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| Product | Description | |
|---|---|---|
| 5-methylphenazine-1-carboxylate 1-monooxygenase | The enzyme, characterized from the bacterium Pseudomonas aeruginosa, is involved in the biosynthesis of pyocyanin, a toxin produced and secreted by the organism. It can also act on phenazine-1-carboxylate, converting it into phenazin-1-ol. Group: Enzymes. Synonyms: phzS (gene name). Enzyme Commission Number: EC 1.14.13.218. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0820; 5-methylphenazine-1-carboxylate 1-monooxygenase; EC 1.14.13.218; phzS (gene name). Cat No: EXWM-0820. |  |
| 6-Chloro-5-(2,3-dichlorophenoxy)-2-methylthio-benzimidazole (Triclabendazole) | Triclabendazole is a member of the benzimidazole family of anthelmintics. It is effective against F. hepatica helminths that cause fascioliasis, reducing secreted protease enzyme activities that are critical for the invasion, migration, nutrition, and survival of the parasite.1 In yeast and mammalian cells, triclabendazole was shown to inhibit adenylyl cyclase in the Ras-adenylyl cyclase-protein kinase A nutrient-sensing pathway and to prevent apoptosis induced by the Parkinsons disease-related protein α-synuclein, demonstrating a protective role during various cellular stresses.2,3. Group: Biochemicals. Alternative Names: 5-Chloro-6- (2, 3-dichlorophenoxy) -2- methyl thiobenzimidazole; CGA-89317, egaten; Fasinex; Triclabendazole. Grades: Highly Purified. CAS No. 68786-66-3. Pack Sizes: 25g, 50g, 100g. Molecular Formula: C14H9Cl3N2OS, Molecular Weight: 359.66. US Biological Life Sciences. |  Worldwide |
| aclacinomycin-A oxidase | A flavoprotein (FAD). This bifunctional enzyme is a secreted flavin-dependent enzyme that is involved in the modification of the terminal sugar residues in the biosynthesis of aclacinomycins. The enzyme utilizes the same active site to catalyse the oxidation of the rhodinose moiety of aclacinomycin N to the cinerulose A moiety of aclacinomycin A (cf. EC 1.1.3.45) and the oxidation of the latter to the L-aculose moiety of aclacinomycin Y. Group: Enzymes. Synonyms: AknOx (ambiguous); aclacinomycin oxidoreductase (ambiguous). Enzyme Commission Number: EC 1.3.3.14. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1375; aclacinomycin-A oxidase; EC 1.3.3.14; AknOx (ambiguous); aclacinomycin oxidoreductase (ambiguous). Cat No: EXWM-1375. | |
| aclacinomycin-N oxidase | A flavoprotein (FAD). This bifunctional enzyme is a secreted flavin-dependent enzyme that is involved in the modification of the terminal sugar residues in the biosynthesis of aclacinomycins. The enzyme utilizes the same active site to catalyse the oxidation of the rhodinose moiety of aclacinomycin N to the cinerulose A moiety of aclacinomycin A and the oxidation of the latter to the L-aculose moiety of aclacinomycin Y (cf. EC 1.3.3.14, aclacinomycin A oxidase). Group: Enzymes. Synonyms: AknOx (ambiguous); aclacinomycin oxidoreductase (ambiguous). Enzyme Commission Number: EC 1.1.3.45. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0418; aclacinomycin-N oxidase; EC 1.1.3.45; AknOx (ambiguous); aclacinomycin oxidoreductase (ambiguous). Cat No: EXWM-0418. | |
| α-Amylase from Bacillus subtilis, Recombinant | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9000-90-2. Purity: > 95 % as judged by SDS-PAGE. α-Amylase. Mole weight: 72550.6 Da. Activity: 4449.51 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Bacillus subtilis subsp. subtilis str. 168. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Cat No: NATE-1172. | |
| α-Amylase from Bacteroides fragilis, Recombinant | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9000-90-2. Purity: > 95 % as judged by SDS-PAGE. α-Amylase. Mole weight: 59099.7 Da. Activity: 36.25 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Bacteroides fragilis NCTC 9343. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Cat No: NATE-1173. | |
| α-Amylase from Escherichia coli, Recombinant | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9000-90-2. Purity: > 95 % as judged by SDS-PAGE. α-Amylase. Mole weight: 60459.5 Da. Activity: 23.61 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Escherichia coli str. K-12 substr. W3110. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Cat No: NATE-1174. | |
| Amylase 126A from Clostridium perfringens, Recombinant | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9000-90-2. Purity: >90% by SDS-PAGE. α-Amylase. Mole weight: 40.4 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Clostridium perfringens. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A; Amylase 126A. Cat No: NATE-1302. | |
| Amylase 13A from Bacillus licheniformis, Recombinant | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9000-90-2. Purity: >90% by SDS-PAGE. α-Amylase. Mole weight: 57.4 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Bacillus licheniformis. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A; Amylase 13A. Cat No: NATE-1300. | |
| Amylase 13A from Escherichia coli, Recombinant | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9000-90-2. Purity: >90% by SDS-PAGE. α-Amylase. Mole weight: 58.6 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Escherichia coli. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A; Amylase 13A. Cat No: NATE-1304. | |
| Amylase 13A from Streptococcus mutans, Recombinant | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9000-90-2. Purity: >90% by SDS-PAGE. α-Amylase. Mole weight: 58.4 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Streptococcus mutans. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A; Amylase 13A. Cat No: NATE-1301. | |
| Amylase 57C from Thermotoga maritima, Recombinant | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9000-90-2. Purity: >90% by SDS-PAGE. α-Amylase. Mole weight: 48.0 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Thermotoga maritima. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A; Amylase 57C. Cat No: NATE-1303. | |
| barrierpepsin | A secreted endopeptidase known from bakers yeast (Saccharomyces cerevisiae). In peptidase family A1 (pepsin A family). Group: Enzymes. Synonyms: barrier proteinase; Bar proteinase. Enzyme Commission Number: EC 3.4.23.35. CAS No. 152060-38-3. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4272; barrierpepsin; EC 3.4.23.35; 152060-38-3; barrier proteinase; Bar proteinase. Cat No: EXWM-4272. | |
| β-Agarase 16D from Zobellia galactanivorans, Recombinant | Agarase is an enzyme with system name agarose 4-glycanohydrolase. It found in agarolytic bacteria and is the first enzyme in the agar catabolic pathway. It is responsible for allowing them to use agar as their primary source of Carbon and enables their ability to thrive in the ocean. Agarases are classified as either α-agarases or β-agarases based upon whether they degrade αor β linkages in agarose, breaking them into oligosaccharides. When secreted, α-agarases yield oligosaccharides with 3.6 anhydro-L-galactose at the reducing end whereas β-agarases result in D-galactose residues. Group: Enzymes. Synonyms: agarase; AgaA; AgaB; endo-β-agarase; agarose 3-glycanohydrolase; EC 3.2.1.81; 37288-57-6. Enzyme Commission Number: EC 3.2.1.81. CAS No. 37288-57-6. Purity: >90% by SDS-PAGE. Agarase. Mole weight: 42.4 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Zobellia galactanivorans. agarase; AgaA; AgaB; endo-β-agarase; agarose 3-glycanohydrolase; EC 3.2.1.81; 37288-57-6; β-Agarase; β-Agarase 16D. Cat No: NATE-1293. | |
