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| Product | Description | |
|---|---|---|
| Alkaline Protease for detergent | Protease is a kind of enzyme preparation produced by one microbes submerged fermentation. It is also a kind of modified enzyme preparation after DNA recombination. As a common used enzyme preparation in detergent industry, the main activated composition alkaline protease can rapidly decompose protein. Protease can hydrolyze the hardly soluble protein on fabric into soluble peptide chain and amino acid in detergent solution. smoothness. Therefore, after the washing with cellulase, white clothes will be whiter and color clothes will be brighter and softer. At the same time, it can get off the granular dirt in the fiber. Applications: Protease can effectively remove sweat stain, blood stains, food protein dirt, cream stain and etc, the detergent contains protease will make fabric get perfect effect after washing. Group: Enzymes. Synonyms: Alkaline Protease; for detergent; Protease; decompose protein; Detergent Enzymes; Detergents; Alkaline Protease for detergent; DETE-2623. CAS No. 37259-58-8. Alkaline Protease. Appearance: powder or liquid. Alkaline Protease; for detergent; Protease; decompose protein; Detergent Enzymes; Detergents; Alkaline Protease for detergent; DETE-2623. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form). Cat No: DETE-2623. |  |
| Concentrated alkaline protease for Medical | Concentrated, alkaline protease enzyme used in medical and surgical instrument cleaning products to remove protein-containing, organic materials such as blood, mucus, feces and foods. Applications: Laundry. Group: Enzymes. Synonyms: alkaline protease; Concentrated alkaline protease for Medical; alkaline protease enzyme; medical; surgical instrument ; cleaning; Detergents; Concentrated alkaline protease for Medical; DETE-2631. CAS No. 37259-58-8. Alkaline Protease. Appearance: powder or liquid. alkaline protease; Concentrated alkaline protease for Medical; alkaline protease enzyme; medical; surgical instrument ; cleaning; Detergents; Concentrated alkaline protease for Medical; DETE-2631. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form). Cat No: DETE-2631. | |
| Native Bacillus licheniformis Alkaline Protease | Proteinase catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate. Subtilisin a is a member of the serine s8 endoproteinase family. it has broad specificity with a preference for a large uncharged residue in the p1 position. it hydrolyzes native and denatured proteins, and is active under alkaline conditions. Applications: The enzyme has been used to optimize release of all mitochondrial populations from homogenized ventricular tissue of rat heart.1 it has also been used in the pre-hybridisation treatment of formalin fixed, paraffin wax...ex); MCP; proteasome; large multicatalytic protease; multicatalytic proteinase; proteasome organelle; alkaline protease; 26S protease; triCorn proteinase; triCorn protease; EC 3.4.25.1. Enzyme Commission Number: EC 3.4.25.1. CAS No. 140879-24-9. Alkaline Protease. Mole weight: 27 Kda. Activity: 7.0-14.0 units/mg. Form: lyophilized powder. Source: Bacillus licheniformis. ingensin; macropain; multicatalytic endopeptidase complex; prosome; multicatalytic proteinase (complex); MCP; proteasome; large multicatalytic protease; multicatalytic proteinase; proteasome organelle; alkaline protease; 26S protease; triCorn proteinase; triCorn protease; EC 3.4.25.1. Cat No: NATE-0444. | |
| Neutral/alkaline protease for meat proteins | Concentrated neutral - alkaline pH protease enzyme used to hydrolyze protein into smaller polypeptides and free amino acids. It is often combined with a neutral to acid pH protease for more complete processing. Applications: Meat & fish proteins. Group: Enzymes. Neutral/alkaline protease. Appearance: powder or liquid. protease; Neutral - alkaline protease; for meat proteins; Meat and Fish Proteins; neutral - alkaline protease enzyme; alkaline protease; Neutral protease; PRO-1823. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form). Cat No: PRO-1823. | |
