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| Product | Description | |
|---|---|---|
| Bacterial Protease, Liquid, 100 mL | Liquid. Converts protein to amino acid. 100 mL per bottle. Commercial grade enzyme. May be stored at 5° C for up to 1 year without appreciable loss of activity. Comes with safety data sheet (SDS) and Nature's Catalyst Booklet. Product ID: 202390. -- SOLD FOR EDUCATIONAL USE ONLY -- |  |
| Concentrated neutral bacterial protease for detergent | Highly concentrated neutral bacterial protease enzyme used in laundry detergents and cleaning products to remove protein containing stains such as grass, blood, mucus, feces and foods. Applications: Protein stains. Group: Enzymes. Synonyms: Concentrated neutral bacterial protease; for detergent; concentrated neutral bacterial protease enzyme; laundry detergents; remove protein containing stains?Detergent Enzymes; bacterial protease; neutral protease; Detergents; Concentrated neutral bacterial protease for detergent; DETE-2626. CAS No. 37259-58-8. Neutral Protease. Appearance: powder or liquid. Source: Bacterial. Concentrated neutral bacterial protease; for detergent; concentrated neutral bacterial protease enzyme; laundry detergents; remove protein containing stains?Detergent Enzymes; bacterial protease; neutral protease; Detergents; Concentrated neutral bacterial protease for detergent; DETE-2626. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form). Cat No: DETE-2626. |  |
| Neutral bacterial protease for detergent | Neutral bacterial protease enzyme used in laundry detergents and cleaning products to remove protein-containing stains such as grass, blood, mucus, feces and foods. Applications: Protein stains. Group: Enzymes. Synonyms: Neutral bacterial protease; for detergent; neutral bacterial protease enzyme; laundry detergents; remove protein-containing stains; Detergent Enzymes; bacterial protease; Detergents; Neutral bacterial protease for detergent; DETE-2625. CAS No. 37259-58-8. Neutral Protease. Appearance: powder or liquid. Source: Bacterial. Neutral bacterial protease; for detergent; neutral bacterial protease enzyme; laundry detergents; remove protein-containing stains; Detergent Enzymes; bacterial protease; Detergents; Neutral bacterial protease for detergent; DETE-2625. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form). Cat No: DETE-2625. | |
| Non-bacterial protease for Medical | A non-bacterial protease enzyme specifically formulated for cleaning, removal and prevention of mold & mildew stain and related odor. Applications: Surface cleaning. Group: Enzymes. Synonyms: Non-bacterial protease; Medical enzyme; surgical instrument; cleaning detergents; prevention of mold and mildew; Detergents; Non-bacterial protease for Medical; DETE-2633. CAS No. 37259-58-8. Non-bacterial protease. Appearance: powder or liquid. Non-bacterial protease; Medical enzyme; surgical instrument; cleaning detergents; prevention of mold and mildew; Detergents; Non-bacterial protease for Medical; DETE-2633. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form). Cat No: DETE-2633. | |
| 1-(4-Fluorophenyl)-1H-pyrazolo[3,4-d]pyrimidin-4-ol | 1-(4-Fluorophenyl)-1H-pyrazolo[3,4-d]pyrimidin-4-ol is used in the synthesis of pyrrole and pyrazolopyrimidines as inhibitors of ubiquitin-specific protease 7 (USP7) in the treatment of cancers, neurodegenerative diseases, immunology disorders, inflammatory disorders, cardiovascular diseases, ischemic diseases, viral infections and diseases, and bacterial infections and diseases. Group: Biochemicals. Grades: Highly Purified. CAS No. 289651-72-5. Pack Sizes: 100mg, 500mg. Molecular Formula: C11H7FN4O, Molecular Weight: 230.2. US Biological Life Sciences. |  Worldwide |