| β-Agarase I from E. coli, Recombinant | Agarase is an enzyme with system name agarose 4-glycanohydrolase. It found in agarolytic bacteria and is the first enzyme in the agar catabolic pathway. It is responsible for allowing them to use agar as their primary source of Carbon and enables their ability to thrive in the ocean. Agarases are classified as either α-agarases or β-agarases based upon whether they degrade αor β linkages in agarose, breaking them into oligosaccharides. When secreted, α-agarases yield oligosaccharides with 3.6 anhydro-L-galactose at the reducing end whereas β-agarases result in D-galactose residues. Β-agarase cleaves the agarose subunit, unsubstituted...garase i can be used to purify both large (> 50 kb) and small (< 50 kb) fragments of dna from gels. the remaining carbohydrate molecules and β-agarase i will not, in general, interfere with subsequent dna manipulations such as restriction endonuclease digestion, ligation, and transformation. Group: Enzymes. Synonyms: agarase; AgaA; AgaB; endo-β-agarase; agarose 3-glycanohydrolase; EC 3.2.1.81; 37288-57-6. Agarase. Storage: at -20°C. Form: 50 mM Bis Tris-HCl (pH 6.5), 1 mM Na2EDTA and 50% glycerol. Source: E. coli. Species: E. coli. agarase; AgaA; AgaB; endo-β-agarase; agarose 3-glycanohydrolase; EC 3.2.1.81; 37288-57-6; β-Agarase I. Cat No: NATE-1282. | |
| BW-B 70C | BW B70C is a potent and selective inhibitor of 5-lipoxygenase (5-LO). 5-LO is an enzyme that transforms essential fatty acids (EFAs) into leukotrienes and is activated by 5-lipoxygenase activating protein (FLAP). BW-B 70C had high potency and long duration in vivo and was considered as potential anti-asthma drug. It was reported that BW B70C blocks leukotriene C4 synthesis by alveolar macrophages, which decreases the migration for leukocyte to the airway lumen. BW B70C didn't affect vascular leucocyte margination and the blood levels of secreted phospholipase A2 and TNF-&alpha. Synonyms: N-[3-[3-(-Fluorophenoxy)phenyl]-1-methyl-2-propenyl]-N-hydroxyurea. Grades: ≥98%. CAS No. 134470-38-5. Molecular formula: C17H17FN2O3. Mole weight: 316.33. |  |
| Carboxypeptidase B from Porcine, Recombinant | Carboxypeptidase B (or peptidyl-L-lysine (-L-arginine) hydrolase) catalyzes the hydrolysis of the basic amino acids, lysine, arginine, and ornithine from the C-terminal position of polypeptides. It has been shown to be a single polypeptide of 34 kDa Da. Trypsin is capable of converting native enzyme to the active enzyme, carboxypeptidase B II in vitro. The optimum pH is found to be 9.0. The enzyme may be used for sequence analysis by successive cleavage of C-terminal basic amino acids. It can also be used as a serum marker for the diagnosis of acute pancreatitis. Carboxypeptidase b (ec 3.4.17.2), also well known as protaminase, pancreatic procarboxy-peptidase b (pcpb), ... mature chain. the secreted cpb zymogen is converted to enzymatically active cpb by limited proteolysis by trypsin. Group: Enzymes. Synonyms: carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5. Enzyme Commission Number: EC 3.4.17.2. Purity: >90% (SDS-PAGE test). Mole weight: About 35kDa (SDS-PAGE detection). Activity: >180U/mg. Appearance: White powder, lyophilized. Storage: Redissolved in 20% glycerol, 4°C, store at -20°C for long-term preservation, Avoid multiple freeze-thaw cycles. Form: Freeze dried powder. Source: Porcine. carboxypeptidase B; protaminase; C | |
| chloride peroxidase | Brings about the chlorination of a range of organic molecules, forming stable C-Cl bonds. Also oxidizes bromide and iodide. Enzymes of this type are either heme-thiolate proteins, or contain vanadate. A secreted enzyme produced by the ascomycetous fungus Caldariomyces fumago (Leptoxyphium fumago) is an example of the heme-thiolate type. It catalyses the production of hypochlorous acid by transferring one oxygen atom from H2O2 to chloride. At a separate site it catalyses the chlorination of activated aliphatic and aromatic substrates, via HClO and derived chlorine species. In the absence of halides, it shows peroxidase (e.g. phenol oxidation) and peroxygenase activities. The latter ...peroxidase, and is related to bromide peroxidase (EC 1.11.1.18). It contains vanadate and oxidizes chloride, bromide and iodide into hypohalous acids. In the absence of halides, it peroxygenates organic sulfides and oxidizes ABTS [2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)] but no phenols. Group: Enzymes. Synonyms: chloroperoxidase; CPO; vanadium haloperoxidase. Enzyme Commission Number: EC 1.11.1.10. CAS No. 9055-20-3. CPO. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0491; chloride peroxidase; EC 1.11.1.10; 9055-20-3; chloroperoxidase; CPO; vanadium haloperoxidase. Cat No: EXWM-0491. | |
| cholesterol oxidase | Contains FAD. Cholesterol oxidases are secreted bacterial bifunctional enzymes that catalyse the first two steps in the degradation of cholesterol. The enzyme catalyses the oxidation of the 3β-hydroxyl group to a keto group, and the isomerization of the double bond in the oxidized steroid ring system from the Δ5 position to Δ6 position (cf. EC 5.3.3.1, steroid Δ-isomerase). Group: Enzymes. Synonyms: cholesterol- O2 oxidoreductase; 3β-hydroxy steroid oxidoreductase; 3β-hydroxysteroid:oxygen oxidoreductase. Enzyme Commission Number: EC 1.1.3.6. CAS No. 9028-76-6. CHOD. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0424; cholesterol oxidase; EC 1.1.3.6; 9028-76-6; cholesterol- O2 oxidoreductase; 3β-hydroxy steroid oxidoreductase; 3β-hydroxysteroid:oxygen oxidoreductase. Cat No: EXWM-0424. | |
| clostridial aminopeptidase | A secreted enzyme from Clostridium histolyticum, requiring Mn2+ or Co2+. Group: Enzymes. Synonyms: Clostridium histolyticum aminopeptidase. Enzyme Commission Number: EC 3.4.11.13. CAS No. 59680-69-2. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4009; clostridial aminopeptidase; EC 3.4.11.13; 59680-69-2; Clostridium histolyticum aminopeptidase. Cat No: EXWM-4009. | |
| dactylysin | An endopeptidase of 100 kDa secreted from the skin of the amphibian, Xenopus laevis (Dactylêtre du Cap). Resembles neprilysin in insensitivity to 1 μM captopril, but differs from it in being insensitive to thiorphan (1 μM) and unable to digest [Met5]enkephalin, [Leu5]enkephalin, oxytocin, and substance P-(7-11)-peptide. A similar endopeptidase is found in human neuroblastoma cells. Group: Enzymes. Synonyms: peptide hormone inactivating endopeptidase; PHIE. Enzyme Commission Number: EC 3.4.24.60. CAS No. 139466-40-3. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4343; dactylysin; EC 3.4.24.60; 139466-40-3; peptide hormone inactivating endopeptidase; PHIE. Cat No: EXWM-4343. | |
| dye decolorizing peroxidase | Heme proteins with proximal histidine secreted by basidiomycetous fungi and eubacteria. They are similar to EC 1.11.1.16 versatile peroxidase (oxidation of Reactive Black 5, phenols, veratryl alcohol), but differ from the latter in their ability to efficiently oxidize a number of recalcitrant anthraquinone dyes, and inability to oxidize Mn(II). The model substrate Reactive Blue 5 is converted with high efficiency via a so far unique mechanism that combines oxidative and hydrolytic steps and leads to the formation of phthalic acid. Bacterial TfuDyP catalyses sulfoxidation. Group: Enzymes. Synonyms: DyP; DyP-type peroxidase. Enzyme Commission Number: EC 1.11.1.19. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0500; dye decolorizing peroxidase; EC 1.11.1.19; DyP; DyP-type peroxidase. Cat No: EXWM-0500. | |
