of primary alcohols, including D-galactose, to the corresponding aldehyde, with reduction of oxygen to hydrogen peroxide. Galactose oxidase is an extracellular copper-containing enzyme, secreted by the deuteromycete fungus dactylium dendroides. it catalyzes the oxidation of a range of primary alcohols, including d-galactose, to the corresponding aldehyde, with reduction of oxygen to hydrogen peroxide. Applications: Galactose oxidase may be used as an analytical tool for the specific determination of d-galactose in blood plasma, plant extracts, and phospholipids. it could be used for the characterization of terminal d-galactoside units in several polymers. it may also be useful in the determination of lactose. Group: Enzymes. Synonyms: EC 1.1.3.9; D-galactose oxidase; β-galacto. Enzyme Commission Number: EC 1.1.3.9. CAS No. 9028-79-9. Galactose Oxidase. Activity: Type I, 500-1,500 units/mg protein; Type II, > 3000 units/g solid. Storage: -20°C. Form: Type I, Lyophilized, contains buffer salts and stabilizer; Type II, lyophilized powder. Source: Dactylium dendroides. EC 1.1.3.9; D-galactose oxidase; β-galactose oxidase; 9028-79-9; Galactose Oxidase. Cat No: NATE-0273. | |
| Native Dextran | Native Dextran. CAS No. 9004-54-0. Product ID: 4-00633. Mole weight: Mw ~2 million Da. Properties: Tamarind gels in the presence of alcohol and sugar and exhibits sol to gel transition at body temperatures. Removal of the galactose residues affords materials with unique thermal behaviorpresence of alcohol and sugar and exhibits sol to gel transition at body temperatures. Removal of the galactose residues affords materials with unique thermal behavior. Source : ex Tamarind indica. |  |
| Native Diaphorase (NADPH) from Bacillus megaterium | In enzymology, a NADPH dehydrogenase (EC 1.6.99.1) is an enzyme that catalyzes the chemical reaction: NADPH + H+ + acceptor <-> NADP+ + reduced acceptor. The 3 substrates of this enzyme are NADPH, H+, and acceptor, whereas its two products are NADP+ and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with other acceptors. Applications: Useful for enzymatic determination of reduced nadp. Group: Enzymes. Synonyms: NADPH:acceptor oxidoreductase; NADPH2 diaphorase; NADPH diaph. Enzyme Commission Number: EC 1.6.99.1. CAS No. 9001-68-7. Diaphorase. Mole weight: 48 kDa (gel filtration). Activity: More than 5 U/mg solid. Appearance: Yellowish amorphous powder, lyophilized. Storage: At least one year at -20°C. Form: Freeze dried powder. Source: Bacillus megaterium. NADPH:acceptor oxidoreductase; NADPH2 diaphorase; NADPH diaphorase; OYE; diaphorase; dihydronicotinamide adenine dinucleotide phosphate dehydrogenase; NADPH-dehydrogenase; NADPH-diaphorase; NADPH2-dehydrogenase; old yellow enzyme; reduced nicotinamide adenine dinucleotide phosphate dehydrogenase; TPNH dehydrogenase; TPNH-diaphorase; triphosphopyridine diaphorase; triphosphopyridine nucleotide diaphorase; NADPH2 dehydrogenase; NADPH: (acceptor) oxidoreductase; NADPH dehydrogenase; EC 1.6.99.1. Cat No: NATE-1154. | |
| Native Diisopropyl-fluorophosphatase | In enzymology, a diisopropyl-fluorophosphatase (EC 3.1.8.2) is an enzyme that catalyzes the chemical reaction:diisopropyl fluorophosphate + H2O<-> diisopropyl phosphate + fluoride. Thus, the two substrates of this enzyme are diisopropyl fluorophosphate and H2O, whereas its two products are diisopropyl phosphate and fluoride. This enzyme belongs to the family of hydrolases, specifically those acting on ester bonds phosphoric-triester hydrolases. It employs one cofactor, divalent cation. At least one compound, Chelating agent is known to inhibit this enzyme. Group: Enzymes. Synonyms: EC 3.1.8.2, DFPase; tabunase; somanase; organophosphorus acid anhydrolase; organophosphate acid anhydrase; OPA anhydrase; diisopropylphosphofluoridase; dialkylfluorophosphatase; diisopropyl phosphorofluoridate hydrolase; isopropylphosphorofluoridase; diisopropylfluorophosphonate dehaloge. Enzyme Commission Number: EC 3.1.8.2. CAS No. 9032-18-2. DFPase. Activity: > 30 units/mg. EC 3.1.8.2, DFPase; tabunase; somanase; organophosphorus acid anhydrolase; organophosphate acid anhydrase; OPA anhydrase; diisopropylphosphofluoridase; dialkylfluorophosphatase; diisopropyl phosphorofluoridate hydrolase; isopropylphosphorofluoridase; diisopropylfluorophosphonate dehalogenase; 9032-18-2. Pack: Bottomless glass bottle. Contents are inside inserted fused cone. Cat No: NATE-0183. | |
| 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 E. coli 3-Deoxy-D-manno-octulosonate Aldolase | In enzymology, a 3-deoxy-D-manno-octulosonate aldolase (EC 4.1.2.23) is an enzyme that catalyzes the chemical reaction:3-deoxy-D-manno-octulosonate<-> pyruvate + D-arabinose. Hence, this enzyme has one substRate, 3-deoxy-D-manno-octulosonate, and two products, pyruvate and D-arabinose. This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. Group: Enzymes. Synonyms: 2-keto-3-deoxyoctonate aldolase; KDOaldolase; 3-deoxyoctulosonic aldolase; 2-keto-3-deoxyoctonic aldolase; 3-deoxy-D-manno-octulosonic aldolase; 3-deoxy-D-manno-octulosonate D-arabinose-lyase; EC 4.1.2.23; 3-Deoxy-D-manno-octulosonate Aldolase. Enzyme Commission Number: EC 4.1.2.23. CAS No. 9026-95-3. KDOaldolase. Activity: > 1.0 units/mg. Storage: -20°C. Source: E. coli. 2-keto-3-deoxyoctonate aldolase; KDOaldolase; 3-deoxyoctulosonic aldolase; 2-keto-3-deoxyoctonic aldolase; 3-deoxy-D-manno-octulosonic aldolase; 3-deoxy-D-manno-octulosonate D-arabinose-lyase; EC 4.1.2.23; 3-Deoxy-D-manno-octulosonate Aldolase. Cat No: NATE-0363. | |
| Native E. coli Alanine Aminotransferase | Alanine transaminase (ALT) is a transaminase enzyme (EC 2.6.1.2). 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. Group: Enzymes. Synonyms: Alanine transami. Enzyme Commission Number: EC 2.6.1.2. CAS No. 9000-86-6. Purity: > 95% (SDS-PAGE). ALT. Mole weight: 54,479 of subunit deduced from gene sequence. Activity: > 1,000 U/mL. Storage: -20°C. Form: Liquid. Source: E. coli. Alanine transaminase; ALT; EC 2.6.1.2; alanine aminotransferase; ALAT; glutamic-pyruvic transaminase; glutamic-alanine transaminase; GPT; β-alanine aminotransferase; alanine-α-ketoglutarate aminotransferase; alanine-pyruvate aminotransferase; glutamic acid-pyruvic acid transaminase; glutamic-pyruvic aminotransferase; L-alanine aminotransferase; L-alanine transaminase; L-alanine-α-ketoglutarate aminotransferase; pyruvate transaminase; pyruvate-alanine aminotransferase; pyruvate-glutamate transaminase. Cat No: NATE-0064. | |
| Native E.coli Galactose 1-Dehydrogenase | In enzymology, a galactose 1-dehydrogenase (EC 1.1.1.48) is an enzyme that catalyzes the chemical reaction: D-galactose + NAD+ rightleftharpoons D-galactono-1,4-lactone + NADH + H+. Thus, the two substrates of this enzyme are D-galactose and NAD+, whereas its 3 products are D-galactono-1,4-lactone, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in galactose metabolism. Dehydrogenase that catalyzes the oxidation of galactose to d-galactono-1,4-lactone. rely on the proven diagnostic quality of this recombinant enzyme. Applications: Use galactose 1-dehydrogenase in diagnostic tests for the determination of total galactose. Group: Enzymes. Synonyms: D-galactose:NAD+ 1-oxidoreductase; D-galactose dehydrogenase; beta-galactose dehydrogenase; NAD+-dependent D-galactose dehydrogenase; galactose 1-dehy. CAS No. 9028-54-0. Galactose dehydrogenase. Activity: >50 U/mg. Stability: At +2 to +8°C within specification range for 12 months. Appearance: White lyophilizate. Source: E.coli. D-galactose:NAD+ 1-oxidoreductase; D-galactose dehydrogenase; beta-galactose dehydrogenase; NAD+-dependent D-galactose dehydrogenase; galactose 1-dehydrogenase; EC 1.1.1.48; Galactose dehydrogenase; Galactose 1-Dehydrogenase. Cat No: NATE-0979. | |
| Native E. coli Inorganic Pyrophosphatase | Pyrophosphatase (or inorganic pyrophosphatase) is an enzyme (EC 3.6.1.1) that catalyzes the conversion of one molecule of pyrophosphate to two phosphate ions. This is a highly exergonic reaction, and therefore can be coupled to unfavorable biochemical transformations in order to drive these transformations to completion. The functionality of this enzyme plays a critical role in lipid metabolism (including lipid synthesis and degradation), calcium absorption and bone formation, and DNA synthesis,as well as other biochemical transformations. Applications: Increasing rna yield in transcription reaction; enhancing dna replication. Group: Enzymes. Synonyms: Pyrophosphate phosphohydrolase; inorganic pyrophosphatase; EC 3.6.1.1; 9024-82-2; iphosphate phosphohydrolase. CAS No. 9024-82-2. Inorganic pyrophosphatase. Form: 20 mM Tris-HCl, 100 mM NaCl, 1 mM Dithiothreitol, 0.1 mM EDTA, 50% Glycerol, pH 8.0 25°C. Store at -20°C. Source: E. coli. Pyrophosphate phosphohydrolase; inorganic pyrophosphatase; EC 3.6.1.1; 9024-82-2; iphosphate phosphohydrolase. Cat No: NATE-1272. | |