| β-lytic metalloendopeptidase | From Achromobacter lyticus and Lysobacter enzymogenes. Digests bacterial cell walls. Type example of peptidase family M23. Group: Enzymes. Synonyms: Myxobacter β-lytic proteinase; achromopeptidase component; β-lytic metalloproteinase; β-lytic protease; Myxobacterium sorangium β-lytic proteinase; Myxobacter495 β-lytic proteinase. Enzyme Commission Number: EC 3.4.24.32. CAS No. 37288-92-9. 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-4314; β-lytic metalloendopeptidase; EC 3.4.24.32; 37288-92-9; Myxobacter β-lytic proteinase; achromopeptidase component; β-lytic metalloproteinase; β-lytic protease; Myxobacterium sorangium β-lytic proteinase; Myxobacter495 β-lytic proteinase. Cat No: EXWM-4314. | |
| 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. | |
| Insulin Degrading Enzyme (HisoTag) from Rat, Recombinant | Insulin Degrading Enzyme (IDE) is a large zinc-binding protease of the M16A metalloprotease subfamily known to cleave multiple short polypeptides that vary considerably in sequence. IDE was first identified by its ability to degrade the B chain of the hormone insulin. This activity was observed over sixty years ago, though the enzyme specifically responsible for B chain cleavage was identified more recently. This discovery revealed considerable amino acid sequence similarity between IDE and the previously characterized bacterial protease pitrilysin, suggesting a common proteolytic mechanism. Recombinant, rat insulin degrading enzyme fused to a hisotag sequence and expressed in s. frugiperda insect cells. a metalloprotease that degrades insulin and a variety of other peptides including amyloid peptides. Group: Enzymes. Synonyms: IDE; Insulin-degrading enzyme; insulysin; insulin protease. Enzyme Commission Number: EC 3.4.24.56. Purity: >90% by SDS-PAGE. IDE. Mole weight: 110 kDa. Activity: >3 U/mg protein. Storage: < -70°C. Form: Liquid. Source: S. frugiperda. Species: Rat. IDE; Insulin-degrading enzyme; insulysin; insulin protease. Cat No: NATE-0849. | |
| Native Bacillus amyloliquefaciens Protease | Bacterial protease produced by submerged fermentation of a selected strain of Bacillus amyloliquefaciens. Secretion of protease by Bacillus amyloliquefaciens can be inhibited by treatment with the fatty acid synthetase inhibitor cerulenin. Bacterial protease produced by submerged fermentation of a selected strain of bacillus amyloliquefaciens. secretion of protease by bacillus amyloliquefaciens can be inhibited by treatment with the fatty acid synthetase inhibitor cerulenin. Applications: Protease from bacillus amyloliquefaciens has been used for the unhairing of hides and skins. it has also been used in a study to investigate peptide bond formation using the carbamoylmethyl ester as the acyl donor. Group: Enzymes. Synonyms: Protease; Neutrase. CAS No. 9001-92-7. Protease. Form: liquid, > 0.8 U/g. Source: Bacillus amyloliquefaciens. Protease; Neutrase. Cat No: NATE-0632. | |
| Native Bovine Trypsin Acetylated | Trypsin (EC 3.4.21.4) is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyses proteins. Trypsin is produced in the pancreas as the inactive protease trypsinogen. Trypsin cleaves peptide chains mainly at the carboxyl side of the amino acids lysine or arginine, except when either is followed by proline. It is used for numerous biotechnological processes. The process is commonly referred to as trypsin proteolysis or trypsinisation, and proteins that have been digested/treated with trypsin are said to have been trypsinized. The trypsin molecule has two domains: one is related to the enzyme active site and the trypt...e bacterial multidrug atp-binding cassette transporter. Group: Enzymes. Synonyms: α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3.4.21.4; Trypsin; Acetyltrypsin. Enzyme Commission Number: EC 3.4.21.4. Trypsin. Activity: > 8,500 BAEE units/mg protein (biuret). Storage: -20°C. Source: Bovine pancreas. Species: Bovine. α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3.4.21.4; Trypsin; Acetyltrypsin. Cat No: NATE-0720. | |
| 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 | |
| Subtilisin | Subtilisin, or rubinase, is a bacterial serine protease. Subtilisin can be used as a detergent additive with thermal stability, pH tolerance, and calcium dependent stability [1] [2]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: EC 3.4.21.14. CAS No. 9014-1-1. Pack Sizes: 50 mg; 100 mg. Product ID: HY-P2729. |  |