| Enterokinase from bovine intestine, Recombinant | Enteropeptidase (also called enterokinase) is an enzyme produced by cells of the duodenum and involved in human and animal digestion. It is secreted from intestinal glands (the crypts of Lieberkühn) following the entry of ingested food passing from the stomach. Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes. Absence of enteropeptidase results in intestinal digestion impairment. Applications: Enterokinase is a member of the s1 peptidase family. in vivo, it is responsble for the proteolytic activation of trypsin from trypsinogen. enterokinase is used for site specific ...yme from creative enzymes has been used to compare the specific activity with that of purified, recombinant bovine enterokinase (light chain) overexpressed in escherichia coli. Group: Enzymes. Synonyms: enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Enzyme Commission Number: EC 3.4.21.9. CAS No. 9014-74-8. Enterokinase. Mole weight: 28 kDa light chain form. Activity: Type I, > 20 units/mg protein. Storage: -20°C. Form: Type I, supplied as a solution in 20 mM Tris-HCl, 200 mM NaCl, and 50% glycerol; Type II, white powder. Source: E. coli. Species: Bovine intestine. enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Pack: vial of ~0.2 unit. Cat No: NATE-0226. | |
| Enterokinase from Human, Recombinant | Enteropeptidase (also called enterokinase) is an enzyme produced by cells of the duodenum and involved in human and animal digestion. It is secreted from intestinal glands (the crypts of Lieberkühn) following the entry of ingested food passing from the stomach. Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes. Absence of enteropeptidase results in intestinal digestion impairment. > 90% (sds-page), > 90% (hplc), cell culture tested. Group: Enzymes. Synonyms: enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Enzyme Commission Number: EC 3.4.21.9. CAS No. 9014-74-8. Enterokinase. Mole weight: 108.7 kDa. Activity: Type I, > 20 units/mg protein. Form: Lyophilized from 10 mM Sodium Phosphate, pH 7.5 + 1 mM Calcium Chloride. Source: CHO cells. Species: Human. enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Cat No: NATE-0227. | |
| feruloyl esterase | Catalyses the hydrolysis of the 4-hydroxy-3-methoxycinnamoyl (feruloyl) group from an esterified sugar, which is usually arabinose in "natural" substrates. p-Nitrophenol acetate and methyl ferulate are poorer substrates. All microbial ferulate esterases are secreted into the culture medium. They are sometimes called hemicellulase accessory enzymes, since they help xylanases and pectinases to break down plant cell wall hemicellulose. Group: Enzymes. Synonyms: ferulic acid esterase, hydroxycinnamoyl esterase, hemicellulase accessory enzymes; FAE-III, cinnamoyl ester hydrolase, FAEA, cinnAE, FAE-I, FAE-II. Enzyme Commission Number: EC 3.1.1.73. CAS No. 134712-49-5. Feruloyl esterase. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3501; feruloyl esterase; EC 3.1.1.73; 134712-49-5; ferulic acid esterase, hydroxycinnamoyl esterase, hemicellulase accessory enzymes; FAE-III, cinnamoyl ester hydrolase, FAEA, cinnAE, FAE-I, FAE-II. Cat No: EXWM-3501. | |
| flavastacin | A zinc metalloendopeptidase in peptidase family M12 (astacin family), secreted by the bacterium Flavobacterium meningosepticum. The specificity is similar to that of EC 3.4.24.33, peptidyl-Asp metalloendopeptidase from Pseudomonas fragi but the two are reported to be structurally dissimilar. Group: Enzymes. Enzyme Commission Number: EC 3.4.24.76. CAS No. 167973-66-2. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4360; flavastacin; EC 3.4.24.76; 167973-66-2. Cat No: EXWM-4360. | |
| Galactose Oxidase from Dactylium dendroides, Recombinant | 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 (gao) is a recombinantly expressed copper activated enzyme derived from dactylium dendroides that catalyzes the stereospecific oxidation of d-isomer primary alcohols to aldehydes and hydrogen peroxide (1-3). gao has a range of substrates that include d-galactose and polysaccharides, glycolipids, or glycoproteins with d-galactose at their non-reducing end. Applications: Gao has been shown to be useful in a number of biotechnology and medical applications which include monitoring of galactose in blood and urine, paper strengthening additives, test strips for cancer diagnosis, biosensors and lactose detection, dental care and hair coloring and waving. Group: Enzymes. Synonyms: EC 1.1.3.9; D-galactose o. CAS No. 9028-79-9. Purity: >95% by SDS-PAGE. Galactose Oxidase. Mole weight: 68.9 kDa (Calculated). Activity: >1750 U/mg. Stability: 3-6 months. Storage: 2-8°C. Avoid multiple freeze/thaw cycles. Source: Dactylium dendroides. EC 1.1.3.9; D-galactose oxidase; β-galactose oxidase; 9028-79-9; Galactose Oxidase. Cat No: NATE-1288. | |
| γ-glutamyl hydrolase | A lysosomal or secreted, thiol-dependent peptidase, most active at acidic pH. Commonly studied with folylpoly-γ-glutamate as substrate, with which the initial cleavage may release glutamate or poly-γ-glutamate of two or more residues, according to the species of origin of the enzyme. Final products are pteroyl-α-glutamate (folic acid) and free glutamate. Highly specific for the γ-glutamyl bond, but not for the C-terminal amino acid (leaving group). Action on γ-glutamyl bonds is independent of an N-terminal pteroyl moiety, but it is not known whether an N-terminal γ-Glu residue can be hydrolysed. Type example of peptidase family C26. Group: Enzymes. Synonyms: conjugase; folate conjugase; lysosomal γ-glutamyl carboxypeptid. Enzyme Commission Number: EC 3.4.19.9. CAS No. 9074-87-7. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4092; γ-glutamyl hydrolase; EC 3.4.19.9; 9074-87-7; conjugase; folate conjugase; lysosomal γ-glutamyl carboxypeptidase; γ-Glu-X carboxypeptidase; pteroyl-poly-γ-glutamate hydrolase; carboxypeptidase G; folic acid conjugase; poly(γ-glutamic acid) endohydrolase; polyglutamate hydrolase; poly(glutamic acid) hydrolase II; pteroylpoly-γ-glutamyl hydrolase. Cat No: EXWM-4092. | |
| gastricsin | Formed from progastricsin, apparently in the gastric juice of most vertebrates. In addition to the fundus, progastricsin is also secreted in antrum and proximal duodenum. Seminal plasma contains a zymogen that is immunologically identical with progastricsin. In peptidase family A1 (pepsin A family). Group: Enzymes. Synonyms: pepsin C; pig parapepsin II; parapepsin II. Enzyme Commission Number: EC 3.4.23.3. CAS No. 9012-71-9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4267; gastricsin; EC 3.4.23.3; 9012-71-9; pepsin C; pig parapepsin II; parapepsin II. Cat No: EXWM-4267. | |
| gelatinase A | A secreted endopeptidase in peptidase family M10 (interstitial collagenase family), but possessing an additional fibronectin-like domain. Group: Enzymes. Synonyms: 72-kDa gelatinase; matrix metalloproteinase 2; type IV collagenase (ambiguous); 3/4 collagenase (obsolete); matrix metalloproteinase 5 (obsolete); 72 kDa gelatinase type A; collagenase IV (ambiguous); collagenase type IV (ambiguous); MMP 2; type IV collagen metalloproteinase (ambiguous); type IV collagenase/gelatinase (ambiguous). Enzyme Commission Number: EC 3.4.24.24. CAS No. 146480-35-5. Matrix Metalloproteinase. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4305; gelatinase A; EC 3.4.24.24; 146480-35-5; 72-kDa gelatinase; matrix metalloproteinase 2; type IV collagenase (ambiguous); 3/4 collagenase (obsolete); matrix metalloproteinase 5 (obsolete); 72 kDa gelatinase type A; collagenase IV (ambiguous); collagenase type IV (ambiguous); MMP 2; type IV collagen metalloproteinase (ambiguous); type IV collagenase/gelatinase (ambiguous). Cat No: EXWM-4305. | |