| Native E. coli N-Carbamoylsarcosine Amidase | In enzymology, a N-carbamoylsarcosine amidase is an enzyme that catalyzes the chemical reaction: N-carbamoylsarcosine + H2O rightleftharpoons sarcosine + CO2 + NH3. Thus, the two substrates of this enzyme are N-carbamoylsarcosine and H2O, whereas its 3 products are sarcosine, CO2, and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. This enzyme participates in arginine and proline metabolism. Hydrolase that catalyzes the interconversion of n-carbamoylsarcosine to sarcosine. Applications: Use n-carbamoylsarcosine amidase in diagnostic tests for the determination of creatinine in combination with creatinine deaminase, n-methylhydantoinase (atp-hydrolysing) and sarcosine oxidase. Group: Enzymes. Synonyms: N-carbamoylsarcosine amidase; N-carbamoylsarcosine amidohydrolase; carbamoylsarcosine amidase. CAS No. 92767-52-7. N-Carbamoylsarcosine Amidase. Activity: 0.80-1.30 U/mg. Stability: At -15 to -25°C within specification range for 12 months. Store dry. Protect from light. Appearance: White lyophilizate. Source: E. coli. Species: E. coli. N-carbamoylsarcosine amidase; N-carbamoylsarcosine amidohydrolase; carbamoylsarcosine amidase. Cat No: NATE-0876. | |
| Native E. coli PreScission Protease | PreScission Protease is a fusion protein of glutathione S-transferase (GST) and human rhinovirus (HRV) type 14 3C protease. The protease specifically recognizes a subset of sequences which include the core amino acid sequence Leu-Phe-Gln/Gly-Pro cleaving between the Gln and Gly residues. Substrate recognition and cleavage are likely to be dependent not only upon primary structural signals, but also upon the secondary and tertiary structures of the fusion protein as well. Applications: During cleavage reactions, it is recommended that samples be removed at various time points and analyzed by sds-page to estimate the yield, purity, and extent of digestion. the amount of prescission protease, temperature and length of incubation required for complete digestion of a given gst fusion partner may vary depending on the fusion partner. optimal conditions for each fusion should be determined in pilot experiments. digestion may be improved by adding triton x-100, tween 20, nonidet, or np40 to a concentration of 0.01%. concentrations of these detergents up to 1% do not inhibit prescission protease. Group: Enzymes. Synonyms: . Purity: >90% by SDS-PAGE. PSP. Activity: >10000 IU/mg. Appearance: Sterile colorless liquid. Storage: Should be stored in small aliquots at -20°C to -80°C for long term. Source: E. coli. PreScission Protease; PSP. Cat No: NATE-0877. | |
| Native E. coli RNA Polymerase, Holoenzyme | E. coli RNA Polymerase, Holoenzyme is the core enzyme saturated with sigma factor 70. The Holoenzyme initiates RNA synthesis from sigma 70 specific bacterial and phage promoters. E. coli RNA Polymerase, Core Enzyme consists of 5 subunits designated α, α, β?, β, and &omega. The enzyme is free of sigma factor and does not recognize any specific bacterial or phage DNA promoters. The enzyme retains the ability to transcribe RNA from nonspecific initiation sequences. Addition of sigma factors will allow the enzyme to initiate RNA synthesis from specific bacterial and phage promoters. Applications: Rna synthesis from e. coli promoter transcription initiation studies in vitro translation with purexpress. Group: Enzymes. Synonyms: E. coli RNA Polymerase, Holoenzyme; E. coli RNA Polymerase; RNA Polymerase; RNAP; RNApol; DNA-dependent RNA polymerase. RNAP. Mole weight: 400 kDa. Storage: at -20°C. Form: 20 mM Tris-HCl, pH 7.5, 100 mM NaCl, 0.1 mM EDTA, 1 mM dithiothreitol (DTT) and 50% glycerol. Source: E. coli. E. coli RNA Polymerase, Holoenzyme; E. coli RNA Polymerase; RNA Polymerase; RNAP; RNApol; DNA-dependent RNA polymerase. Cat No: NATE-1262. | |
| Native E.coli Sarcosine Oxidase | Oxidoreductase that catalyzes the demethylation of sarcosine to glycine. Use Sarcosine Oxidase in your preferred creatinine reagent mix and rely on the proven diagnostic quality of this product. Applications: Use sarcosine oxidase in diagnostic tests for the determination of creatinine. this can be done using one of two methods: (1) in combination with creatinase and creatininase. (2) in combination with creatinine deaminase, n-carbamoylsarcosine amidase and n-methylhydantoinase (atp-hydrolyzing). Group: Enzymes. Synonyms: Sarcosine Oxidase; SAO. CAS No. 9029-22-5. SAO. Mole weight: 40 kD. Activity: 22-40 U/mg lyophilizate; >45 U/mg protein. Stability: At -15 to -25°C within specification range for 12 months. Store dry. Protect from light. Appearance: Yellow lyophilizate. Source: E. coli. Sarcosine Oxidase; EC 1.5.3.1; SAO. Cat No: DIA-290. | |
| Native E. coli Transketolase | Transketolase is highly specific for ketol donor substrates and is stereospecific and enantioselective to hydroxyaldehyde substrates with an (R) configuration. It specifically catalyzes the irreversible transfer of one ketol unit from α-hydroxypyruvic acid to an aldehyde to produce a D-threo (3S,4R)ketose. Applications: Transketolase is widely used in organic synthesis. Group: Enzymes. Synonyms: Transketolase; EC 2.2.1.1; 9014-48-6; glycolaldehydetransferase; Glycolaldehyde Transferase. Enzyme Commission Number: EC 2.2.1.1. CAS No. 9014-48-6. Transketolase. Activity: > 0.1 units/mg. Storage: -20°C. Source: E. coli. Transketolase; EC 2.2.1.1; 9014-48-6; glycolaldehydetransferase; Glycolaldehyde Transferase. Cat No: NATE-0716. | |
| Native Electrophorus electricus (electric eel) Acetylcholinesterase | Acetylcholinesterase, also known as AChE or acetylhydrolase, is a hydrolase that hydrolyzes the neurotransmitter acetylcholine. AChE is found at mainly neuromuscular junctions and cholinergic brain synapses, where its activity serves to terminate synaptic transmission. It belongs to carboxylesterase family of enzymes. It is the primary target of inhibition by organophosphorus compounds such as nerve agents and pesticides. Type vi-s, lyophilized powder, 200-1000 units/mg protein; type v-s, lyophilized powder, > 1000 units/mg protein. Applications: The enzyme has been used as a reference to to evaluate the effect of aspartame metabolites on hippocampal acetylcholinesterase activity. the enzyme has also been used in immobilization studies for the rapid detection of acetylthiocholine chloride. Group: Enzymes. Synonyms: true c. Enzyme Commission Number: EC 3.1.1.7. CAS No. 9000-81-1. Acetylcholinesterase. Mole weight: 280 kDa. Activity: > 1 ,000 units/mg protein; 200-1 ,000 units/mg protein. Storage: -20°C. Form: lyophilized powder. Source: Electrophorus electricus (electric eel). true cholinesterase; choline esterase I; cholinesterase; acetylthiocholinesterase; acetylcholine hydrolase; acetyl; β-methylcholinesterase; AcCholE; EC 3.1.1.7; 9000-81-1; Acetylcholinesterase; AChE; acetylhydrolase. Cat No: NATE-0018. | |
| Native Elizabethkingia meningoseptica PNGase F | In enzymology, a peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase (EC 3.5.1.52) is an enzyme that catalyzes a chemical reaction that cleaves a N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. Applications: Used to deglycosylate protein. proteomics grade pngase f has been extensively purified and lyophilized from dilute potassium phosphate buffer to prod...eptidase; N-glycanase; glycopeptidase; Jack-bean glycopeptidase; PNGase A; PNGase F; glycopeptide N-glycosidase; peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase; EC 3.5.1.52; PNGase F; 83534-39-8. Enzyme Commission Number: EC 3.5.1.52. CAS No. 83534-39-8. Purity: > 95% (SDS-PAGE). PNGase F. Mole weight: ~36 kDa. Storage: 2-8°C. Source: Elizabethkingia meningoseptica. glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; glycopeptidase; Jack-bean glycopeptidase; PNGase A; PNGase F; glycopeptide N-glycosidase; peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase; EC 3.5.1.52; PNGase F; 83534-39-8. Cat No: NATE-0601. | |
