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| Product | Description | |
|---|---|---|
| Protease enzyme for fermentation | A protease enzyme used in food processing applications to break down and increase the solubility, dispersability, palatability and digestibility of proteins. Applications: Fermentation enhancement. Group: Enzymes. Synonyms: Protease enzyme; for fermentation; protease; Fuel Alcohol; Alcohol and Starch Enzymes; Fermentation enhancement; enhancement; Starch Enzymes. CAS No. 37259-58-8. Protease. Appearance: inquire. 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: ASE-3112. |  |
| Natural protease-enzyme blend for hair care | An all-natural protease-enzyme blend that enhances natural hair color and restores shine by removing excess protein-build up. Applications: Hair conditioners. Group: Enzymes. Synonyms: Natural protease; Natural protease enzyme blend; hair care; hair conditioners; protease enzyme blend; enhances natural hair color; enzyme for hair; natural hair color; Natural protease-enzyme blend for hair care. Cosmetic enzymes. Appearance: powder or liquid. Lipase; Cosmetic; lipase-based enzyme blend; breaks down human sebum; breaks down residual oil; human sebum; breaks down human sebum and residual oil; residual oil; human sebum; Lipase-based enzyme blend for cosmetic. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form). Cat No: BODY-2816. | |
| Protease-based enzyme formulation for toothpaste | A protease-based enzyme formulation used in toothpaste and mouthwash to whiten teeth, remove plaque and odor-causing deposits on teeth and gum tissue. Applications: Teeth. Group: Enzymes. Synonyms: Protease; Protease-based enzyme formulation; for toothpaste; enzyme for whiten teeth; protease-based enzyme; whiten teeth; remove plaque and odor; whiten teeth; teeth; Protease-based enzyme formulation for toothpaste. Cosmetic enzymes. Appearance: powder or liquid. Lipase; Cosmetic; lipase-based enzyme blend; breaks down human sebum; breaks down residual oil; human sebum; breaks down human sebum and residual oil; residual oil; human sebum; Lipase-based enzyme blend for cosmetic. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form). Cat No: BODY-2818. | |
| Proteases enzyme blend for creams | A special blend of proteases used in day/night moisturizing creams and lotions along with conditioning agents to gently exfoliate the skin and increase absorption of water so emollients can smooth and soften skin rendering lines and blemishes less visible. Applications: Cosmetic. Group: Enzymes. Synonyms: Proteases; Proteases enzyme; for creams; Cosmetic; blend of proteases; moisturizing; moisturizing creams and lotions; increase absorption of water; absorption of water; Proteases enzyme blend for creams. Cosmetic enzymes. Appearance: powder or liquid. Lipase; Cosmetic; lipase-based enzyme blend; breaks down human sebum; breaks down residual oil; human sebum; breaks down human sebum and residual oil; residual oil; human sebum; Lipase-based enzyme blend for cosmetic. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form). Cat No: BODY-2813. | |