| gingipain R | A secreted endopeptidase from the bacterium Porphyromonas gingivalis. Strongly activated by glycine, and stabilized by Ca2+. Precursor molecule contains a hemagglutinin domain. Misleadingly described in some literature as "trypsin-like", being a cysteine peptidase, type example of family C25. Group: Enzymes. Synonyms: Arg-gingipain; gingipain-1; argingipain; Arg-gingivain-55 proteinase; Arg-gingivain-70 proteinase; Arg-gingivain-75 proteinase; arginine-specific cysteine protease; arginine-specific gingipain; arginine-specific gingivain; RGP-1; RGP. Enzyme Commission Number: EC 3.4.22.37. CAS No. 159745-71-8. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4212; gingipain R; EC 3.4.22.37; 159745-71-8; Arg-gingipain; gingipain-1; argingipain; Arg-gingivain-55 proteinase; Arg-gingivain-70 proteinase; Arg-gingivain-75 proteinase; arginine-specific cysteine protease; arginine-specific gingipain; arginine-specific gingivain; RGP-1; RGP. Cat No: EXWM-4212. | |
| Glucose-6-Phosphate Isomerase from Human, Recombinant | Glucose-6-phosphate isomerase (GPI) is a part of the GPI family whose members encode multifunctional phosphoglucose isomerase proteins involved in energy pathways. GPI is a dimeric enzyme which catalyzes the reversible isomerization of glucose-6-phosphate and fructose-6-phosphate. Mammalian GPI also functions as a tumor-secreted cytokine and an angiogenic factor (AMF) which stimulates endothelial cell motility. In addition, GPI is a neurotrophic factor (Neuroleukin) for spinal and sensory neurons. GPI performs in different capacities inside and outside the cell. In the cytoplasm, GPI is involved in glycolysis and gluconeogenesis, while outside the cell it acts as a...somerase; Autocrine motility factor; Neuroleukin; Sperm antigen 36; GPI; PGI; PHI; AMF; NLK; SA-36; GNPI. Purity: Greater than 95.0% as determined by SDS-PAGE. PGI. Mole weight: 65.3 kDa. Stability: GPI although stable 4°C for 4 weeks, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles. Appearance: Sterile Filtered colorless solution. Source: E. coli. Species: Human. Glucose-6-phosphate isomerase; Phosphoglucose isomerase; Phosphohexose isomerase; Autocrine motility factor; Neuroleukin; Sperm antigen 36; GPI; PGI; PHI; AMF; NLK; SA-36; GNPI. Cat No: NATE-0841. | |
| HA-155 | HA-155 is an autotaxin inhibitor. Autotaxin, also known as ectonucleotide pyrophosphatase/phosphodiesterase 2 (NPP2 or ENPP2), is a secreted enzyme converting lysophosphatidylcholine (LPC) into lysophosphatidic acid (LPA), which is responsible for tumor cell motility stimulation. Synonyms: HA 155; HA155; Autotaxin Inhibitor IV; Boronic acid, B- [4- [ [4- [ [3- [ (4-fluorophenyl) methyl] -2, 4-dioxo-5-thiazolidinylidene] methyl] phenoxy] methyl] phenyl] -. Grades: ≥95%. CAS No. 1229652-22-5. Molecular formula: C24H19BFNO5S. Mole weight: 463.3. | |
| heparanase | Heparanase cleaves the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying either a 3-O-sulfo or a 6-O-sulfo group. Heparanase-1 cuts macromolecular heparin into fragments of 5000-20000 Da. The enzyme cleaves the heparan sulfate glycosaminoglycans from proteoglycan core proteins and degrades them to small oligosaccharides. Inside cells, the enzyme is important for the normal catabolism of heparan sulfate proteoglycans, generating glycosaminoglycan fragments that are then transported to lysosomes and completely degraded. When secreted, heparanase degrades basement membrane heparan sulfate glycosaminoglycans at sites of injury or inflammation, allowing extravasion of immune cells into nonvascular spaces and releasing factors that regulate cell proliferation and angiogenesis. Group: Enzymes. Synonyms: Hpa1 heparanase; Hpa1; heparanase 1; heparanase-1; C1A heparanase; HPSE. Enzyme Commission Number: EC 3.2.1.166. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3848; heparanase; EC 3.2.1.166; Hpa1 heparanase; Hpa1; heparanase 1; heparanase-1; C1A heparanase; HPSE. Cat No: EXWM-3848. | |
| IgA-specific serine endopeptidase | Species variants differing slightly in specificity are secreted by Gram-negative bacteria Neisseria gonorrhoeae and Haemophilus influenzae. Type example of peptidase family S6. Some other bacterial endopeptidases with similar specificity are of metallo- type (see EC 3.4.24.13, IgA-specific metalloendopeptidase). Group: Enzymes. Synonyms: IgA protease; IgA proteinase; IgA-specific proteinase; immunoglobulin A protease; immunoglobulin A proteinase. Enzyme Commission Number: EC 3.4.21.72. CAS No. 55127-02-1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4164; IgA-specific serine endopeptidase; EC 3.4.21.72; 55127-02-1; IgA protease; IgA proteinase; IgA-specific proteinase; immunoglobulin A protease; immunoglobulin A proteinase. Cat No: EXWM-4164. | |
| Lipase-polyethylene glycol | A lipase is an enzyme that catalyzes the hydrolysis of fats (lipids). Lipases are a subclass of the esterases. Lipases perform essential roles in the digestion, transport and processing of dietary lipids (e.g. triglycerides, fats, oils) in most, if not all, living organisms. Genes encoding lipases are even present in certain viruses. Most lipases act at a specific position on the glycerol backbone of lipid substrate (A1, A2 or A3) (small intestine). Several other types of lipase activities exist in nature, such as phospholipases and sphingomyelinases, however these are usually treated separately from "conventional" lipases. Some lipases are expressed and secreted by pathogenic organisms during the infection. Group: Enzymes. Synonyms: PEG-Lipase; Lipase-polyethylene glycol. Lipase. Activity: ~75,000 units/mg protein (using olive oil). Storage: -20°C. Form: Lyophilized powder containing PEG. PEG-Lipase; Lipase-polyethylene glycol. Pack: Package size based on protein content. Cat No: NATE-0539. | |
| marinobufagenin | Marinobufagenin (marinobufagin) is a cardiotonic bufadienolide steroid secreted by the toad Bufo rubescens and other related species such as Bufo marinus. It is a vasoconstrictor with effects similar to digitalis. Uses: Enzyme inhibitors; vasoconstrictor agents. Synonyms: Marinobufagin; (3beta,5beta,14alpha,15beta)-3,5-dihydroxy-14,15-epoxybufa-20,22-dienolide; NSC-234205. Grades: ≥ 98.0%. CAS No. 470-42-8. Molecular formula: C24H32O5. Mole weight: 400.52. | |
| Matrix Metalloproteinase-3 from Human, Recombinant | Matrix metalloproteinase-3 (MMP-3) also known as stromelysin-1 and transin (EC 3.4.24.17) cleaves a number of substrates including cartilage proteoglycan, collagen types II, III, IV, V and IX, fibronectin, laminin, and can activate MMP 1. MMP-3 is secreted as 57 and 59 kDa proenzymes and can be activated in vitro by organomercurials (e.g., 4 aminophenylmercuric acetate, APMA) and in vivo by proteases via intermediate forms to a 45 kDa active MMP 3 enzyme. Further autolysis to a 28 kDa form can also occur. MMP-3 is thought to play an important role in pathophysiological degradation processes associated with conditions such as rheumatoid arthritis and cancer cell invas...C 3.4.24.17; matrix metalloproteinase 3; proteoglycanase; collagenase activating protein; procollagenase activator; transin; MMP-3; neutral proteoglycanase; stromelysin; collagen-activating protein. Enzyme Commission Number: EC 3.4.24.17. CAS No. 79955-99-0. Purity: >95% by SDS-PAGE. Matrix Metalloproteinase. Mole weight: 57 kDa. Storage: < -70°C; Avoid freeze/thaw. Form: Lyophilized from 100 mM NaCl, 50 mM HEPES, pH 7.3. Species: Human. Stromelysin 1; EC 3.4.24.17; matrix metalloproteinase 3; proteoglycanase; collagenase activating protein; procollagenase activator; transin; MMP-3; neutral proteoglycanase; stromelysin; collagen-activating protein. Cat No: NATE-0861. | |