| 8-Hydroxyquinoline Hemisulfate Salt Hemihydrate | 8-Hydroxyquinoline Hemisulfate Salt Hemihydrate is a 20S proteasome inhibitor. It can be used in pharmacological activity and biological study of treatment of drug-resistant bacterial and fungal infections with metal chelating compounds such as clioquinol analogs and combination with other antibiotics in relation to β lactamase. Group: Biochemicals. Grades: Highly Purified. CAS No. 207386-91-2. Pack Sizes: 100g, 250g. Molecular Formula: C9H11NO6S, Molecular Weight: 261.25. US Biological Life Sciences. | Worldwide |
| endopeptidase Clp | An enzyme from bacteria that contains subunits of two types, ClpP, with peptidase activity, and ClpA, with ATPase activity. The ClpAP complex, which displays ATP-dependent endopeptidase activity, has the composition (ClpP14ClpA6)2. ClpP is the type example of peptidase family S14. Group: Enzymes. Synonyms: endopeptidase Ti; caseinolytic protease; protease Ti; ATP-dependent Clp protease; endopeptidase Ti; caseinolytic protease; ClpP; Clp protease. Enzyme Commission Number: EC 3.4.21.92. CAS No. 110910-59-3. 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-4184; endopeptidase Clp; EC 3.4.21.92; 110910-59-3; endopeptidase Ti; caseinolytic protease; protease Ti; ATP-dependent Clp protease; endopeptidase Ti; caseinolytic protease; ClpP; Clp protease. Cat No: EXWM-4184. | |
| Ethylenediamine-N,N'-diacetic acid | Ethylenediaminediacetic acid is an ethylenediamine derivative in which two of the four amine protons of ethylenediamine are replaced by carboxymethyl groups. It has a role as a chelator and a bacterial xenobiotic metabolite. It is an ethylenediamine derivative, a glycine derivative, a polyamino carboxylic acid and an amino dicarboxylic acid. It is a conjugate acid of an ethylenediaminediacetate(1-). Uses: Ethylenediamine-n,n'-diacetic acid (edda) is a chelating agent that can be used to synthesize: binary and ternary copper(II) complexes with potent proteasome inhibitory properties. pd(edda) complexes which can coordinate with amino acids, peptides, or dna units. Group: Heterocyclic organic compound. Alternative Names: N,N'-Ethylenediglycine. CAS No. 5657-17-0. Molecular formula: C6H12N2O4. Mole weight: 176.17. Appearance: White powder. Purity: 0.98. IUPACName: 2-[2- (Carboxymethylamino) ethylamino]acetic acid. Canonical SMILES: C(CNCC(=O)O)NCC(=O)O. Density: 1.31 g/mL. ECNumber: 227-105-6. Catalog: ACM5657170-1. |  |
| 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. | |
| IPTG Dioxane Free, Sterile Solution, 1M | Sterile solution of dioxane-free IPTG manufactured according to Maniatas, et al. Suitable for use in molecular cloning and M13 bacteriophage plating. Prepared with sterile, RNase and DNase-free molecular biology grade water and ultrapure RNase and DNase-free IPTG.IPTG is a carbohydrate used to induce b-galactosidase in the selection of recombinant plasmids. Used to select for lac Y mutants and to induce the lac operon in E.coli. IPTG will induce the cellular content of lactose permease. Water:Distilled, deionized waterFiltration: Sterile filtered (0.2um)IPTG Component: ≥99%Dioxane: ≤ 0.001%RNase, DNase, Proteases: None Detected. Group: Biochemicals. Alternative Names: IPTG; Isopropyl-ß-D-thiogalactopyranoside; Isopropyl-ß-D-thiogalactoside. Grades: Molecular Biology Grade. CAS No. 367-93-1. Pack Sizes: 10ml, 5x10ml, 100ml. Molecular Formula: C9H18O5S, Molecular Weight: 238.31. US Biological Life Sciences. | Worldwide |
| Kendomycin | Kendomycin is an endothelin receptor antagonist and proteasome inhibitor. It induces apoptosis in lymphoma. It is a potent antibacterial agent against gram-positive and gram-negative bacteria, including MRSA strains. Synonyms: TAN 2162. Grades: >95% by HPLC. CAS No. 183202-73-5. Molecular formula: C29H42O6. Mole weight: 486.64. |  |
| Kunitz-type serine protease inhibitor 1 | Kunitz-type serine protease inhibitor 1 is a Kunitz protease inhibitor isolated from Xanthosoma sagittifolium. It has activity against gram-negative bacteria. Synonyms: Pro-Val-Val-Asp-Thr-Thr-Gly-Asn-Asn-Pro-Leu-Gln-Gln-Gln-Glu-Glu-Tyr-Tyr-Val. Grades: 96.4%. Molecular formula: C96H144N24O35. Mole weight: 2194.34. | |