| Proteases enzyme blend for skin cleansers | A special blend of proteases used in day/night moisturizers, skin cleansers and bath soaks. Used with conditioning agents, it gently exfoliates skin and increases absorption of water so emollients can smooth and soften skin rendering lines and blemishes less visible. Applications: Skin cleansers. Group: Enzymes. Synonyms: Proteases ;Proteases enzyme; for skin cleansers; skin; cleansers enzyme; proteases; moisturizing creams and lotions; increase absorption of water; Proteases enzyme blend for skin cleansers. Cosmetic enzymes. Appearance: powder or liquid. Lipase; Cosmetic; lipase-based enzyme blend; breaks down human sebum; breaks down residual oil; human sebum; breaks down human sebum and residual oil; residual oil; human sebum; Lipase-based enzyme blend for cosmetic. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form). Cat No: BODY-2814. | |
| 1-Methyl-1H-benzotriazole | A benzotriazole derivative with potential inhibitory effect on protease enzymes chymotrypsin, trypsin and papain. Group: Biochemicals. Grades: Highly Purified. CAS No. 13351-73-0. Pack Sizes: 1g, 2.5g. Molecular Formula: C7H7N3. US Biological Life Sciences. |  Worldwide |
| 1-Methyl-1H-benzotriazole-d3 | 1-Methyl-1H-benzotriazole-d3 is the labeled derivative of 1-Methyl-1H-benzotriazole (M289810), which is the benzotriazole derivative with potential inhibitory effect on protease enzymes chymotrypsin, trypsin and papain. Group: Biochemicals. Grades: Highly Purified. Pack Sizes: 1g, 10g. Molecular Formula: C7H4D3N3, Molecular Weight: 136.169999999999. US Biological Life Sciences. | Worldwide |
| 3,4-Dichloroisocoumarin | 3,4-Dichloroisocoumarin is a potent serine-protease and SrLip inhibitor (K i for SrLip: 26.6 μM). 3,4-Dichloroisocoumarin is opened by serine proteases and then undergoes acylation with the enzyme, thereby inhibiting protease activity. 3,4-Dichloroisocoumarin can induce DNA fragmentation and Apoptosis. 3,4-Dichloroisocoumarin can be used in the research of multiple fields such as tumors, cardiovascular disease and enzyme catalytic mechanisms [1] [2] [3] [4] [5]. Uses: Scientific research. Group: Natural products. CAS No. 51050-59-0. Pack Sizes: 5 mg; 10 mg. Product ID: HY-126034. |  |
| 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 |
| Acid Protease for beer | Acid protease abstracts from fermentation of Aspergillus niger. Under low PH value, it can effectively hydrolyze protein. Acid protease be widely used in ethanol, wine, beer, brewage, food processing, feedstuff and etc. Applications: Ethanol, wine, beer, brewage, food processing, feedstuff and etc. Group: Enzymes. Synonyms: Acid Protease; for beer; Acid Protease; ethanol; baijiu Enzyme; beer Enzyme; brewage Enzyme; Acid Protease for beer; BER-1512. Protease. Appearance: powder or liquid. Source: Aspergillus niger. 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: BER-1512. | |
| Acid Stable Protease | An enzyme capable of acidic protein hydrolysis. Typically used in dietary supplements and many other applications requiring hydrolysis in highly acidic conditions. Applications: Dietary supplements. Group: Enzymes. Synonyms: Stable; Acid Stable Protease; Protease; Acid Stable Protease. Protease. Appearance: powder or liquid. Source: Aspergillus niger. 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: DIS-1011. | |
| acrosin | Occurs in spermatozoa; formed from proacrosin by limited proteolysis. Inhibited by naturally occurring trypsin inhibitors. In peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: acrosomal proteinase; acrozonase; α-acrosin; β-acrosin; upsilon-acrosin; acrosomal protease; acrosin amidase. Enzyme Commission Number: EC 3.4.21.10. CAS No. 9068-57-9. 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-4094; acrosin; EC 3.4.21.10; 9068-57-9; acrosomal proteinase; acrozonase; α-acrosin; β-acrosin; upsilon-acrosin; acrosomal protease; acrosin amidase. Cat No: EXWM-4094. | |