| Native Aspergillus oryzae α-Amylase | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Applications: Α-amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. α-amylase has been used in various plant studies, such as metabolism studies in arabidopsis. amylases from aspergillus oryzae are commonly used as baking additives to prevent staling in the baking industry, clarify haze from fruit juices and alcoholic beverages, and to produce glucose and maltose syrup products. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9001-19-8. α-Amylase. Mole weight: Mr ~51 kDa. Activity: > 150 units/mg protein (biuret); ~1.5 units/mg; ~30 units/mg. Storage: -20°C. Form: powder containing dextrin. Source: Aspergillus oryzae. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Cat No: NATE-0740. | |
| Native Bacillus amyloliquefaciens α-Amylase | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Applications: Α-amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. this product is from bacillus amyloliquefaciens and is supplied as a liquid. α-amylase has been used in various plant studies, such as metabolism studies in arabidopsis. α-amylase from bacillus amy...ng sugars, which are then used for ethanol fermentation by saccharomyces cerevisiae fncc 3012. the enzyme catalyzes amylolysis of gelatinised waxy maize starch to produce reducing sugars. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9001-19-8. α-Amylase. Mole weight: 55 kDa. Activity: > 250 units/g. Form: liquid. Source: Bacillus amyloliquefaciens. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Cat No: NATE-0741. | |
| Native Bacillus licheniformis α-Amylase | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Applications: Α-amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. this product is from bacillus licheniformis and is type xii-a. α-amylase, from creative enzymes, has been used in various plant studies, such as metabolism studies in arabidopsis. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9001-19-8. α-Amylase. Activity: Type XII-A, saline solution, > 500 units/mg protein (biuret); Type B, liquid. Source: Bacillus licheniformis. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Cat No: NATE-0742. | |
| 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 Bovine Angiotensin Converting Enzyme | Angiotensin-converting enzyme (EC 3.4.15.1), or "ACE" indirectly increases blood pressure by causing blood vessels to constrict. It does that by converting angiotensin I to angiotensin II, which constricts the vessels. For this reason, drugs known as ACE inhibitors are used to lower blood pressure. ACE, angiotensin I and angiotensin II are part of the renin-angiotensin system (RAS), which controls blood pressure by regulating the volume of fluids in the body. ACE is secreted in the lungs and kidneys by cells in the endothelium (inner layer) of blood vessels. Applications: Positive control. Group: Enzymes. Synonyms: ACE; Angiotensin Converting Enzyme; EC 3.4.15.1; dipept...te buffer-300 mM NaCl, pH 8.3 at 37°C. Storage: Maintain at -20°C in undiluted aliquots for up to 12 months. Maintain at 4°C for up to one month. A decrease in activity may occur within prolonged storage at 4°C. Source: Bovine lung. Species: Bovine. ACE; Angiotensin Converting Enzyme; EC 3.4.15.1; dipeptidyl carboxypeptidase I; peptidase P; dipeptide hydrolase, peptidyl dipeptidase; angiotensin converting enzyme; kininase II; angiotensin I-converting enzyme; carboxycathepsin; dipeptidyl carboxypeptidase; "hypertensin converting enzyme" peptidyl dipeptidase I; peptidyl-dipeptide hydrolase; peptidyldipeptide hydrolase; endothelial cell peptidyl dipeptidase; peptidyl dipept | |
| Native Bovine Enterokinase | Enteropeptidase (also called enterokinase) is an enzyme produced by cells of the duodenum and involved in human and animal digestion. It is secreted from intestinal glands (the crypts of Lieberkühn) following the entry of ingested food passing from the stomach. Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes. Absence of enteropeptidase results in intestinal digestion impairment. Enterokinase is a highly specific serine protease that is used for the removal of the flag peptide from n-terminal and met-n-terminal fusion proteins. it does not remove the c-terminal flag. Applications...ytic activation of trypsin from trypsinogen. enterokinase is used for site specific cleavage of recombinant fusion proteins containing an accessible enterokinase recognition site for removal of affinity tags. removes flag peptide from n-terminal and met-n-terminal fusion proteins. Group: Enzymes. Synonyms: enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Enzyme Commission Number: EC 3.4.21.9. CAS No. 9014-74-8. Enterokinase. Mole weight: 150 kDa (consisting of 115kDa and 35kDa subunits.). Activity: Type I, > 20 units/mg protein. Storage: -20°C. Form: powder. Source: Bovine intestine. Species: Bovine. enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Cat No: NATE-0224. | |
| Native Caldariomyces fumago Chloroperoxidase | Chloroperoxidase (CPO) is a 42 kDa Da extracellular heme glycoenzyme containing ferriprotoporphyrin IX as the prosthetic group. CPO is secreted from fungus and exhibits a broad spectrum of chemical reactivities. It is a peroxide-dependent chlorinating enzyme. It also catalyzes peroxidase-, catalase-and cytochrome P450-type reactions of dehydrogenation, H2O2 decomposition and oxygen insertion, respectively. The enzyme has magnetic and spectroscopic properties similar to that of cyctochrome P-450. CPO from the fungus Caldariomyces fumago has the capacity to chlorinate aromatic hydrocarbons, including polycyclic aromatic hydrocarbons (PAHs). Applications: A useful alternative to lactoperoxidase for 131i ion labeling studies, for bromination of proteins, and for cl labeling of macromolecules in long-term isolation procedures. Group: Enzymes. Synonyms: Chloroperoxidase; CPO; Vanadium halopero. Enzyme Commission Number: EC 1.11.1.10. CAS No. 9055-20-3. CPO. Activity: 1,000-2,000 units/mg protein (E1%/280); > 3,000 units/mL; >10,000 U/mL. Storage: 2-8°C. Form: buffered aqueous suspension. Purified suspension in 0.1 M sodium phosphate solution, pH approx. 4.5. Source: Caldariomyces fumago. Chloroperoxidase; CPO; Vanadium haloperoxidase; EC 1.11.1.10; 9055-20-3; Chloride Peroxidase; Chloride:hydrogen-peroxide oxidoreductase. Cat No: NATE-0156. | |
| Native Calf Enterokinase | Enteropeptidase (also called enterokinase) is an enzyme produced by cells of the duodenum and involved in human and animal digestion. It is secreted from intestinal glands (the crypts of Lieberkühn) following the entry of ingested food passing from the stomach. Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes. Absence of enteropeptidase results in intestinal digestion impairment. Applications: Enterokinase is used for the cleavage of fusion proteins at definite cleavage sites. for the processing of recombinant proteins, the desired protein is fused with enterokinase recognition sequence. after purification of the entire fusion protein, the protein or peptide is released by incubation with enterokinase. Group: Enzymes. Synonyms: enterokinase; enteropeptidase; EC 3.4.21.9; restriction protease enterokinase. Enzyme Commission Number: EC 3.4.21.9. CAS No. 9014-74-8. Enterokinase. Mole weight: 150 kDa. Storage: Store at 2-8°C. Form: Lyophilized. Source: Calf intestine. Species: Calf. enterokinase; enteropeptidase; EC 3.4.21.9; restriction protease enterokinase. Cat No: NATE-0872. | |