| Native Elizabethkingia miricola PNGase F | In enzymology, a peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase (EC 3.5.1.52) is an enzyme that catalyzes a chemical reaction that cleaves a N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. Applications: Used to deglycosylate protein. Group: Enzymes. Synonyms: glycopeptide N-glycosida. Enzyme Commission Number: EC 3.5.1.52. CAS No. 83534-39-8. PNGase F. Mole weight: 36 kDa. Activity: > 20,000 units/mg protein and > 5,000 units/ml. Stability: The product remains active for at least 12 months when stored properly. Exposure for several days to ambient temperatures will not reduce activity. Do Not Freeze. Storage: 2-8°C. Form: Supplied as a solution in 20 mM Tris HCl, pH 7.5, 50 mM NaCl and 1 mM EDTA. Source: Elizabethkingia miricola. glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; glycopeptidase; Jack-bean glycopeptidase; PNGase A; PNGase F; glycopeptide N-glycosidase; peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase; EC 3.5.1.52; PNGase F; 83534-39-8. Cat No: NATE-0602. | |
| Native Enterobacter aerogenes Glycerol Dehydrogenase | Glycerol dehydrogenase is an enzyme in the oxidoreductase family that utilizes the NAD+ to catalyze the oxidation of glycerol to form glycerone (dihydroxyacetone). Applications: Glycerol dehydrogenase was used in the kinetic enzymatic determination of glycerol in wine and beer. Group: Enzymes. Synonyms: EC 1.1.1.6; NAD+-linked glycerol dehydrogenase; glycerol:NAD+ 2-oxidoreductase; GDH; GlDH; GlyDH; 9028-14-2; glycerin dehydrogenase. Enzyme Commission Number: EC 1.1.1.6. CAS No. 9028-14-2. GDH. Activity: 20-80 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing potassium phosphate buffer salts. Source: Enterobacter aerogenes. EC 1.1.1.6; NAD+-linked glycerol dehydrogenase; glycerol:NAD+ 2-oxidoreductase; GDH; GlDH; GlyDH; 9028-14-2; glycerin dehydrogenase. Cat No: NATE-0284. | |
| Native Enterobacter aerogenes myo-Inositol Dehydrogenase | In enzymology, an inositol 2-dehydrogenase (EC 1.1.1.18) is an enzyme that catalyzes the chemical reaction:myo-inositol + NAD+<-> 2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+. Thus, the two substrates of this enzyme are myo-inositol and NAD+, whereas its 3 products are 2,4,6/3,5 pentahydroxycyclohexanone, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in inositol metabolism and inositol phosphate metabolism. Group: Enzymes. Synonyms: myo-inositol 2-dehydrogenase; myo-inositol:NAD+ oxidoreductase; inositol dehydrogenase; myo-inositol dehydrogenase; EC 1.1.1.18; 9028-25-5. Enzyme Commission Number: EC 1.1.1.18. CAS No. 9028-25-5. myo-Inositol Dehydrogenase. Activity: > 10 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing buffer salts and stabilizers. Source: Enterobacter aerogenes. myo-inositol 2-dehydrogenase; myo-inositol:NAD+ oxidoreductase; inositol dehydrogenase; myo-inositol dehydrogenase; EC 1.1.1.18; 9028-25-5. Cat No: NATE-0467. | |
| Native Enterobacter cloacae β-Lactamase | β--lactamase inactivates β-lactam antibiotics by breaking open the β-lactam ring. Protein determined by biuret. Applications: Β-lactamase is used to inactivate β-lactam antibiotics by breaking open the β-lactam ring. β-lactamase is used to study antibiotic resistance and resistance suppression1. this product is produced from enterobacter cloacae. Group: Enzymes. Synonyms: β-lactamase; penicillinase; cephalosporinase; neutrapen; penicillin β-lactamase; exopenicillinase; ampicillinase; penicillin amido-β-lactamhydrolase; penicillinase I, II; β-lactamase I-III; β-lactamase A, B, C; β-lactamase AME I; cephalosporin-β-lactamase; EC . Enzyme Commission Number: EC 3.5.2.6. CAS No. 9073-60-3. β-Lactamase. Activity: 6-18 units/mg protein (using benzylpenicillin); 0.2-0.6 units/mg protein (using benzylpenicillin). Storage: 2-8°C. Form: Lyophilized powder containing sodium phosphate and sodium Citrate buffer salts. Source: Enterobacter cloacae. β-lactamase; penicillinase; cephalosporinase; neutrapen; penicillin β-lactamase; exopenicillinase; ampicillinase; penicillin amido-β-lactamhydrolase; penicillinase I, II; β-lactamase I-III; β-lactamase A, B, C; β-lactamase AME I; cephalosporin-β-lactamase; EC 3.5.2.6; 9073-60-3. Cat No: NATE-0774. | |
| Native environmental DNA α-Fucosidase | In enzymology, an alpha-L-fucosidase (EC 3.2.1.51) is an enzyme that catalyzes the chemical reaction:an alpha-L-fucoside + H2O<-> L-fucose + an alcohol. Thus, the two substRates of this enzyme are alpha-L-fucoside and H2O, whereas its two products are L-fucose and alcohol. This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O-and S-glycosyl compounds. This enzyme participates in n-glycan degradation and glycan structures-degradation. Group: Enzymes. Synonyms: alpha-L-fucoside fucohydrolase; alpha-fucosidase; EC 3.2.1.51; alpha-L-fucosidase. Enzyme Commission Number: EC 3.2.1.51. CAS No. 9037-65-4. FUCA. Source: Proprietary environmental DNA. Species: environmental DNA. alpha-L-fucoside fucohydrolase; alpha-fucosidase; EC 3.2.1.51; alpha-L-fucosidase. Cat No: NATE-0749. | |
| Native Environmental DNA Pustulanase (β-glucanase) | A thermostable β-1,6-endoglucanase or pustulanase (E.C. 3.2.1.75) which catalyses the cleavage of β-1,6 bonds in pustulan and other beta-glucans containing 1,6 linked glucose units. The enzyme is now a component in a standard assay for beta-glucan from Bakers yeast as documented in US Pharmacopeia Food and Chemicals Index. Group: Enzymes. Synonyms: EC 3.2.1.75; glycoside hydrolase; pustulanase; glucan endo-1,6-β-glucosidase; 6-β-D-glucan glucanohydrolase; endo-1,6-β-glucanase; β-1?6)-β-D-glucanase; β-1,6-glucanase-pustulanase; β-1,6-glucan hydrolase; β-1,6-glucan 6-glucanohydrolase; 1,6-β-D-glucan glucanohydrolase. Enzyme Commission Number: EC 3.2.1.75. CAS No. 37278-39-0. Pustulanase. Source: Proprietary metagenome environmental DNA. Species: Environmental DNA. EC 3.2.1.75; glycoside hydrolase; pustulanase; glucan endo-1,6-β-glucosidase; 6-β-D-glucan glucanohydrolase; endo-1,6-β-glucanase; β-1?6)-β-D-glucanase; β-1,6-glucanase-pustulanase; β-1,6-glucan hydrolase; β-1,6-glucan 6-glucanohydrolase; 1,6-β-D-glucan glucanohydrolase. Cat No: NATE-0645. | |
| Native Equine Butyrylcholinesterase | Butyrylcholinesterase (BChE) is a serine hydrolase that is structurally similar to acetylcholinesterase (AChE), but differs in substRate specificities and inhibitor sensitivities. BChE can, unlike AChE, efficiently hydrolyze larger esters of choline such as butyrylcholine and benzoylcholine. The enzyme is a tetrameric glycoprotein with four equal subunits (110 kDa each). The enzyme is activated by Ca2+ and Mg2+ and the activity is constant over the pH range 6.0-8.0. It is inhibited by Betaine, nicotine, organophosphates, carbamates. This product is prepared from equine serum using ammonium sulfate fractionation and supplied as a lyophilized powder. Applications: Butyrylchol...vestigations into selective inhibitors may provide a clearer picture of the physiological role of bche in both healthy and diseased individuals. this product has been used for the screening of cholineesterase inhibitors in selected fruits and vegetables, for restoring cognitive function and improving memory. it has also been used to develop a butyrylcholinesterase and choline oxidase immobilized bio-sniffer for the detection of nicotine. nicotine inhibits bche activity. a decrease in the byproducts of bche activity reflects the volume of nicotine. Group: Enzymes. Synonyms: Butyrylcholinesterase; BCHE; BuChE; pseudocholinesterase; plasma cholinesterase; EC 3.1.1.8; 9001-08-5; | |
| Native Equine Ferritin | Ferritin is a highly specialized protein whose main function is to store excess iron intracellularly. It is widely distributed throughout the animal and plant kingdoms. In mammalian tissues, ferritin is present in concentrated form in spleen, liver and the intestinal mucosa. Ferritin is not a structurally homogeneous protein since purified preparations, when examined by polyacrylamide gel electrophoresis, show multiple bands. Immunologically, ferritins appear to be species specific but not organ specific. Iron: 30% (bipyridyl method). Group: Others. Purity: Not less than 90% as determined by electrophoresis on 4% polyacrylamide gels. Storage: Store at 4° C; Do not freeze. Form: Saline buffer. Source: Equine Spleen. Species: Equine. Ferritin. Cat No: NATE-1876. | |
| Native Equine γ-Glutamyltranspeptidase | γ-glutamyl transferase is an enzyme that transfers gamma-glutamyl functional groups. It is found in many tissues, the most notable one being the liver, and has significance in medicine as a diagnostic marker. GGT catalyzes the transfer of the gamma-glutamyl moiety of glutathione to an acceptor that may be an amino acid, a peptide or water (forming glutamate). GGT plays a key role in the gamma-glutamyl cycle, a pathway for the synthesis and degradation of glutathione and drug and xenobiotic detoxification. Other lines of evidence indicate that GGT can also exert a prooxidant role, with regulatory effects at various levels in cellular signal transduction and cellular pathophysiology. Group: Enzymes. Synonyms: EC 2.3.2.2; glutamyl transpeptidase; α-glutamyl transpeptidase; . Enzyme Commission Number: EC 2.3.2.2. CAS No. 9046-27-9. γ-GT. Activity: 5-12 units/mg solid. Storage: -20°C. Source: Equine kidney. Species: Equine. EC 2.3.2.2; glutamyl transpeptidase; α-glutamyl transpeptidase; γ-glutamyl peptidyltransferase; γ-glutamyl transpeptidase (ambiguous); γ-GPT; γ-GT; γ-GTP; L-γ-glutamyl transpeptidase; L-γ-glutamyltransferase; L-glutamyltransferase; GGT (ambiguous); γ-glutamyltranspeptidase (ambiguous); γ-glutamyltransferase; 9046-27-9; GGTP. Cat No: NATE-0791. | |