| actinidain | From the kiwi fruit or Chinese gooseberry (Actinidia chinensis). In peptidase family C1 (papain family). Group: Enzymes. Synonyms: actinidin; Actinidia anionic protease; proteinase A2 of Actinidia chinensis. Enzyme Commission Number: EC 3.4.22.14. CAS No. 39279-27-1. 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-4194; actinidain; EC 3.4.22.14; 39279-27-1; actinidin; Actinidia anionic protease; proteinase A2 of Actinidia chinensis. Cat No: EXWM-4194. | |
| ADAMTS13 endopeptidase | In peptidase family M12. Group: Enzymes. Synonyms: ADAMTS VWF cleaving metalloprotease; ADAMTS-13; ADAMTS13;vWF-cleaving protease; VWF-CP; vWF-degrading protease; Upshaw factor; von Willebrand factor cleaving protease; ADAMTS13 peptidase. Enzyme Commission Number: EC 3.4.24.87. 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-4371; ADAMTS13 endopeptidase; EC 3.4.24.87; ADAMTS VWF cleaving metalloprotease; ADAMTS-13; ADAMTS13;vWF-cleaving protease; VWF-CP; vWF-degrading protease; Upshaw factor; von Willebrand factor cleaving protease; ADAMTS13 peptidase. Cat No: EXWM-4371. | |
| 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. | |
| α-lytic endopeptidase | From the myxobacterium Lysobacter enzymogenes. In peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: myxobacter α-lytic proteinase; α-lytic proteinase; α-lytic protease; Mycobacterium sorangium α-lytic proteinase; Myxobacter 495 α-lytic proteinase; α-lytic proteinase; Myxobacter α-lytic proteinase; Mycobacterium sorangium α-lytic proteinase. Enzyme Commission Number: EC 3.4.21.12. CAS No. 37288-76-9. 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-4115; α-lytic endopeptidase; EC 3.4.21.12; 37288-76-9; myxobacter α-lytic proteinase; α-lytic proteinase; α-lytic protease; Mycobacterium sorangium α-lytic proteinase; Myxobacter 495 α-lytic proteinase; α-lytic proteinase; Myxobacter α-lytic proteinase; Mycobacterium sorangium α-lytic proteinase. Cat No: EXWM-4115. | |
| α-Lytic Protease M190A Mutant, Recombinant | Alpha-lytic protease (aLP) is an alternative specificity protease for proteomics applications, whose wild-type (WT) version cleaves after T, A, S, and V residues. The M190A (Met190 ? Ala190) mutant of aLP has different cleavage specificities, and cleaves after M, F, and L residues. Both the WT and M190A forms of aLP geneRate peptides of similar average length as trypsin. Group: Enzymes. Synonyms: ALP M190A; Alpha-Lytic Protease M190A Mutant. ALP M190A. Activity: > 0.05 U/mg. Storage: -70°C. ALP M190A; Alpha-Lytic Protease M190A Mutant. Cat No: NATE-0051. | |
| Aminopeptidase N Inhibitor | Membrane alanyl aminopeptidase is also known as alanyl aminopeptidase (AAP) or aminopeptidase N (AP-N), which is an enzyme that in humans is encoded by the ANPEP gene. Aminopeptidase N (AP-N) inhibitor is a reversible inhibitor of AP-N/CD13 (IC50 = 25 μM). It is selective for AP-N/CD13 over matrix metalloproteinase-9 (MMP-9), angiotensin converting enzyme (ACE), neutral endopeptidase (NEP), γ-glutamyl transpeptidase, and the serine proteases dipeptidyl peptidase 4 (DPP-4) and cathepsin G at a concentration of 1 mM. AP-N inhibitor is non-cytotoxic to U937 cells at a concentration of 100 μM. Human aminopeptidase N is a receptor for one strain of human coronavirus that is an important cause of upper respiratory tract infections. Defects in this gene appear to be a cause of various types of leukemia or lymphoma. Synonyms: AP-N Inhibitor. Grades: ≥95%. CAS No. 596108-59-7. Molecular formula: C17H10N2O8. Mole weight: 370.27. |  |