| Native Calf Rennin | Rennin, a 323 amino acid chain, is secreted as an inactive precursor which is then converted into an active enzyme through limited proteolysis. It cleaves the peptide bond between phenylalanine and methionine in K-Casein. Applications: Rennin, also known as chymosin, is a milkclotting acid proteinase produced in the stomach of a calf. it is used in cheesemaking and to study neonatal gastric digestion. Group: Enzymes. Synonyms: chymosin; rennin; EC 3.4.23.4; 9001-98-3. Enzyme Commission Number: EC 3.4.23.4. CAS No. 9001-98-3. Rennin. Activity: > 20 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing sodium chloride. Source: Calf stomach. Species: Calf. chymosin; rennin; EC 3.4.23.4; 9001-98-3. Cat No: NATE-0651. | |
| 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 Human α-Amylase | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Applications: Α-amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. α-amylase has been used in various plant studies, such as metabolism studies in arabidopsis. α-amylase from human saliva has been used to study the development of nutraceuticals, which may aid the treatment of diabetes and obesity. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9001-19-8. α-Amylase. Activity: 1,000-3,000 units/mg protein; 300-1,500 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing (NH4)2SO4 and sodium Citrate. Source: Human saliva. Species: Human. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Cat No: NATE-0743. | |
| Native Human Elastase | Neutrophil elastase is a serine proteinase in the same family as chymotrypsin and has broad substrate specificity. Secreted by neutrophils and macrophages during inflammation, it destroys bacteria and host tissue. It also localizes to Neutrophil extracellular traps (NETs), via its high affinity for DNA, an unusual property for serine proteases. Leuk ocyte elastase is a 29 kda serine endoprotease of the proteinase s1 family. it exists as a single 238 amino acid-peptide chain with four disulfide bonds. it contains two or thee n-linked glycans of variable composition which account for its three major isoforms. Applications: Elastase from creative enzymes has been used to digest fibro...mal models. Group: Enzymes. Synonyms: ELANE; elastase; EC 3.4.21.37; leukocyte elastase; ELA2; elastase 2; neutrophil elaszym; serine elastase; lysosomal elastase; neutrophil elastase; polymorphonuclear leukocyte elastase; elaszym; granulocyte elastase. Enzyme Commission Number: EC 3.4.21.37. CAS No. 9004-6-2. ELA2. Mole weight: 29 kDa. Activity: > 50 units/mg protein (Bradford). Storage: -20°C. Form: Lyophilized from 0.05 M sodium acetate (pH 5.5) and 0.6 M NaCl. Source: Human leuk ocytes. Species: Human. ELANE; elastase; EC 3.4.21.37; leukocyte elastase; ELA2; elastase 2; neutrophil elaszym; serine elastase; lysosomal elastase; neutrophil elastase; polymorphonuclear leukocyte ela | |
| Native Porcine α-Amylase | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Applications: Α-amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. this product is from porcine pancreas and is type i-a. α-amylase, from creative enzymes, has been used in various plant studies, such as metabolism studies in arabidopsis. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9001-19-8. α-Amylase. Mole weight: 51-54 kDa. Activity: > 1000 units/mg protein (E1%/280); > 10 units/mg solid; 700-1400 units/mg protein (E1%/280). Storage: 2-8°C. Form: saline suspension. Suspension in 2.9 M NaCl solution containing 3 mM CaCl2. Source: Porcine pancreas. Species: Porcine. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Cat No: NATE-0745. | |
| Native Porcine Angiotensin Converting Enzyme | Angiotensin-converting enzyme (EC 3.4.15.1), or "ACE" indirectly increases blood pressure by causing blood vessels to constrict. It does that by converting angiotensin I to angiotensin II, which constricts the vessels. For this reason, drugs known as ACE inhibitors are used to lower blood pressure. ACE, angiotensin I and angiotensin II are part of the renin-angiotensin system (RAS), which controls blood pressure by regulating the volume of fluids in the body. ACE is secreted in the lungs and kidneys by cells in the endothelium (inner layer) of blood vessels. Ace is a monomer with molecular weight of ~170 kda ph range for activity: 7-8.5 temperature optimum: 37°c zinc is...-82-1. Angiotensin Converting Enzyme. Activity: > 10 units/mg protein (Bradford). Storage: -20°C. Form: Lyophilized powder containing Tris buffer salts. Source: Porcine kidney. Species: Porcine. ACE; Angiotensin Converting Enzyme; EC 3.4.15.1; dipeptidyl carboxypeptidase I; peptidase P; dipeptide hydrolase, peptidyl dipeptidase; angiotensin converting enzyme; kininase II; angiotensin I-converting enzyme; carboxycathepsin; dipeptidyl carboxypeptidase; "hypertensin converting enzyme" peptidyl dipeptidase I; peptidyl-dipeptide hydrolase; peptidyldipeptide hydrolase; endothelial cell peptidyl dipeptidase; peptidyl dipeptidase-4; PDH; peptidyl dipeptide hydrolase; DCP. Cat N | |
| Native Porcine Colipase | Colipase is a protein co-enzyme required for optimal enzyme activity of pancreatic lipase. It is secreted by the pancreas in an inactive form, procolipase, which is activated in the intestinal lumen by trypsin. Its function is to prevent the inhibitory effect of bile salts on the lipase-catalyzed intraduodenal hydrolysis of dietary long-chain triglycerides. In humans, the colipase protein is encoded by the CLPS gene. Applications: Pancreatic colipase is a required co-factor for pancreatic lipase, being necessary for its activity during hydrolysis of dietary triglycerides in the presence of bile salts. Group: Enzymes. Synonyms: CLPS; colipase; pancreatic colipase. CLPS. Activity: 10 KU-20 KU/mL. Appearance: Colourless liquid. Form: Liquid. Source: Porcine pancreas. Species: Porcine. CLPS; colipase; pancreatic colipase. Cat No: NATE-0144. | |
| Native Porcine Enterokinase | Enteropeptidase (also called enterokinase) is an enzyme produced by cells of the duodenum and involved in human and animal digestion. It is secreted from intestinal glands (the crypts of Lieberkühn) following the entry of ingested food passing from the stomach. Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes. Absence of enteropeptidase results in intestinal digestion impairment. Applications: Enterokinase from porcine intestine has been used in a study to report a new experimental model of the anomalous pancreatico-biliary junction. enterokinase from porcine intestine has also ...peptide. the enzyme from creative enzymes has been used for the activation of trypsinogen in order to measure the activity of trypsin in hog pancreas. the study showed that antimicrobial treatment reduces intestinal microflora and improves protein digestive capacity without changes in villous structure of weanling pigs. Group: Enzymes. Synonyms: enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Enzyme Commission Number: EC 3.4.21.9. CAS No. 9014-74-8. Enterokinase. Activity: Type I, > 20 units/mg protein. Storage: -20°C. Form: salt-free, lyophilized powder. Source: Porcine intestine. Species: Porcine. enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Cat No: NATE-0225. | |
| Native Porcine Pancreozymin | Cholecystokinin is a peptide hormone of the gastrointestinal system responsible for stimulating the digestion of fat and protein. Cholecystokinin, previously called pancreozymin, is synthesized by I-cells in the mucosal epithelium of the small intestine and secreted in the duodenum, the first segment of the small intestine, and causes the release of digestive enzymes and bile from the pancreas and gallbladder, respectively. It also acts as a hunger suppressant. Recent evidence has suggested that it also plays a major role in inducing drug tolerance to opioids like morphine and heroin, and is partly implicated in experiences of pain hypersensitivity during opioid withdrawal. Applications: Cholecystokinin (cck) is a peptide hormone of the gastrointestinal system responsible for stimulating the digestion of fat and protein. it is used to study brain, kidney and pancreatic functioning as well as reproductive behavior and glucose tolerance. Group: Enzymes. Synonyms: Cholecystokinin, CCK, CCK-PZ; 9011-97-6; Pancreozymin. CAS No. 9011-97-6. CCK. Activity: 2-6 Crick units/mg solid. Storage: 2-8°C. Source: Porcine intestine. Species: Porcine. Cholecystokinin, CCK, CCK-PZ; 9011-97-6; Pancreozymin. Cat No: NATE-0113. | |