| Lambda Protein Phosphatase, Recombinant | λ Protein Phosphatase (λ-PPase) is a Mn+2-dependent protein phosphatase with activity towards phosphorylated serine, threonine, tyrosine and histidine residues. It is the 221 amino-acid product of ORF221 open reading frame on bacteriophage lambda (1, 2). λ-PPase was expressed as a recombinant protein in E.coli and highly purified (2). This product is an intact enzyme of high quality without tag. Applications: Λ-ppase can be used to release phosphate groups from phosphorylated serine, threonine, tyrosine and histidine residues in proteins (2). it should be noted that different proteins are dephosphorylated at different rates. optimal reaction temperature is 30°c. inclusion of protease inhibitor cocktail and shortest incubation time is desired when assays are done with crude samples. Group: Enzymes. Synonyms: Protein phosphatase 1F; PPM1F; CAMKP; CaMKPase; FEM-2; POPX2; hFEM-2; Lambda Protein. Purity: >98% by SDS-PAGE. λ-PPase. Activity: 400,000 U/mg (400 U/ul). Storage: Store at -80°C. Avoid repeating freeze-thaw cycles. Form: 400 U/ul λ-PPase in 50mM HEPES (pH 7.5), 100mM NaCl, 2mM dithiothreitol, 0.1 mM MnCl2, 0.1mM EDTA, 50% glycerol, 0.01% Brij 35. Source: E. coli. Protein phosphatase 1F; PPM1F; CAMKP; CaMKPase; FEM-2; POPX2; hFEM-2; Lambda Protein Phosphatase; λ-PPase. Cat No: NATE-0990. | |
| Native Aspergillus melleus Proteinase | A protease (also called peptidase or proteinase) is any enzyme that performs proteolysis, that is, begins protein catabolism by hydrolysis of the peptide bonds that link amino acids together in a polypeptide chain. Proteases have evolved multiple times, and different classes of protease can perform the same reaction by completely different catalytic mechanisms. Proteases can be found in animals, plants, bacteria, archaea and viruses. Applications: Proteinase is an enzyme used to break down proteins by hydrolyzing peptide bonds. proteinase is used to degrade proteins, to study proteinase inhibitors and to study thermal inactivation kinetics. proteinase is used in nucleic acid isolation procedures in incubations. it is used to study proteinase-activated receptors, such as the transducers of proteinase-mediated signaling in inflammation and the immune response. it is from aspergillus melleus and has been used to non-specifically degraded xylanase from streptomyces halstedii. Group: Enzymes. Synonyms: Protease; peptidase; proteinase; 9001-92-7. CAS No. 9001-92-7. Proteinase. Activity: > 3 units/mg solid. Storage: 2-8°C. Source: Aspergillus melleus. Protease; peptidase; proteinase; 9001-92-7. Cat No: NATE-0638. | |
| Native Bacillus polymyxa Dispase | Dispase is a protease which cleaves fibronectin, collagen IV, and to a lesser extent collagen I. It is found in some bacteria and can be isolated from culture filtrates of Bacillus polymyxa. It can be extracted, purified, and used in research. It can be particularly useful to separate embryonic epithelia and mesenchyme. Dispase II is specific for the cleavage of Leucine-Phenylalanine bonds. Dispase is often used to digest adhering primary cells in culture, since this treatment turned out to be milder than trypsin digestion. Applications: Dispase is a protease which cleaves fibronectin, collagen iv, and to a lesser extent collagen i. it is found in some bacteria and can be iso...d used in research. it can be particularly useful to separate embryonic epithelia and mesenchyme. dispase ii is specific for the cleavage of leucine-phenylalanine bonds. dispase is often used to digest adhering primary cells in culture, since this treatment turned out to be milder than trypsin digestion (sinclair et al., 2013). a recent article also finds that dispase can digest serine-phenylalanine. Group: Enzymes. Synonyms: Dispase; 42613-33-2; Proteinase; Bacillus polymyxa neutral. CAS No. 42613-33-2. Dispase. Activity: ~0.4 unit/mg solid. Storage: 2-8°C. Form: powder. Source: Bacillus polymyxa. Dispase; 42613-33-2; Proteinase; Bacillus polymyxa neutral. Cat No: NATE-0193. | |