| Neutral/alkaline protease for vegetable proteins | A concentrated, neutral - alkaline pH protease enzyme used as a processing aid in technical applications to break down protein and increase their solubility, dispersability and digestibility. Applications: Vegetable proteins. Group: Enzymes. Neutral/alkaline protease. Appearance: powder or liquid. protease; Neutral - alkaline protease; for meat proteins; Meat and Fish Proteins; neutral - alkaline protease enzyme; alkaline protease; Neutral protease; PRO-1823. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form). Cat No: PRO-1824. | |
| 1-[N2, N6-Bis[ (phenylmethoxy) carbonyl]-L-lysyl]-L-proline Phenylmethyl Ester | 1-[N2, N6-Bis[ (phenylmethoxy) carbonyl]-L-lysyl]-L-proline Phenylmethyl Ester is an intermediate in the biosynthesis of secondary amines for alkaline protease catalysis studies. Group: Biochemicals. Grades: Highly Purified. CAS No. 145435-28-5. Pack Sizes: 25mg, 100mg. Molecular Formula: C34H39N3O7. US Biological Life Sciences. |  Worldwide |
| Immobilized Proteinase K on G3m | Proteinase K is an unspecific serine protease with strong proteolytic activity on denatured (in SDS) and high molecular weight native proteins. It cleaves peptide bonds mostly after the carboxyl group of N-substituted hydrophobic, aliphatic and aromatic amino acids. G3m: 25 ug proteinase K immobilized on matrix G3m per CR-column. 0.7 mAnson units immobilized per CR-column. This CR-column cuts at least 370 ug BSA per application. Nr. 5 Storage buffer: 50 mM Tris/HCl, pH 7. 5Nr. 16 Reaction buffer: 50 mM Tris/HCl, 5 mM NaCl, pH 8. 0Nr. 17 Washing buffer: 50 mM Tris/HCl, 1. 0 M NaCl, pH 8. 0The columns are more active in 0.1% SDS and at 40°C. Also active in PBS buffer (20 mM Na-phosphate, 150 mM NaCl at pH 7. 6). Group: Enzymes. Synonyms: Tritirachium alkaline proteinase; Tritirachium album serine proteinase; proteinase K; Tritirachium album proteinase K; endopeptidase K; EC 3. 4. 21. 64; 39450-01-6. Enzyme Commission Number: EC 3. 4. 21. 64. Purity: Chromatographically purified, free of ribo- and deoxyribonucleases. Storage: 4 °C. Source: Tritirachium album. Tritirachium alkaline proteinase; Tritirachium album serine proteinase; proteinase K; Tritirachium album proteinase K; endopeptidase K; EC 3. 4. 21. 64; 39450-01-6; Immobilized Proteinase K. Cat No: NATE-1768. | |
| lysyl endopeptidase | From Achromobacter lyticus. Enzymes with similar specificity are produced by Lysobacter enzymogenes (Endoproteinase Lys-C;) and Pseudomonas aeruginosa (Ps-1;). In peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: Achromobacter proteinase I (also see Comment); Achromobacter lyticus alkaline proteinase I; protease I; achromopeptidase; lysyl bond specific proteinase. Enzyme Commission Number: EC 3.4.21.50. CAS No. 123175-82-6. Achromopeptidase. 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-4144; lysyl endopeptidase; EC 3.4.21.50; 123175-82-6; Achromobacter proteinase I (also see Comment); Achromobacter lyticus alkaline proteinase I; protease I; achromopeptidase; lysyl bond specific proteinase. Cat No: EXWM-4144. | |
| Native Achromobacter lyticus Achromopeptidase | Lysyl endopeptidase (EC 3.4.21.50, Achromobacter proteinase I, Achromobacter lyticus alkaline proteinase I, protease I, achromopeptidase, lysyl bond specific proteinase) is an enzyme. This enzyme catalyses the following chemical reaction:Preferential cleavage:Lys-, including-Lys-Pro-. This enzyme is isolated from Achromobacter lyticus. Group: Enzymes. Synonyms: Achromobacter proteinase I; Achromobacter lyticus alkaline proteinase I; protease I; achromopeptidase; lysyl bond specific proteinase; EC 3.4.21.50; 123175-82-6; Lysyl endopeptidase. Enzyme Commission Number: EC 3.4.21.50. CAS No. 123175-82-6. Achromopeptidase. Storage: -20°C. Form: lyophilized powder, Protein ~5 % by biuret, 300-600 units/mg solid. Source: Achromobacter lyticus. Achromobacter proteinase I; Achromobacter lyticus alkaline proteinase I; protease I; achromopeptidase; lysyl bond specific proteinase; EC 3.4.21.50; 123175-82-6; Lysyl endopeptidase. Cat No: NATE-0021. | |