| Native Equine Glutathione S-Transferase | Glutathione S-transferases are a family of proteins that catalyze the conjugation of reduced glutathione with a variety of hydrophobic chemicals containing electrophilic centers. Group: Enzymes. Synonyms: EC 2.5.1.18; glutathione S-transferase; glutathione S-alkyltransferase; glutathione S-aryltransferase; S-(hydroxyalkyl)glutathione lyase; glutathione S-aralkyltransferase; glutathione S-alkyl transferase; GST; 50812-37-8. Enzyme Commission Number: EC 2.5.1.18. CAS No. 50812-37-8. Glutathione S-Transferase. Mole weight: mol wt 45-50 kDa. Activity: > 25 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Tris and phosphate buffer salts, reduced glutathione and EDTA. Source: Equine liver. Species: Equine. EC 2.5.1.18; glutathione S-transferase; glutathione S-alkyltransferase; glutathione S-aryltransferase; S-(hydroxyalkyl)glutathione lyase; glutathione S-aralkyltransferase; glutathione S-alkyl transferase; GST; 50812-37-8. Cat No: NATE-0325. | |
| Native Equine Spleen Apoferritin | Native apo-ferritin from equine spleen is a native protein shell of ferritin molecule lacking iron. Group: Enzymes. Synonyms: Ferritin, Apo-; Apoferritin; Ferritin; Apo-Ferritin; Apo ferritin. CAS No. 9013-31-4. Purity: 0.95. Storage: Store at -20° C. Form: Freeze-dried powder. Source: Equine Spleen. Species: Equine. Ferritin, Apo-; Apoferritin; Ferritin; Apo-Ferritin; Apo ferritin. Cat No: NATE-1873. | |
| Native Escherichia coli Acetate Kinase | In molecular biology, acetate kinase (EC 2.7.2.1), which is predominantly found in micro-organisms, facilitates the production of acetyl-CoA by phosphorylating acetate in the presence of ATP and a divalent cation. Short-chain fatty acids (SCFAs) play a major role in carbon cycle and can be utilized as a source of carbon and energy by bacteria. The enzyme is important in the process of glycolysis, enzyme levels being increased in the presence of excess glucose. The growth of a bacterial mutant lacking acetate kinase has been shown to be inhibited by glucose, suggesting that the enzyme is involved in excretion of excess carbohydRate. A related enzyme, butyRate kinase, facili...rom escherichia coli has been used as part of an atp-regenerating system to study the kinetics of agonist-stimulated transphosphatidylatio. Group: Enzymes. Synonyms: Acetate kinase (phosphorylating); Acetic kinase; Acetokinase; AK; EC 2.7.2.1; 9027-42-3; Acetate kinase. Enzyme Commission Number: EC 2.7.2.1. CAS No. 9027-42-3. Acetate kinase. Activity: > 150 units/mg protein (biuret). Storage: -20°C. Form: Lyophilized powder containing trehalose with small amounts of potassium phosphate, magnesium chloride, and dithiothreitol. Source: Escherichia coli. Acetate kinase (phosphorylating); Acetic kinase; Acetokinase; AK; EC 2.7.2.1; 9027-42-3; Acetate kinase. Cat No: NATE-0017. | |
| Native Escherichia coli Alkaline Phosphatase | Alkaline phosphatase (ALP, ALKP, ALPase, Alk Phos) (EC 3.1.3.1) is a hydrolase enzyme responsible for removing phosphate groups from many types of molecules, including nucleotides, proteins, and alkaloids. The process of removing the phosphate group is called dephosphorylation. As the name suggests, alkaline phosphatases are most effective in an alkaline environment. It is sometimes used synonymously as basic phosphatase. Applications: Alkaline phosphatase is used for conjugation to antibodies and other proteins for elisa, western blotting, and hist ochemical detection. it may be used for protein labeling when high sensitivity is required. Group: Enzymes. Synonyms: Alkaline phosphatase; ALP; ALKP; ALPase; Alk Phos; EC 3.1.3.1; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase. Enzyme Commission Number: EC 3.1.3.1. CAS No. 9001-78-9. ALP. Activity: Type I, >30 units per mg protein; Type II, >20 units per mg protein; Type III, >10 units per mg protein. Storage: 2-8°C. Form: A suspension in 2.6M ammonium sulfate, pH 8.0. Source: Escherichia coli. Alkaline phosphatase; ALP; ALKP; ALPase; Alk Phos; EC 3.1.3.1; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase. Cat No: NATE-0056. | |
| Native Escherichia coli Apotryptophanase | Apotryptophanase hydrolizes tryptophan and is capable of catalyzing α,β-elimination reactions with a number of substituted amino acids, including S-methyl-, S-ethyl-and S-benzyl-L-cysteine. DTNB inactivates tryptophanase. Applications: Apotryptophanase is used for the quantitative determination of pyridoxal-phosphate. apotryptophanase, from creative enzymes, has been used to study pregnancy-associated plp deficiency and vitamin b-6 deficiency. Group: Enzymes. Synonyms: L-tryptophanase; L-tryptophan indole-lyase (deaminating); TNase; EC 4.1.99.1; 9024-00-4. Enzyme Commission Number: EC 4.1.99.1. CAS No. 9024-00-4. TNase. Activity: 75-150 units/mg solid. Storage: -20°C. Form: soluble powder. Source: Escherichia coli. L-tryptophanase; L-tryptophan indole-lyase (deaminating); TNase; EC 4.1.99.1; 9024-00-4. Cat No: NATE-0706. | |
| Native Escherichia coli Asparaginase | Asparaginase (EC 3.5.1.1, USAN) or Colaspase (BAN) is an enzyme that catalyzes the hydrolysis of asparagine to aspartic acid. Asparaginases are enzymes expressed and produced by microorganisms. Applications: Asparaginase is used in enzymatic assays and to convert asparagine to aspartic acid. asparaginase is used to reduce the formation of acrylamide in starchy food products. it is also used as a chemotherapy agent for acute lymphoblastic leukemia. product is from escherichia coli and is provided as a lyophilized powder containing sodium chloride. Group: Enzymes. Synonyms: EC 3.5.1.1; Asparaginase; Colaspase; L-asparaginase; L-asparagine amidohydrolase. Enzyme Commission Number: EC 3.5.1.1. CAS No. 9015-68-3. Asparaginase. Storage: 2-8°C. Form: lyophilized powder. Source: Escherichia coli. EC 3.5.1.1; Asparaginase; Colaspase; L-asparaginase; L-asparagine amidohydrolase. Cat No: PHAM-226. | |
| Native Escherichia coli β-Galactosidase | β-galactosidase, also called beta-gal or β-gal, is a hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides. Substrates of different β-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. Applications: This enzyme is useful for structural investigation of carbohydrates, the determination of lactose (foodstuff analysis) and as an enzyme label for enzyme immunoassay. Group: Enzymes. Synonyms: β-galactosidase; beta-gal; β-gal; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat; β-D-galactoside galactohydrolase. Enzyme Commission Number: EC 3.2.1.23. CAS No. 9031-11-2. β-gal. Mole weight: 540 kDa. Activity: Grade? 500U/mg-solid or more. Stability: Stable at-20°C for at least 6 months. Appearance: White amorphous powder, lyophilized. Form: Freeze dried powder. Source: Escherichia coli. β-galactosidase; beta-gal; β-gal; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat; β-D-galactoside galactohydrolase. Cat No: DIA-189. | |
| Native Escherichia coli β-Galactosidase-biotin labeled | β-galactosidase is a hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides. Substrates of different β-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. Applications: Β-galactosidase was used as a control antigen in the selection of human antibody fragments by phage display. Group: Enzymes. Synonyms: β-galactosidase; beta-gal; β-gal; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat; β-D-galactoside galactohydrolase. β-gal. Activity: 350-1200 units/mg protein. Form: Lyophilized powder containing Tris-acetate, DTT, MgCl2, and isopropyl β-D-thiogalactopyranoside. Source: E. coli. β-galactosidase; beta-gal; β-gal; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat; β-D-galactoside galactohydrolase; β-Galactosidase-biotin labeled; biotin β-gal. Cat No: NATE-1585. | |