| Native 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 Bovine Protease | A protease (also called peptidase or proteinase) is any enzyme that performs proteolysis, that is, begins protein catabolism by hydrolysis of the peptide bonds that link amino acids together in a polypeptide chain. Proteases have evolved multiple times, and different classes of protease can perform the same reaction by completely different catalytic mechanisms. Proteases can be found in animals, plants, bacteria, archaea and viruses. Derived from new zealand-sourced pancreas. Applications: Protease is an enzyme used to break down proteins by hydrolyzing peptide bonds. protease is used to degrade proteins, to study protease inhibitors and to study thermal inactivation kinetics. this product is from bovine pancreas. protease from bovine pancrease (type i) has been used for the extraction of hemicellulose. Group: Enzymes. Synonyms: Protease; peptidase; proteinase; 9001-92-7. CAS No. 9001-92-7. Protease. Activity: > 5 units/mg solid. Storage: -20°C. Source: bovine pancreas. Species: Bovine. Protease; peptidase; proteinase; 9001-92-7. Cat No: NATE-0628. | |
| 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 Peptidase | A protease (also called peptidase or proteinase) is any enzyme that performs proteolysis, that is, begins protein catabolism by hydrolysis of the peptide bonds that link amino acids together in a polypeptide chain. Proteases have evolved multiple times, and different classes of protease can perform the same reaction by completely different catalytic mechanisms. Proteases can be found in animals, plants, bacteria, archaea and viruses. Applications: A protease (also called peptidase or proteinase) is any enzyme that performs proteolysis, that is, begins protein catabolism by hydrolysis of the peptide bonds that link amino acids together in a polypeptide chain. proteases have evolved multiple times, and different classes of protease can perform the same reaction by completely different catalytic mechanisms. proteases can be found in animals, plants, bacteria, archaea and viruses. Group: Enzymes. Synonyms: protease; peptidase; proteinase; 9031-96-3. CAS No. 9031-96-3. Peptidase. Activity: ≥ 500 U/g. Storage: -20°C. Source: Porcine intestinal mucosa. Species: Porcine. protease; peptidase; proteinase; 9031-96-3. Cat No: NATE-0548. | |
| Native Rhizopus sp. Protease | A protease (also called peptidase or proteinase) is any enzyme that performs proteolysis, that is, begins protein catabolism by hydrolysis of the peptide bonds that link amino acids together in a polypeptide chain. Proteases have evolved multiple times, and different classes of protease can perform the same reaction by completely different catalytic mechanisms. Proteases can be found in animals, plants, bacteria, archaea and viruses. Acidic protease exhibits both proteolytic and lipolytic activities. stable in the acid range of ph 3-5. ph optimum is 3.0. Applications: Protease from rhizopus spp. has been used in a study to assess the amino acid sequences near the amino termini using automated edman degradation. it has also been used in a study to investigate inactivation of the enzyme by reaction with diazoacetyl-dl-norleucine methyl ester in the presence of cupric acetate. Group: Enzymes. Synonyms: Protease; peptidase; proteinase; 9001-92-7. CAS No. 9001-92-7. Protease. Activity: > 0.2 unit/mg solid. Storage: 2-8°C. Form: Supplied as a powder containing dextrin as a stabilizer. Source: Rhizopus sp. Protease; peptidase; proteinase; 9001-92-7. Cat No: NATE-0629. | |