| Native Bacillus licheniformis Protease | Protease catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate. Protease is a serine endoproteinase with a broad specificity towards native and denatured proteins, and is active under alkaline conditions. It is active in some organic solvents such as dry octane. The enzyme is found to be stable at ph 8-10, retaining activity of up to 90% for 24 hours. it shows maximum activity at temperatures between 55-60°c. Applications: The product has been used with other enzymes for in situ proteolysis to produce crystals suitable for structure determi...f bacillus licheniformis. it is a serine endoproteinase with a broad specificity towards native and denatured proteins, and is active under alkaline conditions. Group: Enzymes. Synonyms: Protease; 9014-01-1; Subtilisin A; EC 3.4.21.62; Alcalase. Enzyme Commission Number: EC 3.4.21.62. CAS No. 9001-92-7. Protease. Mole weight: Subtilisin is a non-glycosylated single polypeptide chain without disulfide bonds and has a molecular weight of 27 KDa. Activity: Type VIII, 7-15 units/mg solid; Type I, > 2.4 U/g. Form: Type VIII, lyophilized powder; Type I, aqueous solution. Source: Bacillus licheniformis. Protease; 9014-01-1; Subtilisin A; EC 3.4.21.62; Alcalase. Cat No: NATE-0633. | |
| Native Bacillus licheniformis Proteinase | Proteinase catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate. Subtilisin is a non-glycosylated single polypeptide chain without disulfide bonds and has a molecular weight of 27 kda. Applications: The enzyme from creative enzymes has been used to optimize release of all mit ochondrial populations from homogenized ventricular tissue of rat heart. it has also been used in the pre-hybridisation treatment of formalin fixed, paraffin wax-embedded liver specimens for detecting human and viral dna. this is a proteolytic enzyme isolated from th...ls to study the silencing of cardiac mit ochondrial nhe1. Group: Enzymes. Synonyms: protease; peptidase; proteinase; EC 3.4.21.62; 9014-01-1; Alkaline Protease; Protease from Bacillus licheniformis; Proteinase from Bacillus licheniformis; Subtilo peptidase A. Enzyme Commission Number: EC 3.4.21.62. CAS No. 9001-92-7. Purity: crystallization. Proteinase. Mole weight: 27 KDa. Activity: 7.0-14.0 units/mg solid. Storage: -20°C. Form: lyophilized powder. Source: Bacillus licheniformis. protease; peptidase; proteinase; EC 3.4.21.62; 9014-01-1; Alkaline Protease; Protease from Bacillus licheniformis; Proteinase from Bacillus licheniformis; Subtilo peptidase A. Cat No: NATE-0639. | |
| Native Bacteria Achromopeptidase | Lysyl endopeptidase (EC 3.4.21.50, Achromobacter proteinase I, Achromobacter lyticus alkaline proteinase I, protease I, achromopeptidase, lysyl bond specific proteinase) is an enzyme. This enzyme catalyses the following chemical reaction:Preferential cleavage:Lys-, including-Lys-Pro-. This enzyme is isolated from Achromobacter lyticus. Hemolysins are lipids and proteins that cause lysis of red blood cells by destroying their cell membrane. although the lytic activity of some microbe-derived hemolysins on red blood cells may be of great importance for nutrient acquisition, many hemolysins produced by pathogens do not cause significant destruction of red blood cells during infe...and the effect of ciprofloxacin on biofilm formation. Group: Enzymes. Synonyms: Achromobacter proteinase I; Achromobacter lyticus alkaline proteinase I; protease I; achromopeptidase; lysyl bond specific proteinase; EC 3.4.21.50; 123175-82-6; Lysyl endopeptidase. Enzyme Commission Number: EC 3.4.21.50. CAS No. 123175-82-6. Achromopeptidase. Mole weight: ~27 kDa. Activity: > 1,000 units/mg solid; > 20,000 units/mg solid. Storage: 2-8°C. Form: lyophilized powder. Source: Bacteria. Achromobacter proteinase I; Achromobacter lyticus alkaline proteinase I; protease I; achromopeptidase; lysyl bond specific proteinase; EC 3.4.21.50; 123175-82-6; Lysyl endopeptidase. Cat No: NATE-0022. | |