| Native Pseudomonas atlantica Agarase | Agarase is an enzyme with system name agarose 4-glycanohydrolase. It found in agarolytic bacteria and is the first enzyme in the agar catabolic pathway. It is responsible for allowing them to use agar as their primary source of Carbon and enables their ability to thrive in the ocean. Agarases are classified as either α-agarases or β-agarases based upon whether they degrade αor β linkages in agarose, breaking them into oligosaccharides. When secreted, α-agarases yield oligosaccharides with 3.6 anhydro-L-galactose at the reducing end whereas β-agarases result in D-galactose residues. Group: Enzymes. Synonyms: agarase; AgaA; AgaB; endo-β-agarase; agarose 3-glycanohydrolase; EC 3.2.1.81; 37288-57-6. Enzyme Commission Number: EC 3.2.1.81. CAS No. 37288-57-6. Agarase. Activity: > 5,000 units/mg protein (Lowry). Storage: 2-8°C. Form: lyophilized powder. Contains phosphate buffer salts. May contain bovine serum albumin to standardize protein content. Source: Pseudomonas atlantica. agarase; AgaA; AgaB; endo-β-agarase; agarose 3-glycanohydrolase; EC 3.2.1.81; 37288-57-6. Cat No: NATE-0040. | |
| Native Rabbit Angiotensin Converting Enzyme | Angiotensin-converting enzyme (EC 3.4.15.1), or "ACE" indirectly increases blood pressure by causing blood vessels to constrict. It does that by converting angiotensin I to angiotensin II, which constricts the vessels. For this reason, drugs known as ACE inhibitors are used to lower blood pressure. ACE, angiotensin I and angiotensin II are part of the renin-angiotensin system (RAS), which controls blood pressure by regulating the volume of fluids in the body. ACE is secreted in the lungs and kidneys by cells in the endothelium (inner layer) of blood vessels. Group: Enzymes. Synonyms: ACE; Angiotensin Converting Enzyme; EC 3.4.15.1; dip. Enzyme Commission Number: EC 3.4.15.1. CAS No. 9015-82-1. Angiotensin Converting Enzyme. Activity: > 2.0 units/mg protein (modified Warburg-Christian). Form: lyophilized powder. Source: Rabbit lung. Species: Rabbit. ACE; Angiotensin Converting Enzyme; EC 3.4.15.1; dipeptidyl carboxypeptidase I; peptidase P; dipeptide hydrolase, peptidyl dipeptidase; angiotensin converting enzyme; kininase II; angiotensin I-converting enzyme; carboxycathepsin; dipeptidyl carboxypeptidase; "hypertensin converting enzyme" peptidyl dipeptidase I; peptidyl-dipeptide hydrolase; peptidyldipeptide hydrolase; endothelial cell peptidyl dipeptidase; peptidyl dipeptidase-4; PDH; peptidyl dipeptide hydrolase; DCP. Cat No: NATE-0015. | |
| Native Rat Angiotensin Converting Enzyme | Angiotensin-converting enzyme (EC 3.4.15.1), or "ACE" indirectly increases blood pressure by causing blood vessels to constrict. It does that by converting angiotensin I to angiotensin II, which constricts the vessels. For this reason, drugs known as ACE inhibitors are used to lower blood pressure. ACE, angiotensin I and angiotensin II are part of the renin-angiotensin system (RAS), which controls blood pressure by regulating the volume of fluids in the body. ACE is secreted in the lungs and kidneys by cells in the endothelium (inner layer) of blood vessels. Applications: Positive control. Group: Enzymes. Synonyms: ACE; Angiotensin Converting Enzyme; EC 3.4.15.1; dipeptid....1 M phosphate buffer and 300 mM NaCl at pH 8.3 at 37°C. Storage: Maintain at -20°C in undiluted aliquots for up to 6 months. Avoid repeated freeze/thaw cycles. Form: Liquid in 100 mM phosphate buffered saline, 150 mM NaCl, pH 7.4 with 0.2mM CHAPS. Source: Rat lung. Species: Rat. ACE; Angiotensin Converting Enzyme; EC 3.4.15.1; dipeptidyl carboxypeptidase I; peptidase P; dipeptide hydrolase, peptidyl dipeptidase; angiotensin converting enzyme; kininase II; angiotensin I-converting enzyme; carboxycathepsin; dipeptidyl carboxypeptidase; "hypertensin converting enzyme" peptidyl dipeptidase I; peptidyl-dipeptide hydrolase; peptidyldipeptide hydrolase; endothelial cell peptidy | |
| Native Staphylococcus aureus α-Hemolysin | α-Hemolysin is a 33 kDa extracellular protein secreted by most strains of pathogenic Staphylococcus aureus. It is selectively hemolytic and has a marked preference for rabbit red blood cells. It induces dermonecrosis, spastic muscle paralysis, and it is lethal for laboratory animals. The toxin must be in the monomeric form to initially bind to a membrane and specific receptors are not required for binding. Upon binding to biological membranes and/or artificial membranes, self-oligomerization occurs, resulting in ring structures (hexameric aggregates) believed to represent transmembrane pores, which are permeable to ions and small metabolites. Group: Enzymes. Synonyms: α-Hemolysin; 94716-94-6; α-Toxin. α-Hemolysin. Activity: > 10,000 units/mg protein. Storage: 2-8°C. Source: Staphylococcus aureus. α-Hemolysin; 94716-94-6; α-Toxin. Cat No: NATE-0753. | |
| Native Staphylococcus aureus Staphopain A | Staphopains A and B are part of the staphylococcal proteolytic cascade (SPC) and may contribute to tissue invasion and metastatic infections of Staphylococcus aureus. Staphopain A, along with Staphopain B, may contribute to septic shock through the release of bradykinin and S-kinin from human kininogens. This activity required proteolytically-active Staphopain A and was augmented by Staphopain B. Staphopain a is inhibited by staphostatin a, e-64, and heavy metal ions such as hg2+ and ag+. staphopain a is also inhibited by plasma α2-macroglobulin but not by human cystatin c. staphopain a and staphopain b, members of the peptidase c47 family, are the major cysteine proteases secreted by s. aureus. Applications: Staphopain a was used for cleaving the n terminus of atypical chemokine receptor (ackr2) to suppress its ligand internalization activity in a study on the pivotal role of ackr2 in ligand binding, internalization and scavenging of inflammatory responses. Group: Enzymes. Synonyms: Staphopain; EC 3.4.2. Enzyme Commission Number: EC 3.4.22.48. CAS No. 347841-89-8. Staphopain. Mole weight: mol wt ~20 kDa by SDS-PAGE. Storage: -20°C. Form: lyophilized powder. Source: Staphylococcus aureus. Staphopain; EC 3.4.22.48; staphylopain; 347841-89-8; ScpA; Staphopain A; Staphylococcal cysteine proteinase A; Staphylopain A. Cat No: NATE-0666. | |
| Native Staphylococcus aureus Staphopain B | Staphopains A and B are part of the staphylococcal proteolytic cascade (SPC) and may contribute to tissue invasion and metastatic infections of Staphylococcus aureus. Staphopain A, along with Staphopain B, may contribute to septic shock through the release of bradykinin and S-kinin from human kininogens. This activity required proteolytically-active Staphopain A and was augmented by Staphopain B. Staphopain activity is inhbited by staphostatin b (sspc) and e-64. staphopain activity is stimulated by edta. staphopain a and staphopain b, members of the peptidase c47 family, are the major cysteine proteases secreted by s. aureus. Group: Enzymes. Synonyms: Staphopain; EC 3.4.22.48; staphylopain; 347841-89-8; Staphopain B; Staphylococcal cysteine proteinase B; Staphylopain B; sspB. Enzyme Commission Number: EC 3.4.22.48. CAS No. 347841-89-8. Purity: > 95% (SDS-PAGE). Staphopain. Mole weight: mol wt ~20 kDa by SDS-PAGE. Storage: -20°C. Source: Staphylococcus aureus. Staphopain; EC 3.4.22.48; staphylopain; 347841-89-8; Staphopain B; Staphylococcal cysteine proteinase B; Staphylopain B; sspB. Cat No: NATE-0683. | |