| Native Serratia sp. Serrapeptase | Serrapeptase is a protein decomposition enzymes produced by bacteria serratia. Can decompose slow bradykinin, fibrin and fibrinogen. Applications: 1. as pharmaceutical raw materials manufacturing injection, oral agents, executive standard: ybh clinic? used for anti-inflammation, eliminate swelling. promote the dissolution of sputum, thick liquid to drain. promote the migration of antibiotics to lesion. 2. plant and animal protein hydrolysate powder (hap, hvp) production applications the flora and fauna of macromolecular protein hydrolysis into small molecular peptides or amino acids, to facilitate the effective absorption and utilization of protein. 3. the application of baki...y used in beer production, proteins can be ruled out "cold cloudy" phenomenon 7. application of textile industry processing of wool, and improve quality 8. application of leather industry made from the hair removal agent. 9. application of feed industry to improve protein utilization and lower costs. Group: Enzymes. Synonyms: Serratiopeptidase; Serratia E-15 protease; serralysin; serrapeptase; serratiapeptase; serratia peptidase; serratio peptidase; serrapeptidase. CAS No. 70851-98-8. Serrapeptase. Source: Serratia sp. Serratiopeptidase; Serratia E-15 protease; serralysin; serrapeptase; serratiapeptase; serratia peptidase; serratio peptidase; serrapeptidase. Cat No: PHAM-381. | |
| prokaryotic ubiquitin-like protein ligase | The enzyme has been characterized from the bacteria Mycobacterium tuberculosis and Corynebacterium glutamicum. It catalyses the ligation of the prokaryotic ubiquitin-like protein (Pup) to a target protein by forming a bond between an ε-amino group of a lysine residue of the target protein and the γ-carboxylate of the C-terminal glutamate of the ubiquitin-like protein (Pup). The attachment of Pup, also known as Pupylation, marks proteins for proteasomal degradation. Group: Enzymes. Synonyms: PafA (ambiguous); Pup ligase; proteasome accessory factor A. Enzyme Commission Number: EC 6.3.1.19. 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-5721; prokaryotic ubiquitin-like protein ligase; EC 6.3.1.19; PafA (ambiguous); Pup ligase; proteasome accessory factor A. Cat No: EXWM-5721. | |
| Protease-polyethylene glycol | A protease (also called peptidase or proteinase) is any enzyme that performs proteolysis, that is, begins protein catabolism by hydrolysis of the peptide bonds that link amino acids together in a polypeptide chain. Proteases have evolved multiple times, and different classes of protease can perform the same reaction by completely different catalytic mechanisms. Proteases can be found in animals, plants, bacteria, archaea and viruses. Group: Enzymes. Synonyms: PEG-Subtilisin Carlsberg; Protease-polyethylene glycol; Protease-PEG. Protease. Activity: ~600 BAEE units/mg protein. Storage: -20°C. Form: lyophilized powder. PEG-Subtilisin Carlsberg; Protease-polyethylene glycol; Protease-PEG. Pack: Package size based on protein content. Cat No: NATE-0635. | |
| rhomboid protease | These endopeptidases are multi-spanning membrane proteins. Their catalytic site is embedded within the membrane and they cleave type-1 transmembrane domains. A catalytic dyad is involved in proteolysis rather than a catalytic triad, as was thought previously. They are important for embryo development in Drosophila melanogaster. Rhomboid is a key regulator of EGF receptor signalling and is responsible for cleaving Spitz, the main ligand of the Drosophila EGF receptor pathway. Belongs in peptidase family S54. Parasite-encoded rhomboid enzymes are also important for invasion of host cells by Toxoplasma and the malaria parasite. Rhomboids are widely conserved from bacteria to archaea to humans. Group: Enzymes. Enzyme Commission Number: EC 3.4.21.105. CAS No. 713145-02-9. 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-4100; rhomboid protease; EC 3.4.21.105; 713145-02-9. Cat No: EXWM-4100. | |
| streptopain | From the bacterium, group A Streptococcus. Formed from the proenzyme by limited proteolysis. Type example of peptidase family C10. Group: Enzymes. Synonyms: Streptococcus peptidase A; streptococcal cysteine proteinase; Streptococcus protease. Enzyme Commission Number: EC 3.4.22.10. CAS No. 9025-51-8. 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-4193; streptopain; EC 3.4.22.10; 9025-51-8; Streptococcus peptidase A; streptococcal cysteine proteinase; Streptococcus protease. Cat No: EXWM-4193. | |
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