| Native Lysobacter enzymogenes Endoproteinase Lys-C | Endoproteinase Lys-C inactivates the enzyme inositol monophosphatase by cleaving it at a single site directly after Lys 36. Endoproteinase lys-c is an enzyme that preferentially cleaves at the carboxyl side of lysine residues. Applications: Endoproteinase lys-c from lysobacter enzymogenes is useful in the determination of primary structures of proteins. it has been used in a study to investigate the evidence for trisulfide bonds in a recombinant variant of a human igg2 mon oclonal antibody. endoproteinase lys-c has been used for the digestion mon oclonal antibodies for disulfide bond assignment. Group: Enzymes. Synonyms: EC 3.4.21.50; chromobacter proteinase I; Achromobacter lyticus alkaline proteinase I; protease I; achromopeptidase; lysyl bond specific proteinase; 72561-05-8; Achromobacter proteinase I; Endoproteinase Lys-C. Enzyme Commission Number: EC 3.4.21.50. CAS No. 72561-05-8. Achromopeptidase. Storage: 2-8°C. Form: lyophilized powder. Source: Lysobacter enzymogenes. EC 3.4.21.50; chromobacter proteinase I; Achromobacter lyticus alkaline proteinase I; protease I; achromopeptidase; lysyl bond specific proteinase; 72561-05-8; Achromobacter proteinase I; Endoproteinase Lys-C. Cat No: NATE-0220. | |
| Native Streptomyces griseus Protease | Protease from Streptomyces griseus is a mixture of at least three proteolytic activities including an extracellular serine protease. In general, serine proteases display a wide range of substrate specificities, which are believed to be mediated by an active site composed of one Asp, one His, and a Ser residue in the molecule. This enzyme prefers to hydrolyze peptide bonds on the carboxyl side of glutamic or aspartic acid. Collected from culture broth of s. griseus and purified by successive column procedures. a mixture of at least three proteolytic activities including an extracellular serine protease. in general, serine proteases display a wide range of substrate specifici...de aldehydes and serine proteases. protease is typically used in nucleic acid isolation procedures in incubations of 0.5-3.0 hours supplemented with 0.2% sodium dodecyl sulfate and 10 mm edta. the enzyme from creative enzymes has been used for the digestion and analysis of antithrombin-heparin complexes. it has also been used for the isolation of enzyme-resistant starch. this enzyme is more active at a higher ph range than the known alkaline protease, showing the proteolytic activity even in 0.2n naoh solution. this enzyme is useful for proteolysis of insoluble protein and for structure investigation of protein. Group: Enzymes. Synonyms: Protease; 9036-06-0; Actinase E, Pro | |
| Native Streptomyces sp. Alkalophilic proteinase | Native Streptomyces sp. Alkalophilic proteinase. Applications: This enzyme is more active at a higher ph range than the known alkaline protease, showing the proteolytic activity even in 0.2n naoh solution. this enzyme is useful for proteolysis of insoluble protein and for structure investigation of protein. Group: Enzymes. Synonyms: Alkalophilic proteinase; EC 3.4.21.-. Enzyme Commission Number: EC 3.4.21.-. Alkalophilic proteinase. Mole weight: approx. 50 kDa. Activity: Grade ? 20U/mg-solid or more. Stability: Stable at-20?C for at least one year. Appearance: White amorphous powder, lyophilized. Form: Freeze dried powder. Source: Streptomyces sp. Alkalophilic proteinase; EC 3.4.21.-. Cat No: DIA-183. | |
| Native Tritirachium album limber Proteinase K | Proteinase K (PROK) is a serine protease with broad specificity towards aliphatic, aromatic and other hydrophobic amino acids. PROK has a molecular weight of 27,000 daltons and is Ca2+ dependent. It is not inactivated by metal ion chelating agents such as EDTA, sulfhydryl reagents, PCMB, TLCK, or TPCK. It also retains activity in 0.5% SDS. It can be inhibited by PMSF or DFP. Applications: Useful for the proteolytic inactivation of nucleases during the isolation of dna and rna. removes endotoxins that bind to cationic proteins such as lysozyme and ribonuclease a. reported useful for the isolation of hepatic, yeast, and mung bean mit ochondria determination of enzyme l o...oteinase; Tritirachium album proteinase K; endopeptidase K; 39450-01-6; protease K. Enzyme Commission Number: EC 3.4.21.64. CAS No. 39450-01-6. Purity: Purified to remove DNase and RNase. Proteinase K. Mole weight: 27 kDa. Activity: Type I, > 20 units per mg dry weight; Type II, > 400 u/ml. Storage: Powder: 2-8°C; Liquid: -20°C. Form: Type I, powder; Type II, Liquid in 20mg/ml in 10mM Tris-HCl, 1mM calcium acetate, pH 7.5 containing 50% glycerol. Source: Tritirachium album limber. Proteinase K; EC 3.4.21.64; Tritirachium alkaline proteinase; Tritirachium album serine proteinase; Tritirachium album proteinase K; endopeptidase K; 39450-01-6; protease K. Cat No: NATE-0637. | |