| Aprotinin, Bovine (Pancreatic trypsin inhibitor) | Aprotinin is a competitive serine protease inhibitor that inhibits trypsin, chymotrypsin, kallikrein and plasmin. Aprotinin forms stable complexes with and blocks the active sites of enzymes. Binding is reversible with most aprotinin-protease complexes, dissociating at pH >10 or <3. Effective concentration is equimolar with protease. Group: Biochemicals. Alternative Names: Antikrein; Antilysin; Antilysine; Aprostat; Aprotinin; BPTI; BPTI Trypsin Inhibitor; Basic Pancreatic Trypsin Inhibitor; Bayer A 128; Bovine Basic Pancreatic Trypsin Inhibitor; Bovine Pancreatic Trypsin Inhibitor; Bovine Trypsin Inhibitor; Fosten; Kallikrein-trypsin Inactivator; Kiker 52G; Kir Richter; Kunitz Pancreatic Trypsin Inhibitor; Kunitz Protease Inhibitor; Kunitz Trypsin Inhibitor; Kunitz-type Inhibitor; Kunitz-type Proteinase Inhibitor; Kunitz-type Trypsin Inhibitor; Onquinin; Pancreatic Basic Trypsin Inhibitor; Pancreatic Trypsin Inhibitor; Pancreatic Trypsin Inhibitor (Kunitz); Protease Inhibitor, Kunitz Type; RP 9921; Repulson; Trasuylol; Trasylol; Trazinin; Triazinin; Trypsin Inhibitor, Trasylol; Trypsin-kallikrein Inhibitor (Kunitz); Zymofren. Grades: Highly Purified. CAS No. 9087-70-1. Pack Sizes: 100mg, 250mg, 500mg, 1g. Molecular Formula: C???H???N??O??S?, Molecular Weight: 6511.45. US Biological Life Sciences. | Worldwide |
| Arginine Specific Protease from Porphyromonas gingivalis | Arginine Specific Protease specifically digests peptides and proteins C-terminal to arginine residues. The protease is specific for Arg-X motifs and does not have activity at lysines as commonly observed using Arg-C. The enzymatic activity of Arginine Specific Protease includes digestion of Arg-Pro linkages, which is difficult to digest with other enzymes. The enzyme is active at pH ranging from pH 5.0-9.0 and in presence of denaturing agents such as 6M urea and 0.1% SDS. Applications: Peptide mappingprotein sequence analysisprotein fingerprintingpost-translational modification analysis. Group: Enzymes. Synonyms: Arginine Specific Protease; GingisREX. Purity: > 95% homogeneity as determined by SDS-PAGE and HPLC. Arginine Specific Protease. Stability: 1 year when stored at -20°C. After reconstitution by addition of water it is stable for at least 1 month at 4-8°C. Appearance: White to light yellow powder. Storage: The product is shipped on ice and should be stored at -20°C upon arrival. Form: Lyophilized powder in 20 mM Bis-Tris, 150 mM NaCl, 5 mM CaCl2, Ph 6.8 without preservatives. Source: Porphyromonas gingivalis. Arginine Specific Protease; GingisREX; Rgp protease; Rgp; protease. Cat No: NATE-1602. | |
| aspergillopepsin I | Found in a variety of Aspergillus species (imperfect fungi): Aspergillus awamori (awamorin, aspergillopepsin A:), A. foetidus (aspergillopepsin F:), A. fumigatus, A. kawachii, A. niger (proteinase B, proctase B:), A. oryzae (trypsinogen kinase:), A. saitoi (aspergillopeptidase A:), and A. sojae. In peptidase family A1 (pepsin A family). Formerly included in EC 3.4.23.6. Group: Enzymes. Synonyms: Aspergillus acid protease; Aspergillus acid proteinase; Aspergillus aspartic proteinase; Aspergillus awamori acid proteinase; Aspergillus carboxyl proteinase; (see also Comments); carboxyl proteinase; Aspergillus kawachii aspartic proteinase; Aspergillus saitoi acid proteinase; pepsin-type aspartic proteinase. Enzyme Commission Number: EC 3.4.23.18. CAS No. 9025-49-4. 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-4255; aspergillopepsin I; EC 3.4.23.18; 9025-49-4; Aspergillus acid protease; Aspergillus acid proteinase; Aspergillus aspartic proteinase; Aspergillus awamori acid proteinase; Aspergillus carboxyl proteinase; (see also Comments); carboxyl proteinase; Aspergillus kawachii aspartic proteinase; Aspergillus saitoi acid proteinase; pepsin-type aspartic proteinase; Aspergillus niger acid proteinase; sumizyme AP; proctase P; denapsin; denapsin XP 271; proctase. Cat No: EXWM-4255. | |