| Native Escherichia coli β-Glucuronidase | β-glucuronidase catalyzes the breakdown of complex carbohydrates. In humans it converts conjugated bilirubin into the unconjugated form, making bilirubin suitable for reabsorption. Type ix-a, 1,000-5,000 units/mg protein; type vii-a, lyophilized powder, 5,000-20,000 units/mg protein. Applications: Β-glucuronidase is used as a reporter gene in gus assays to monitor gene expression. Group: Enzymes. Synonyms: β-glucuronide glucuronohydrolase glucuronidase; exo-β-D-glucuronidase; ketodase; EC 3.2.1.31; 9001-45-0; β-D-glucuronoside glucuronosohydrolase; GUSB. Enzyme Commission Number: EC 3.2.1.31. CAS No. 9001-45-0. GUSB. Form: lyophilized powder. Source: Escherichia coli. β-glucuronide glucuronohydrolase glucuronidase; exo-β-D-glucuronidase; ketodase; EC 3.2.1.31; 9001-45-0; β-D-glucuronoside glucuronosohydrolase; GUSB. Cat No: NATE-0330. | |
| Native Escherichia coli Chloramphenicol Acetyltransferase | Chloramphenicol acetyltransferase (or CAT) is a bacterial enzyme (EC 2.3.1.28) that detoxifies the antibiotic chloramphenicol and is responsible for chloramphenicol resistance in bacteria. This enzyme covalently attaches an acetyl group from acetyl-CoA to chloramphenicol, which prevents chloramphenicol from binding to ribosomes. A histidine residue, located in the C-terminal section of the enzyme, plays a central role in its catalytic mechanism. Applications: Chloramphenicol acetyltransferase from escherichia coli has been used in a study to assess the construction of a novel expression system in klebsiella pneumoniae and its application for 1,3-propanediol produ...etyl-CoA:chloramphenicol 3-O-acetyltransferase; CAT; 9040-07-7; chloramphenicol acetyltransferase; chloramphenicol acetylase; chloramphenicol transacetylase; CAT I; CAT II; CAT III. CAS No. 9040-7-7. Chloramphenicol Acetyltransferase. Mole weight: mol wt 75 kDa (three identical subunits). Activity: 50,000-150,000 units/mg protein (Lowry). Storage: -20°C. Form: Type I, lyophilized powder. Partially purified; contains Tris buffer salts; Type II, buffered aqueous glycerol solution. Clear, colorless solution in 50% glycerol containing 5 mM Tris-HCl, pH 7.8, and 0.5 mM 2-mercaptoethanol. Source: Escherichia coli. Acetyl-CoA:chloramphenicol 3-O-acetyltransferase; CAT; 9 | |
| Native Escherichia coli Diacylglycerol Kinase | Diacylglycerol kinase (DGK or DAGK) is a family of enzymes that catalyzes the conversion of diacylglycerol (DAG) to phosphatidic acid (PA) utilizing ATP as a source of the phosphate. In non-stimulated cells, DGK activity is low allowing DAG to be used for glycerophospholipid biosynthesis but on receptor activation of the phosphoinositide pathway, DGK activity increases driving the conversion of DAG to PA. As both lipids are thought to function as bioactive lipid signaling molecules with distinct cellular targets, DGK therefore occupies an important position, effectively serving as a switch by terminating the signalling of one lipid while simultaneously activating signa...n of dgka and plsb genes of phospholipid synthesis by multiple stress responses in escherichia coli. diacylglycerol kinase from escherichia coli has also been used in a study to identify an alcohol binding site in the first cysteine-rich domain of protein kinase cdelta. Group: Enzymes. Synonyms: Diacylglycerol Kinase; DGK; DAGK; EC 2.7.1.107; Diacylglycerol kinase (ATP); sn-1,2-Diacylglycerol kinase. Enzyme Commission Number: EC 2.7.1.107. CAS No. 60382-71-0. DAGK. Mole weight: mol wt 13.7 kDa. Stability: -70°C. Form: suspension. Source: E. coli. Diacylglycerol Kinase; DGK; DAGK; EC 2.7.1.107; Diacylglycerol kinase (ATP); sn-1,2-Diacylglycerol kinase. Cat No: NATE-0181. | |
| Native Escherichia coli Glutaminase | Glutaminase catalyzes the conversion of glutamine to glutamate. Glutaminase is an amidohydrolase enzyme that generates glutamate from glutamine. Glutaminase has tissue-specific isoenzymes. Glutaminase has an important role in glial cells. Glutaminase catalyzes the following reaction:Glutamine + H2O ? Glutamate + NH3. Group: Enzymes. Synonyms: EC 3.5.1.2; glutaminase I; L-glutaminase; glutamine aminohydrolase; Glutaminase; 9001-47-2. Enzyme Commission Number: EC 3.5.1.2. CAS No. 9001-47-2. Glutaminase. Activity: Type I, 500-1,500 units/mg protein; Type II, 50-200 units/mg protein. Storage: -20°C. Form: Type I, Lyophilized powder containing stabilizer and potassium succinate; Type II, Lyophilized powder containing potassium succinate and EDTA. Source: Escherichia coli. EC 3.5.1.2; glutaminase I; L-glutaminase; glutamine aminohydrolase; Glutaminase; 9001-47-2. Cat No: NATE-0307. | |
| Native Escherichia coli 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. Applications: Glycerol kinase (glpk) was used to study the effects of pain controlling neuropeptides on human fat cell lipolysis. 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: Type I, 50-100 units/mg protein; Type II, 300-600 units/mL. Storage: -20°C. Form: Type I, lyophilized powder, Partially purified lyophilized powder, balance is primarily salts and EDTA; Type II, ammonium sulfate suspension, Suspension in 3.1 M (NH4)2SO4 pH 7.3, with 1% BSA and 2% trehalose. Source: Escherichia coli. EC 2.7.1.30; glycerokinase; GK; ATP:glycerol-3-phosphotransferase; glycerol kinase (phosphorylating); glyceric kinase; 9030-66-4. Cat No: NATE-0288. | |
| Native Escherichia coli L-Arginine Decarboxylase | In enzymology, an arginine decarboxylase (EC 4.1.1.19) is an enzyme that catalyzes the chemical reaction:L-arginine<-> agmatine + CO2. Hence, this enzyme has one substRate, L-arginine, and two products, agmatine and CO2. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. It employs one cofactor, pyridoxal phosphate. Group: Enzymes. Synonyms: arginine decarboxylase; EC 4.1.1.19; 9024-77-5; SpeA; L-arginine carboxylyase; L-Arginine Decarboxylase; ADC. Enzyme Commission Number: EC 4.1.1.19. CAS No. 9024-77-5. ADC. Activity: 5-15 units/mg protein. Storage: -20°C. Source: Escherichia coli. arginine decarboxylase; EC 4.1.1.19; 9024-77-5; SpeA; L-arginine carboxylyase; L-Arginine Decarboxylase; ADC. Cat No: NATE-0033. | |
| Native Escherichia coli L-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. Applications: L-glutamine synthetase may be used for the purification of proteases from escherichia coli. Group: Enzymes. Synonyms: glutamine synthetase; glutamylhydroxamic synthetase; L-glutamine synthetase; glutamate-ammonia ligase; L-Glutamate:ammonia ligase (ADP-forming); EC 6.3.1.2; GS; 9023-70-5. Enzyme Commission Number: EC 6.3.1.2. CAS No. 9023-70-5. Purity: affinity chromatography. GS. Activity: 400-2,000 units/mg protein. Storage: -20°C. Form: lyophilized powder; Contains potassium phosphate, sodium Citrate and magnesium acetate buffer salts. Source: Escherichia coli. glutamine synthetase; glutamylhydroxamic synthetase; L-glutamine synthetase; glutamate-ammonia ligase; L-Glutamate:ammonia ligase (ADP-forming); EC 6.3.1.2; GS; 9023-70-5. Cat No: NATE-0321. | |
| Native Escherichia coli N-Acetylneuraminic Acid Aldolase | In enzymology, a N-acetylneuraminate lyase (EC 4.1.3.3) is an enzyme that catalyzes the chemical reaction:N-acetylneuraminate<-> N-acetyl-D-mannosamine + pyruvate. Hence, this enzyme has one substrate, N-acetylneuraminate, and two products, N-acetyl-D-mannosamine and pyruvate. This enzyme belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. This enzyme participates in aminosugars metabolism. Applications: This enzyme is useful for enzymatic determination of n-acetylneuraminic acid and sialic acid when coupled with the related enzymes in clinical analysis. for industrial use, this enzyme is useful for enzymatic synthe...o. 9027-60-5. NALase. Mole weight: mol wt ~98 kDa. Activity: > 20 units/mg protein (biuret). Storage: -20°C. Form: Lyophilized powder containing potassium phosphate buffer salt. Source: Escherichia coli. N-acetylneuraminic acid aldolase; acetylneuraminate lyase; sialic aldolase; sialic acid aldolase; sialate lyase; N-acetylneuraminic aldolase; neuraminic aldolase; N-acetylneuraminate aldolase; neuraminic acid aldolase; N-acetylneuraminic acid aldolase; neuraminate aldolase; N-acetylneuraminic lyase; N-acetylneuraminic acid lyase; NPL; NALase; NANA lyase; acetylneuraminate pyruvate-lyase; N-acetylneuraminate pyruvate-lyase; 9027-60-5; EC 4.1.3.3. Cat No: NATE-0490. | |
| Native Escherichia coli Nitrate Reductase (cytochrome) | Nitrate reductase (cytochrome) is an enzyme with system name ferrocytochrome:nitrate oxidoreductase. This enzyme catalises the following chemical reaction:2 ferrocytochrome + 2 H+ + nitrate<-> 2 ferricytochrome + nitrite. Group: Enzymes. Synonyms: Nitrate reductase (cytochrome); respiratory Nitrate reductase; benzyl viologen-Nitrate reductase; EC 1.9.6.1; 9029-42-9. Enzyme Commission Number: EC 1.9.6.1. CAS No. 9029-42-9. Nitrate reductase. Activity: > 5 units/g solid. Storage: -20°C. Form: lyophilized powder. Source: Escherichia coli. Nitrate reductase (cytochrome); respiratory Nitrate reductase; benzyl viologen-Nitrate reductase; EC 1.9.6.1; 9029-42-9. Cat No: NATE-0485. | |