| Native Streptococcus hemolyticus 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. Streptokinase from β-hemolytic streptococcus (lancefield group c). Applications: Streptokinase is commonly used as a thrombolytic agent in the therapy of ischemic stroke. this therapy carries the important risk of intracerebral hemorrhage. streptokinase is also used in the treatment of complicated parapneumonic effusions and empyema where adverse reactions, allergic type, are rare. Group: Enzymes. Synonyms: St. Enzyme Commission Number: EC 3.4.99.0. CAS No. 9002-1-1. SK. Activity: > 3,500 units/mg solid. Appearance: Appearance (Color): Conforms to Requirements Off-White to Light Yellow to Light Beige. Form: Lyophilized powder containing ~50% total protein by biuret and sodium glutamate. Total protein composed of enzyme protein and human serum albumin. Source: Streptococcus hemolyticus. Streptokinase; SK; EC 3.4.99.0. Cat No: PHAM-261. | |
| Native Streptococcus pyogenes Streptolysin O | Streptolysin O possesses a single polypeptide chain with a molecular weight of f62 kDa. Streptolysin O binds to membrane cholesterol and oligomerizes to create a ring structure that consists of 45 to 50 units. The ring structure inserts into the membrane to make a large pore (25 to 30 nm), which DNA, RNA, peptides and proteins may pass. It is thiol-activated. It is inhibited by allicin, an active component of garlic. Applications: Permeabilizes membranes to permit cellular uptake of large or charged molecules. streptolysin o is a toxin secreted by streptococcus pyogenes and is a prototype member of poreforming bacterial cytolysins. it is used permeabilize cell membranes to permit cellular uptake of large or charged molecules. it is used to study macromolecule delivery. it is a potential anticancer agent and is used to study suicide cancer gene therapy. Group: Enzymes. Synonyms: Streptolysin O; 98072-47-0; SLO. CAS No. 98072-47-0. SLO. Mole weight: 69 kDa. Storage: 2-8°C. Form: lyophilized powder. Source: Streptococcus pyogenes. Streptolysin O; 98072-47-0; SLO. Cat No: NATE-0671. | |
| Neuronal Specific Enolase (His Tag) from Human, Recombinant | NSE is the γ isoform of the glycolytic enzyme enolase and is expressed primarily in neurons, in normal and neoplastic neuroendocrine cells. NSE is a highly soluble cytoplasmic protein that is readily secreted into the CSF and serum following tissue damage. NSE shows neurotrophic and neuroprotective properties on a broad spectrum of central nervous system (CNS) neurons and binds in a calcium-dependent manner to cultured neocortical neurons promoting cell survival. Neuron specific enolase human recombinant is expressed in e. coli containing 433 amino acids 2-434 fused to an amino terminal hexahistidine tag. the nse is purified by proprietary chromatographic ...y: Greater than 95% as determined by SDS-PAGE. Single band on Western Blot. Enolase. Stability: Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. Please prevent freeze-thaw cycles. Appearance: Sterile Filtered clear solution. Source: E. coli. Species: Human. EC 4.2.1.11; Neuron Specific Enolase; NSE; 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; phosphopyruvate hydratase. Cat No: NATE-0903. | |
| O-sialoglycoprotein endopeptidase | An enzyme secreted by the bacterium Pasteurella haemolytica. Inhibited by EDTA (100 mM) and 1,10-phenanthroline. Type example of peptidase family M22. Group: Enzymes. Synonyms: glycoprotease; glycophorin A proteinase; glycoproteinase; sialoglycoprotease; sialoglycoproteinase. Enzyme Commission Number: EC 3.4.24.57. CAS No. 129430-53-1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4339; O-sialoglycoprotein endopeptidase; EC 3.4.24.57; 129430-53-1; glycoprotease; glycophorin A proteinase; glycoproteinase; sialoglycoprotease; sialoglycoproteinase. Cat No: EXWM-4339. | |
| Pepsin | Pepsin is a digestive enzyme: It is extracted from Pepsinogen under pH 1.5-5.0 and the pepsinogen is secreted by the stomach cell. Pepsin can decompose the solidified proteins into peptone by effect of stomach acid, but it can not go any further to amino acid. The best effective condition for pepsin is pH 1.6-1.8. Applications: It is widely used for the dyspepsia caused by over taking proteinic foods and lack of stomach proteinase caused by digestive hypofunction in the recovering period. it also has effect on curing chronic atrophic gastritis, gastric cancer and malignant anaemia. pepsin is extracted from porcine gastric mucosa through our exclusive skill. Group: Enzymes. Synonyms: EC 3.4.23.1; Pepsin. CAS No. 9001-75-6. Pepsin. Appearance: inquire. EC 3.4.23.1; Pepsin. Pack: inquire. Cat No: DIS-1033. | |
| phenazine-1-carboxylate N-methyltransferase | The enzyme, characterized from the bacterium Pseudomonas aeruginosa, is involved in the biosynthesis of pyocyanin, a toxin produced and secreted by the organism. The enzyme is active in vitro only in the presence of EC 1.14.13.218, 5-methylphenazine-1-carboxylate 1-monooxygenase. Group: Enzymes. Synonyms: phzM (gene name). Enzyme Commission Number: EC 2.1.1.327. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1935; phenazine-1-carboxylate N-methyltransferase; EC 2.1.1.327; phzM (gene name). Cat No: EXWM-1935. | |
| presilphiperfolanol synthase | Requires Mg2+. Presilphiperfolan-8β-ol is the precursor of botrydial, a phytotoxic sesquiterpene metabolite secreted by the fungus Botryotinia fuckeliana (Botrytis cinerea), the causal agent of gray mold disease in plants. Group: Enzymes. Synonyms: BcBOT2, CND15. Enzyme Commission Number: EC 4.2.3.74. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5236; presilphiperfolanol synthase; EC 4.2.3.74; BcBOT2, CND15. Cat No: EXWM-5236. | |
| Pro-Pro endopeptidase | This metalloprotease, which is secreted by the bacterium Peptoclostridium difficile, contains zinc. Group: Enzymes. Synonyms: metalloprotease CD2830. Enzyme Commission Number: EC 3.4.24.89. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4373; Pro-Pro endopeptidase; EC 3.4.24.89; metalloprotease CD2830. Cat No: EXWM-4373. | |
| Prostatic acid phosphatase from Human, recombinant | ACPP, also known as prostatic acid phosphatase isoform PAP, is a type I integral membrane protein of the plasma membrane and lysosomes, and a secreted form also exists. The concentration of ACPP is elevated in the circulation of prostate cancer patients, making the enzyme a marker for the progression of prostate cancer. Recombinant human ACPP, fused to His-tag at C-terminus, was expressed in insect cell and purified by using conventional chromatography techniques. Group: Enzymes. Synonyms: Prostatic acid phosphatase; PAP; prostatic specific acid phosphatase; PSAP; EC 3.1.3.2; ACP; Acid Phos; 5'-nucleotidase; 5'-NT; Ecto-5'-nucleotidase; Thiamine monophosphatase; TMPase; PAPf39; ACPP; ACP-3, ACP3. Enzyme Commission Number: EC 3.1.3.2. CAS No. 9001-77-8. Purity: > 95% by SDS-PAGE. Apase. Mole weight: 41.8 kDa. Activity: >100,000 units/mg. Storage: Can be stored at 4°C short term (1-2 weeks). For long term storage, aliquot and store at -70°C. Avoid repeated freezing and thawing cycles. Form: Liquid. Source: Baculovirus. Species: Human. Prostatic acid phosphatase; PAP; prostatic specific acid phosphatase; PSAP; EC 3.1.3.2; ACP; Acid Phos; 5'-nucleotidase; 5'-NT; Ecto-5'-nucleotidase; Thiamine monophosphatase; TMPase; PAPf39; ACPP; ACP-3, ACP3. Cat No: NATE-1673. | |
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