| Atazanavir | Atazanavir is a novel and potent azapeptide protease inhibitor that specifically inhibits the human immunodeficiency virus type 1 (HIV-1) protease enzyme with inhibition constant Ki of 66 nmol/L and also inhibits the viral replication of HIV-1 with 50% effective concentration EC50 ranging from 2.6 to 5.3 nmol/L. Atazanavir binds to HIV-1 protease preventing the cleavage of gag and gag-pol polyproteins, which results in the formation of immature virions in HIV-1-infected cells. Atazanavir has a different C-2 symmetric chemical structure and a generally greater antiretroviral potency in various HIV strains compared to other protease inhibitors, including indinavir, nelfinavir, ritonavir, saquinavir and amprenavir. Synonyms: Atazanavir ; Reyataz ; Atazanavir sulfate ; CGP75136 ; CGP75176 ; CGP75355 ; BMS232632 ; CGP 73547 ; CGP 75136 ; CGP 75176 ; CGP 75355 ; CGP-73547 ; CGP-75136 ; CGP-75176 ; CGP-75355 ; BMS 232632 ; BMS-232632 ; BMS-232632-05 ; C413408. Grades: 0.98. CAS No. 198904-31-3. Molecular formula: C38H52N6O7. Mole weight: 704.869. | |
| aureolysin | A metalloenzyme from S. aureus earlier confused with staphylokinase (a non-enzymic activator of plasminogen). Group: Enzymes. Synonyms: Staphylococcus aureus neutral proteinase; Staphylococcus aureus neutral protease. Enzyme Commission Number: EC 3.4.24.29. CAS No. 39335-13-2. 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-4310; aureolysin; EC 3.4.24.29; 39335-13-2; Staphylococcus aureus neutral proteinase; Staphylococcus aureus neutral protease. Cat No: EXWM-4310. | |
| bacillolysin | Variants of this enzyme have been found in species of Bacillus including B. subtilis, B. amyloliquefaciens, B. megaterium (megateriopeptidase,), B. mesentericus, B. cereus and B. stearothermophilus. In peptidase family M4 (thermolysin family). Formerly included in EC 3.4.24.4. Group: Enzymes. Synonyms: Bacillus metalloendopeptidase; Bacillus subtilis neutral proteinase; anilozyme P 10; Bacillus metalloproteinase; Bacillus neutral proteinase; megateriopeptidase. Enzyme Commission Number: EC 3.4.24.28. CAS No. 9080-56-2. Neutral 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-4309; bacillolysin; EC 3.4.24.28; 9080-56-2; Bacillus metalloendopeptidase; Bacillus subtilis neutral proteinase; anilozyme P 10; Bacillus metalloproteinase; Bacillus neutral proteinase; megateriopeptidase. Cat No: EXWM-4309. | |
| 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. | |
| Bexarotene (4-(1-(3,5,5,8,8-Pentamethyl-5,6,7,8-tetrahydronaphthalen-2-yl)vinyl)benzoic Acid) | A retinoid X receptor (RXR) agonist that can permeate the blood-brain barrier and rapidly reduce AB40 and AB42 levels in APP/PS1 mice in an ApoE-dependent manner (25% reduction in 6h and 50% reduction in 72h). Causes a rapid reversal of cognitive, social, and olfactory deficts. Shown to progressively enhance the expression of ApoE and ATP-binding cassette transporters ABCA1 and ABCG1. Also stimulates the secretion of highly lapidated HDL particles in primary microglia and astrocytes. Does not affect the levels of AB proteases, insulin degrading enzyme, and neprilysin. Group: Biochemicals. Grades: Highly Purified. CAS No. 153559-49-0. Pack Sizes: 50mg. US Biological Life Sciences. | Worldwide |