| Native Escherichia coli Penicillin Amidase | The biosynthesis of Penicillin amidase in E. coli by hydrophobic protein chromatography is an inducible reaction which is regulated by metabolized carbon source (e.g. polyols, carboxylic acid etc.). It is also influenced by catabolite repression. It catalyzes the formation of amide bonds through an acyl-enzyme intermediate. Penicillin amidase is a periplasmic 80k heterodimer with a and b chains (209 and 566 amino acids, respectively). it is widely distributed among microorganisms, including bacteria, yeast and filamentous fungi. among all the sources, the enzyme produced by e. coli is most well-characterized and common for industrial application. Applications: Penicillin...; benzylpenicillin acylase; novozym 217; semacylase; α-acylamino-β-lactam acylhydrolase; ampicillin acylase; EC 3.5.1.11; 9014-06-6. Enzyme Commission Number: EC 3.5.1.11. CAS No. 9014-6-6. Penicillin Amidase. Mole weight: Mr ~70 kDa. Activity: Type I, 5-10 units/mg protein; Type II, > 10 units/mg protein (E1%/280). Storage: 2-8°C. Form: Type II, ammonium sulfate suspension, Suspension in 0.1 M phosphate, pH 7.5 and 3 M ammonium sulfate. Source: Escherichia coli. penicillin amidase; penicillin acylase; benzylpenicillin acylase; novozym 217; semacylase; α-acylamino-β-lactam acylhydrolase; ampicillin acylase; EC 3.5.1.11; 9014-06-6. Cat No: NATE-0541. | |
| Native Escherichia coli 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. Superoxide dismutases are a group of low molecular weight metalloproteins present in all aerobic cells of plants, animals...5.1.1; 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. Enzyme Commission Number: EC 1.15.1.1. CAS No. 9054-89-1. SOD. Mole weight: mol wt 32.5 kDa. Activity: > 1 ,000 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Tris buffer salts. Source: Escherichia coli. Superoxide dismutases; EC 1.15.1.1; superoxidase dismutase; copper-zinc superoxide dismutase; Cu-Zn superoxide dismutase; ferrisuper | |
| Native Escherichia coli Thioredoxin Reductase | Thioredoxin reductase (TrxR) is an NADPH-dependent oxidoreductase containing one FAD per subunit that reduces the active site disulfide in oxidised thioredoxin (Trx). The molecular weight of the isozymes from mammalian sources vary between 55-67 kDa as compared with 35 kDa in prokaryotes, plants or yeast. The substrate specificity of the mammalian enzyme is much broader than the prokaryotic enzyme reducing both mammalian and E. coli thioredoxins as well as well as non-disulfide substrates such selenite, lipoic acids, lipid hydroperoxides and hydrogen peroxide. Applications: Thioredoxin reductase from escherichia coli can be used in peroxidase-coupled thioredoxin system assay for assessing the peroxidase activitiy of cys-based thiol peroxidases. the product was used for determining the enzymatic activity of his6-ahp1p. Group: Enzymes. Synonyms: NADP-thioredoxi. Enzyme Commission Number: EC 1.8.1.9. CAS No. 9074-14-0. TrxR. Activity: >25 units/mg protein (Bradford). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 3.6 M (NH4)2SO4 containing 30 mM potassium phosphate buffer, pH 7.5, and 2 mM EDTA. Source: Escherichia coli. NADP-thioredoxin reductase; NADPH-thioredoxin reductase; thioredoxin reductase (NADPH); NADPH2:oxidized thioredoxin oxidoreductase; thioredoxin-disulfide reductase; EC 1.8.1.9; TrxR. Cat No: NATE-0718. | |
| Native Fig tree latex Ficin | Ficin is classified as a thiol protease. It contains a single reactive cysteine at its active site. The amino acid homology of the active site is similar to that of papain. Ficin will cleave proteins at the carboxyl side of Gly, Ser, Thr, Met, Lys, Arg, Tyr, Ala, Asn, and Val. The reported Km for the chromogenic substrate pGlu-Phe-Leu-p-nitroanilide is 0.43 mM. Ficin is inhibited by iodoacetamide, iodoacetic acid, N-ethylmaleimide, mercuric chloride, DFP (diisopropyl fluorophosphate), TLCK (Na-p-Tosyl-lysine chloromethyl ketone), and TPCK (N-Tosyl-L-phenylalanine chloromethyl ketone). Ficin can be used to generate high yielding F (ab')2 fragments from mouse IgG1. Group: Enzymes. Synonyms: ficin; debricin; higueroxyl delabarre; EC 3.4.22.3; 9001-33-6; ficain. Enzyme Commission Number: EC 3.4.22.3. CAS No. 9001-33-6. Ficin. Mole weight: 23.8 kDa. Activity: > 1.0 units/mg protein. Form: saline suspension or lyophilized powder. Source: Fig tree latex. ficin; debricin; higueroxyl delabarre; EC 3.4.22.3; 9001-33-6; ficain. Cat No: NATE-0255. | |
| Native Flavobacterium heparinum 2-O-Sulfatase | Hydrolyses the terminal 2-O-sulphate on the unsaturated di-and oligo-saccharides produced by the action of lyases on sulphated glycosaminoglycans. Hydrolyses the terminal 2-o-sulphate on the unsaturated di-and oligo-saccharides produced by the action of lyases on sulphated glycosaminoglycans. Applications: 2-o-sulfatase from flavobacterium heparinum has been used in a study to determine that oversulfated chondroitin sulfate is a contaminant in heparin associated with adverse clinical events. 2-o-sulfatase from flavobacterium heparinum has also been used in a study to determine the structure of oligosaccharides prepared from acharan sulfate. Group: Enzymes. Synonyms: 2-O-Sulfatase. 2-O-Sulfatase. Activity: 10-40 (units/ml). Storage: -20°C. Form: Solution contains 10 mM tris-acetate, pH 7.3, 80 mM NaCl, 10 mM potassium phosphate, 0.2% BSA. Source: Flavobacterium heparinum. 2-O-Sulfatase. Cat No: NATE-0002. | |
| Native Flavobacterium heparinum Chondroitinase AC | Chondroitinase AC from Flavobacterium heparinum is an enzyme that cleaves sulfated and non-sulfated polysaccharide chains with (1-4) linkages between hexosamines and glucuronic acid residues, by an elimination mechanism. The resulting oligosaccharide products are mainly disaccharides with unsatuRated uronic acids. Chondroitinase AC specifically degrades chondroitin sulfates A and C, but not chondroitin sulfate B (dermatan sulfate). Applications: Chondroitinase ac from creative enzymes has been used for the large scale preparation of glycosaminoglycan (gag) fractions during the study of structural and sequence motifs in dermatan sulfate. Group: Enzymes. Synonyms: EC 4.2.2.5; 9047-57-8; chondroitin AC lyase; chondroitinase; chondroitin sulfate lyase; chondroitin AC eliminase; chondroitin AC lyase; chondroitinase AC; ChnAC. Enzyme Commission Number: EC 4.2.2.5. CAS No. 9047-57-8. ChnAC. Activity: 0.5-1.5 units/mg solid (using chondroitin sulfate A as substrate, also cleaves chondroitin sulfate C). Storage: -20°C. Form: lyophilized powder. Source: Flavobacterium heparinum. EC 4.2.2.5; 9047-57-8; chondroitin AC lyase; chondroitinase; chondroitin sulfate lyase; chondroitin AC eliminase; chondroitin AC lyase; chondroitinase AC; ChnAC. Cat No: NATE-0126. | |
| Native Flavobacterium heparinum Chondroitinase B | Chondroitinase B cleaves, via an elimination mechanism, polysaccharide chains containing 1-4 linkages between hexosamines and iduronic acid residues in dermatan sulfate (chondroitin B).The reaction yields oligosaccharide products (mainly disaccharides) containing unsaturated uronic acids which can be detected by UV spectroscopy at 232 nm. Applications: Research reagent (glycobiology, preparation of oligosaccharide libraries from dermatan sulfate).determination of contents of chondrotin sulfates by hplc. Group: Enzymes. Synonyms: Chondroitinase B; EC 4.2.2.19; chondroitin B lyase; ChonB; ChnB. Enzyme Commission Number: EC 4.2.2.19. CAS No. 52227-83-5. ChonB. Mole weight: 55 kDa. Activity: >200 IU/mg (substrate: dermatan sulfate). Stability: 12 months frozen at -20°C in aqueous buffers containing sodium phosphate and sucrose 5%. Source: Flavobacterium heparinum. Chondroitinase B; EC 4.2.2.19; chondroitin B lyase; ChonB; ChnB. Cat No: NATE-1950. | |
| Native Flavobacterium heparinum Chondroitinase C | Chondroitinase C acts upon chondroitin sulfate C, releasing unsatuRated 6-sulfated disaccharides. The enzyme also acts on hyaluronic acid, producing unsatuRated nonsulfated disaccharides. The enzyme is strongly inhibited by NaCl, Fe2+, Co2+ and phosphate ions. Group: Enzymes. Synonyms: EC 4.2.2.x,; 60184-91-0; Chondroitinase C; Chondroitin C lyase. Enzyme Commission Number: EC 4.2.2.x. CAS No. 60184-91-0. Chondroitinase C. Activity: > 200 units/mg solid. Storage: -20°C. Form: lyophilized powder. Source: Flavobacterium heparinum. EC 4.2.2.x,; 60184-91-0; Chondroitinase C; Chondroitin C lyase. Cat No: NATE-0132. | |