| oligopeptidase B | Known from Escherichia coli. Inhibited by Tos-Lys-CH2Cl. In peptidase family S9 (prolyl oligopeptidase family). Group: Enzymes. Synonyms: protease II; Escherichia coli alkaline proteinase II; protease II. Enzyme Commission Number: EC 3.4.21.83. CAS No. 57657-67-7. 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-4175; oligopeptidase B; EC 3.4.21.83; 57657-67-7; protease II; Escherichia coli alkaline proteinase II; protease II. Cat No: EXWM-4175. | |
| oryzin | A peptidase of family S8 (subtilisin family), not containing cysteine, that is the predominant extracellular alkaline endopeptidase of the mold Aspergillus oryzae.Identical or closely related enzymes are produced by A. flavus and A. sojae. Group: Enzymes. Synonyms: Aspergillus alkaline proteinase; aspergillopeptidase B; API 21; aspergillopepsin B; aspergillopepsin F; Aspergillus candidus alkaline proteinase; Aspergillus flavus alkaline proteinase; Aspergillus melleus semi-alkaline proteinase;. Enzyme Commission Number: EC 3.4.21.63. CAS No. 9074-7-1. 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-4154; oryzin; EC 3.4.21.63; 9074-07-1; Aspergillus alkaline proteinase; aspergillopeptidase B; API 21; aspergillopepsin B; aspergillopepsin F; Aspergillus candidus alkaline proteinase; Aspergillus flavus alkaline proteinase; Aspergillus melleus semi-alkaline proteinase; Aspergillus oryzae alkaline proteinase; Aspergillus parasiticus alkaline proteinase; Aspergillus serine proteinase; Aspergillus sydowi alkaline proteinase; Aspergillus soya alkaline proteinase; Aspergillus melleus alkaline proteinase; Aspergillus sulphureus alkaline proteinase; prozyme; P 5380; kyorinase; seaprose S; semi-alkaline protease; sumizyme MP; prozyme 10; onoprose; onoprose SA; protease P; promelase. Cat No: EXWM-4154. | |
| Protease for flavors | Protease used in a neutral to alkaline environment. Used to develop savory flavors and to debitter protein hydrolysates. Applications: Flavors in high-protein flours used in baking. Group: Enzymes. CAS No. 37259-58-8. Protease. Appearance: powder or liquid. Acid Protease; for beer; Acid Protease; ethanol; baijiu Enzyme; beer Enzyme; brewage Enzyme; Acid Protease for beer; BER-1512. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form). Cat No: PRO-1827. | |
| proteasome endopeptidase complex | A 20-S protein composed of 28 subunits arranged in four rings of seven. The outer rings are composed of α subunits, but the β subunits forming the inner rings are responsible for peptidase activity. In eukaryotic organisms there are up to seven different types of β subunits, three of which may carry the N-terminal threonine residues that are the nucleophiles in catalysis, and show different specificities. The molecule is barrel-shaped, and the active sites are on the inner surfaces. Terminal apertures restrict access of substrates to the active sites. There is evidence that catalytic subunits are replaced by others under some conditions so as to alter the spec...atalytic proteinase; proteasome organelle; alkaline protease; 26S protease; tricorn proteinase; tricorn protease. Enzyme Commission Number: EC 3.4.25.1. CAS No. 140879-24-9. Alkaline Protease. 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-4374; proteasome endopeptidase complex; EC 3.4.25.1; 140879-24-9; ingensin; macropain; multicatalytic endopeptidase complex; prosome; multicatalytic proteinase (complex); MCP; proteasome; large multicatalytic protease; multicatalytic proteinase; proteasome organelle; alkaline protease; 26S protease; tricorn proteinase; tricorn protease. Cat No: EXWM-4374. | |