| Native Flavobacterium heparinum Heparinase I | In enzymology, a heparin lyase (EC 4.2.2.7) is an enzyme that catalyzes the chemical reaction: Eliminative cleavage of polysaccharides containing 1,4-linked D-glucuronate or L-iduronate residues and 1,4-alpha-linked 2-sulfoamino-2-deoxy-6-sulfo-D-glucose residues to give oligosaccharides with terminal 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends. This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. Group: Enzymes. Synonyms: EC 4.2.2.7; Heparinase I; 9025-39-2; heparin eliminase; heparinase; heparin lyase. Enzyme Commission Number: EC 4.2.2.7. CAS No. 9025-39-2. Heparinase. Mole weight: mol wt 42.8 kDa. Activity: > 200 units/mg protein (enzyme + BSA). Storage: -20°C. Source: Flavobacterium heparinum. EC 4.2.2.7; Heparinase I; 9025-39-2; heparin eliminase; heparinase; heparin lyase. Cat No: NATE-0338. | |
| Native Flavobacterium heparinum Heparinase I and III Blend | Heparin-degrading lyase that recognizes heparin sulfate proteoglycan as its primary substrate. Heparinase I and III plays vital role in various biological processes: modulate cell-growth factor interactions, cell-lipoprotein interactions, neovascularization. It cleaves highly sulphated polysaccharide chains in presence of 2-O-sulfated α-L-idopyranosyluronic acid and β-D-glucopyranosyluronic acid residues of polysaccharides. Heparinase is an inducible, non-extracellular heparin-degrading enzyme. three types of heparinises are produced by flavobacterium heparinum and contains specific sequences of heparin. Applications: Heparinase i and iii may be used for the study of heparin production during fermentation and specific activity of heparinise. Group: Enzymes. Synonyms: Heparinase; Heparin lyase; Heparin eliminase; Heparin-sulfate lyase; Heparin-sulfate eliminase; Heparitin-sulfate lyase; Heparinase I; Heparinase III. Heparinase. Storage: -20°C. Source: Flavobacterium heparinum. Heparinase; Heparin lyase; Heparin eliminase; Heparin-sulfate lyase; Heparin-sulfate eliminase; Heparitin-sulfate lyase; Heparinase I; Heparinase III. Cat No: NATE-0337. | |
| Native Flavobacterium heparinum Heparinase II | Heparin-degrading lyase that recognizes heparin sulfate proteoglycan as its primary substrate. Heparinase I and III plays vital role in various biological processes: modulate cell-growth factor interactions, cell-lipoprotein interactions, neovascularization. It cleaves highly sulphated polysaccharide chains in presence of 2-O-sulfated α-L-idopyranosyluronic acid and β-D-glucopyranosyluronic acid residues of polysaccharides. Group: Enzymes. Synonyms: Heparinase; Heparin lyase II; Heparinase II; 149371-12-0. CAS No. 149371-12-0. Heparinase. Mole weight: mol wt 84.1 kDa. Activity: > 100 units/mg protein (enzyme + BSA). Form: Lyophilized powder stabilized with approx. 25% bovine serum albumin. Source: Flavobacterium heparinum. Heparinase; Heparin lyase II; Heparinase II; 149371-12-0. Cat No: NATE-0339. | |
| Native Flavobacterium heparinum Heparinase III | Heparin-degrading lyase that recognizes heparin sulfate proteoglycan as its primary substrate. In enzymology, a heparin-sulfate lyase (EC 4.2.2.8) is an enzyme that catalyzes the chemical reaction:Elimination of sulfate; appears to act on linkages between N-acetyl-D-glucosamine and uronate. Product is an unsaturated sugar. This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. Group: Enzymes. Synonyms: EC 4.2.2.8; Heparinase III; 37290-86-1; heparin-sulfate eliminase; heparitin-sulfate lyase; heparitinase I; heparitinase II; heparin-sulfate lyase. Enzyme Commission Number: EC 4.2.2.8. CAS No. 37290-86-1. Heparinase. Mole weight: mol wt 70.8 kDa. Activity: > 100 units/mg protein (enzyme + BSA). Storage: -20°C. Source: Flavobacterium heparinum. EC 4.2.2.8; Heparinase III; 37290-86-1; heparin-sulfate eliminase; heparitin-sulfate lyase; heparitinase I; heparitinase II; heparin-sulfate lyase. Cat No: NATE-0340. | |
| Native Flavobacterium menigosepticum Endoproteinase AspN | Endopeptidase or endoproteinase are proteolytic peptidases that break peptide bonds of nonterminal amino acids (i.e. within the molecule), in contrast to exopeptidases, which break peptide bonds from end-pieces of terminal amino acids. For this reason, endopeptidases cannot break down peptides into monomers, while exopeptidases can break down proteins into monomers. A particular case of endopeptidase is the oligopeptidase, whose substrates are oligopeptides instead of proteins. Endoproteinase aspn (flavastacin) is a zinc metalloendopeptidase which selectively cleaves peptide bonds n-terminal to aspartic acid residues. this enzyme is recommended to digest peptides with molecular weights of 5 kda or less. Applications: O digestion of proteins for proteomic analysis by mass spectrometry o protein and peptide identification. Group: Enzymes. Synonyms: Endopeptidase; endoproteinase. CAS No. 9001-92-7. Endoproteinase Asp-N. Mole weight: 40089.9 daltons. Activity: 25 μmol/min/mg. Storage: at -20°C. Form: Supplied in lyophilized form. Source: Flavobacterium menigosepticum. Endopeptidase; endoproteinase; Endoproteinase AspN; Endoproteinase Asp-N. Cat No: NATE-1274. | |
| 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 Flavobacterium meningosepticum PNGase F | In enzymology, a peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase (EC 3.5.1.52) is an enzyme that catalyzes a chemical reaction that cleaves a N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. Pngase f is purified from flavobacterium meningosepticum (3) and it is free of proteases and endo f activities. the following reagents are supplied with this produ...osaminyl)asparagine amidase; EC 3.5.1.52; PNGase F; 83534-39-8. Enzyme Commission Number: EC 3.5.1.52. CAS No. 83534-39-8. PNGase F. Mole weight: 36 kDa. Activity: 500,000 units/ml. Stability: Storage Conditions: 20 mM Tris-HCl, 50 mM NaCl, 5 mM Na2EDTA, 50% Glycerol, pH 7.5 25°C Heat Inactivation: 75°C for 10 min. Storage: Store at -20°C. Source: Flavobacterium meningosepticum. glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; glycopeptidase; Jack-bean glycopeptidase; PNGase A; PNGase F; glycopeptide N-glycosidase; peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase; EC 3.5.1.52; PNGase F; 83534-39-8. Cat No: NATE-0603. | |
| Native Flavobacterium sp. Creatinase | In enzymology, a creatinase (EC 3.5.3.3) is an enzyme that catalyzes the chemical reaction:creatine + H2O<-> sarcosine + urea. Thus, the two substrates of this enzyme are creatine and H2O, whereas its two products are sarcosine and urea. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. Creatinase accelerates the conversion reaction of creatine and water molecule to sarcosine and urea. It always acts in homodimer state and is induced by choline chloride. Group: Enzymes. Synonyms: Creatine amidinohydrolase; creatinase; 37340-58-2; EC 3.5.3.3. Enzyme Commission Number: EC 3.5.3.3. CAS No. 37340-58-2. Creatinase. Activity: 10-20 units/mg protein. Stability: 2-8°C. Form: lyophilized powder. Source: Flavobacterium sp. Creatine amidinohydrolase; creatinase; 37340-58-2; EC 3.5.3.3. Cat No: NATE-0161. | |
| Native Flavobacterium sp. Proline specific endopeptidase | Prolyl endopeptidase (PE) also known as prolyl oligopeptidase or post-proline cleaving enzyme is an enzyme that in humans is encoded by the PREP gene. Applications: This enzyme is useful for the determination of amino acid sequences of peptides and proteins containing proline residues. Group: Enzymes. Synonyms: EC 3.4.21.26; post-proline cleaving enzyme; proline-specific endopeptidase; post-proline endopeptidase; proline endopeptidase; endoprolylpeptidase; prolyl endopeptidase; prolyl oligopeptidase; PE. Enzyme Commission Number: EC 3.4.21.26. CAS No. 72162-84-6. PE. Mole weight: approx. 78 kDa. Activity: Grade? 5.0U/mg-solid or more. Stability: Stable at-20°C. Appearance: White amorphous powder, lyophilized. Source: Flavobacterium sp. EC 3.4.21.26; post-proline cleaving enzyme; proline-specific endopeptidase; post-proline endopeptidase; proline endopeptidase; endoprolylpeptidase; prolyl endopeptidase; prolyl oligopeptidase; PE. Cat No: DIA-213. | |