| Proteinase K from Tritirachium album limber, Recombinant | Proteinase K is a stable and highly reactive serine protease. Evidence from crystal and molecular structure studies indicates the enzyme belongs to the subtilisin family with an active-site catalytic triad (Asp39-His69-Ser224). It is stable in a broad range of environments:pH, buffer salts, detergents (SDS), and temperature. In the presence of 0.1-0.5% SDS, proteinase K retains activity and will digest a variety of proteins and nucleases in DNA preparations without compromising the integrity of the isolated DNA. Group: Enzymes. Synonyms: Proteinase K; EC 3.4.21.64; Tritirachium alkaline proteinase; Tritirachium album serine proteinase; Tritirachium album proteinase K; endopeptidase K; 39450-01-6; protease K. CAS No. 39450-01-6. Purity: > 95%. Proteinase K. Activity: > 30U/mg. Storage: 4°C~-20°C. Form: Powder. Source: Pichia pastoris. Species: Tritirachium album limber. Proteinase K; EC 3.4.21.64; Tritirachium alkaline proteinase; Tritirachium album serine proteinase; Tritirachium album proteinase K; endopeptidase K; 39450-01-6; protease K. Cat No: NATE-1240. | |
| serralysin | A 50 kDa extracellular endopeptidase from Pseudomonas aeruginosa, Escherichia freundii, Serratia marcescens and Erwinia chrysanthemi. There is broad specificity in cleavage of the insulin B chain, with some species variations. The pH optimum for digesting various proteins is about 9 - 10. In peptidase family M10 (interstitial collagenase family). Formerly included in EC 3.4.24.4. Group: Enzymes. Synonyms: Pseudomonas aeruginosa alkaline proteinase; Escherichia freundii proteinase; Serratia marcescens extracellular proteinase; Serratia marcescens metalloproteinase; Pseudomonas aeruginosa alk. protease; Serratia marcescens metalloprotease. Enzyme Commission Number: EC 3.4.24.40. CAS No. 70851-98-8. 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-4322; serralysin; EC 3.4.24.40; 70851-98-8; Pseudomonas aeruginosa alkaline proteinase; Escherichia freundii proteinase; Serratia marcescens extracellular proteinase; Serratia marcescens metalloproteinase; Pseudomonas aeruginosa alk. protease; Serratia marcescens metalloprotease. Cat No: EXWM-4322. | |
| subtilisin | Subtilisin is a serine endopeptidase, type example of peptidase family S8. It contains no cysteine residues (although these are found in homologous enzymes). Species variants include subtilisin BPN' (also subtilisin B, subtilopeptidase B, subtilopeptidase C, Nagarse, Nagarse proteinase, subtilisin Novo, bacterial proteinase Novo) and subtilisin Carlsberg (subtilisin A, subtilopeptidase A, alcalase Novo). Similar enzymes are produced by various Bacillus subtilis strains and other Bacillus species. Group: Enzymes. Synonyms: alcalase; alcala. Enzyme Commission Number: EC 3.4.21.62. CAS No. 9014-1-1. Protease. 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-4153; subtilisin; EC 3.4.21.62; 9014-01-1; alcalase; alcalase 0.6L; alcalase 2.5L; ALK-enzyme; bacillopeptidase A; bacillopeptidase B; Bacillus subtilis alkaline proteinase bioprase; bioprase AL 15; bioprase APL 30; colistinase; (see also comments); subtilisin J; subtilisin S41; subtilisin Sendai; subtilisin GX; subtilisin E; subtilisin BL; genenase I; esperase; maxatase; alcalase; thermoase PC 10; protease XXVII; thermoase; superase; subtilisin DY; subtilopeptidase; SP 266; savinase 8.0L; savinase 4.0T; kazusase; protease VIII; opticlean; Bacillus subtilis alkaline proteinase; protin A 3L; savinase; savinase 16.0L; savinase 32.0 L EX | |
| Trypsin | [Source]: porcine pancreas (or bovine pancreas) [Molecular weight] :~23.3KDa [Structure features]: folding single-chain (alkalescence) [Nature]: As a protein enzyme, a type of serine proteases, specialized hydrolysis carboxyl terminal is peptide linkage of alkaline amino acid. Applications: (1) used to research, with polypeptide and protein to survey and evaluate sequence. (2) bio-products tools enzyme, such as activation of the recombinant human insulin original, and so on. (3) biochemical medicine bulk drug. Group: Enzymes. Synonyms: Trypsin; EGF. CAS No. 9002-7-7. Trypsin. Appearance: inquire. Trypsin; EGF. Pack: inquire. Cat No: BIO-1011. | |
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