| Native Fructose-bisphosphate aldolase from Thermophillic bacteria | Fructose-bisphosphate aldolase (EC 4.1.2.13), often just aldolase, is an enzyme catalyzing a reversible reaction that splits the aldol, fructose 1,6-bisphosphate, into the triose phosphates dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (G3P). Aldolase can also produce DHAP from other (3S,4R)-ketose 1-phosphates such as fructose 1-phosphate and sedoheptulose 1,7-bisphosphate. Gluconeogenesis and the Calvin cycle, which are anabolic pathways, use the reverse reaction. Glycolysis, a catabolic pathway, uses the forward reaction. Aldolase is divided into two classes by mechanism. Applications: Carbon bond formation between dihydroxyacetone phosphate and linear aldehydes. Group: Enzymes. Synonyms: aldolase; fructose-1,6-bisphosphate triosephosphate-lyase; Fructose-bisphosphate aldolase; fructose diphosphate aldolase; D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase; EC 4.1.2.13; 9024-52-6. Enzyme Commission Number: EC 4.1.2.13. CAS No. 9024-52-6. Aldolase. Storage: Store at -20°C. Form: Frozen liquid. Source: Thermophillic bacteria. aldolase; fructose-1,6-bisphosphate triosephosphate-lyase; Fructose-bisphosphate aldolase; fructose diphosphate aldolase; D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase; EC 4.1.2.13; 9024-52-6. Cat No: NATE-1152. | |
| Native Galactose-adapted yeast Galactose-1-phosphate Uridyltransferase | Galactose-1-phosphate uridyltransferase (GALT) facilitates the simultaneous conversion of uridine diphosphoglucose (UDP-glucose) and galactose-1-phosphate (gal-1P) to uridine diphosphogalactose (UDP-galactose) and glucose-1-phosphate. Classic Galactosemia (CG) is an inherited metabolic condition caused by deficiency of GALT activity. Group: Enzymes. Synonyms: EC 2.7.7.12; UDP-glucose-hexose-1-phosphate uridylyltransferase; uridyl transferase; hexose-1-phosphate uridylyltransferase; uridyltransferase; hexose 1-phosphate uridyltransferase; UDP-glucose:alpha-D-galactose-1-phosphate uridylyltransferase; 9016-11-9. Enzyme Commission Number: EC 2.7.7.12. CAS No. 9026-21-5. GALT. Activity: 20-60 units/mg protein (modified Warburg-Christian). Storage: -20°C. Form: lyophilized powder; Contains buffer salts as Citrate and reduced glutathione. Source: Galactose-adapted yeast. EC 2.7.7.12; UDP-glucose-hexose-1-phosphate uridylyltransferase; uridyl transferase; hexose-1-phosphate uridylyltransferase; uridyltransferase; hexose 1-phosphate uridyltransferase; UDP-glucose:alpha-D-galactose-1-phosphate uridylyltransferase; 9016-11-9. Cat No: NATE-0277. | |
| Native Galactose-adapted yeast Uridine-5'-diphosphogalactose 4-epimerase | The enzyme UDP-glucose 4-epimerase (EC 5.1.3.2), also known as UDP-galactose 4-epimerase or GALE, is a homodimeric epimerase found in bacterial, fungal, plant, and mammalian cells. This enzyme performs the final step in the Leloir pathway of galactose metabolism, catalyzing the reversible conversion of UDP-galactose to UDP-glucose. GALE tightly binds nicotinamide adenine dinucleotide (NAD+), a co-factor required for catalytic activity. Group: Enzymes. Synonyms: UDP-galactose 4-epimerase; uridine diphosphoglucose epimerase; galactowaldenase; UDPG-4-epimerase; uridine diphosphate galactose 4-epimerase; uridine diphospho-gal. Enzyme Commission Number: EC 5.1.3.2. CAS No. 9032-89-7. UDP-Glc 4-epimerase. Activity: 10-20 units/mg protein (modified Warburg-Christian). Storage: -20°C. Form: Lyophilized powder containing approx. 40% buffer salts. Source: Galactose-adapted yeast. UDP-galactose 4-epimerase; uridine diphosphoglucose epimerase; galactowaldenase; UDPG-4-epimerase; uridine diphosphate galactose 4-epimerase; uridine diphospho-galactose-4-epimerase; UDP-glucose epimerase; UDP-galactose 4-epimerase; 4-epimerase; UDPG-4-epimerase; uridine diphosphoglucose 4-epimerase; uridine diphosphate glucose 4-epimerase; UDP-D-galactose 4-epimerase; EC 5.1.3.2; UDP-glucose 4-epimerase; GALE. Pack: vial. Cat No: NATE-0275. | |
| Native Geobacillus stearothermophilus 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). Suitable for cell culture. Applica... of n-terminal to phe which is preferred over the others. often used to do limited proteolysis for peptide mapping and studies of protein structure and conformational changes. 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. Activity: 30-175 units/mg protein (E1%/280). Storage: -20°C. Form: lyophilized powder containing calcium and sodium acetate buffer salts. Source: Geobacillus stearothermophilus. thermolysin; Bacillus thermoproteolyticus neutral proteinase; thermoase; thermoase Y10; TLN; EC 3.4.24.27. Cat No: NATE-0704. | |
| 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 Gluconobacter industrius D-Fructose Dehydrogenase | D-fructose dehydrogenase is a heterotrimeric membrane-bound enzyme commonly seen in various Gluconobacter sp. especially in Gluconobacter japonicus (Gluconobacter industrius). It has a molecular mass of ca. 140 kDa, consisting of subunits I (67kDa), II (51 kDa), and III (20 kDa) and catalyzes the oxidation of D-fructose to produce 5-keto-D-fructose. The enzyme is a flavoprotein-cytochrome c complex with subunits I and II covalently bound to flavin adenine dinucleotide (FAD) and heme C as prosthetic groups, respectively. Applications: D-fructose dehydrogenase is used as a biosensor to detect the presence of d-fructose. fructose dehydrogenase (fdh) is used in a numb...he bio-industry. a direct electron transfer reaction of d-fructose dehydrogenase adsorbed on a porous carbon electrode surface has been used to describe a batch-type coulometric d-fructose biosensor. Group: Enzymes. Synonyms: EC 1.1.99.11; fructose 5-dehydrogenase; D-fructose dehydrogenase; D-fructose:(acceptor) 5-oxidoreductase; 37250-85-4. Enzyme Commission Number: EC 1.1.99.11. CAS No. 37250-85-4. D-Fructose Dehydrogenase. Activity: 400-1,200 units/mg. Storage: -20°C. Form: Lyophilized powder. Source: Gluconobacter industrius. EC 1.1.99.11; fructose 5-dehydrogenase; D-fructose dehydrogenase; D-fructose:(acceptor) 5-oxidoreductase; 37250-85-4. Cat No: NATE-0184. | |
| Native Gluconobacter sp. D-Fructose Dehydrogenase | D-fructose dehydrogenase is a heterotrimeric membrane-bound enzyme commonly seen in various Gluconobacter sp. especially in Gluconobacter japonicus (Gluconobacter industrius). It has a molecular mass of ca. 140 kDa, consisting of subunits I (67kDa), II (51 kDa), and III (20 kDa) and catalyzes the oxidation of D-fructose to produce 5-keto-D-fructose. The enzyme is a flavoprotein-cytochrome c complex with subunits I and II covalently bound to flavin adenine dinucleotide (FAD) and heme C as prosthetic groups, respectively. Applications: D-fructose dehydrogenase is used as a biosensor to detect the presence of d-fructose. this enzyme is also used in a number of basic res...tic determination of d-fructose in clinical analysis. Group: Enzymes. Synonyms: EC 1.1.99.11; fructose 5-dehydrogenase; D-fructose dehydrogenase; D-fructose: (acceptor) 5-oxidoreductase; 37250-85-4. Enzyme Commission Number: EC 1.1.99.11. CAS No. 37250-85-4. D-Fructose Dehydrogenase. Mole weight: mol wt ~140 kDa. Activity: > 20 units/mg solid; 400-1,200 units/mg protein. Storage: -20°C. Form: lyophilized powder. supplied as a lyophilized powder containing approx 80% stabilizers, sugars, amino acids and BSA. Source: Gluconobacter sp. EC 1.1.99.11; fructose 5-dehydrogenase; D-fructose dehydrogenase; D-fructose: (acceptor) 5-oxidoreductase; 37250-85-4. Cat No: NATE-0185. | |
| Native Glutamate dehydrogenase (NADP+) from Yeast | Glutamate dehydrogenase (GLDH) is an enzyme, present in most microbes and the mitochondria of eukaryotes, as are some of the other enzymes required for urea synthesis, that converts glutamate to α-ketoglutarate, and vice versa. In animals, the produced ammonia is usually used as a substrate in the urea cycle. Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate. Group: Enzymes. Synonyms: glutamate dehydrogenase (NADP+); glutamic dehydrogenase; dehydrogenase; glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD(P)-glutamate dehydrogenase; NAD(P)H-dependent glutamate dehydrogenase; glutamate d. Enzyme Commission Number: EC 1.4.1.4. CAS No. 9029-11-2. GLDH. Activity: > 10 U/mg protein. Storage: Below -20°C. Form: Lyophilized Powder. Source: Yeast. glutamate dehydrogenase (NADP+); glutamic dehydrogenase; dehydrogenase; glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD(P)-glutamate dehydrogenase; NAD(P)H-dependent glutamate dehydrogenase; glutamate dehydrogenase (NADP); EC 1.4.1.4; GLDH. Cat No: NATE-1037. | |
| Native Glutamine Synthetase from Microorganism | 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. 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. Mole weight: ca. 900 kDa. Activity: > 7 U/mg lyophilizate. Appearance: Light yellow lyophilizate. Storage: at -20°C. Source: Microorganism. Glutamine synthetase; GS; EC 6.3.1.2; Glutamate-ammonia ligase. Cat No: DIA-411. | |
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