| Boceprevir | Boceprevir (EBP 520) is a potent, highly selective, orally bioavailable HCV NS3 protease inhibitor with a K i of 14 nM in both enzyme assay and an EC 90 of 350 nM in cell-based replicon assay [1] [2] [3] [4] [5]. Boceprevir inhibits SARS-CoV-2 3CL pro activity [6]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: EBP 520; SCH 503034. CAS No. 394730-60-0. Pack Sizes: 10 mM * 1 mL; 5 mg; 10 mg; 50 mg; 100 mg; 200 mg. Product ID: HY-10237. | |
| bothrolysin | A 22.5 kDa endopeptidase from the venom of the jararaca snake (Bothrops jararaca), insensitive to phosphoramidon at 0.5 mM. In peptidase family M12 (astacin family). Group: Enzymes. Synonyms: Bothrops metalloendopeptidase J; J protease. Enzyme Commission Number: EC 3.4.24.50. CAS No. 443890-65-1. 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-4332; bothrolysin; EC 3.4.24.50; 443890-65-1; Bothrops metalloendopeptidase J; J protease. Cat No: EXWM-4332. | |
| brachyurin | From hepatopancreas of the fiddler crab, Uca pugilator. In peptidase family S1 (trypsin family). Other serine endopeptidases that degrade collagen, but are not listed separately here, include a second endopeptidase from Uca pugilator, digestive enzymes from other decapod crustacea, and an enzyme from the fungus Entomophthora coronata. Group: Enzymes. Synonyms: Uca pugilator collagenolytic proteinase; crab protease I; crab protease II. Enzyme Commission Number: EC 3.4.21.32. CAS No. 848900-32-3. 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-4127; brachyurin; EC 3.4.21.32; 848900-32-3; Uca pugilator collagenolytic proteinase; crab protease I; crab protease II. Cat No: EXWM-4127. | |
| Bromelain | Bromelain is a protein-digesting enzyme extracted from the stem, fruit, and juice of the pineapple plant (Ananas comosus). It belongs to a group of enzymes called proteases or proteinases. Bromelain is a complex mixture of enzymes that can hydrolyze (break down) various types of proteins, including collagen, elastin, and fibrin. Uses: 1. anti-inflammatory: bromelain has been found to possess anti-inflammatory properties, which makes it useful in the treatment of arthritis, asthma, allergies, and other conditions characterized by inflammation. 2. digestive aid: bromelain is often used as a digestive aid because it helps break down proteins in the digestive tract, aiding digestion and reducing bloating. 3. wound healing: bromelai. Group: Heterocyclic organic compound. Alternative Names: STEM BROMELAIN; 3.4.22.32; BROMELAIN; BROMELAIN PINEAPPLE;BROMELIN;EC 3.4.22.1;EC 3.4.22.32;EC 3.4.22.4. CAS No. 9001-00-7. Molecular formula: N/A. Mole weight: N/A. Appearance: yellow to beige crystalline powder. Catalog: ACM9001007. |  |
| calicivirin | Viruses that are members of the Norovirus genus (Caliciviridae family) are a major cause of epidemic acute viral gastroenteritis. The nonstructural proteins of these viruses are produced by proteolytic cleavage of a large precursor polyprotein, performed by a protease that is incorporated into the polyprotein.Cleavage sites are apparently defined by features based on both sequence and structure since several sites in the polyprotein fulfilling the identified sequence requirements are not cleaved. The presence of acidic (Asp), basic (Arg), aromatic (Tyr) or aliphatic (Leu) amino acids at the P1' position results in only minor differences in cleavage efficiency, suggesting that steric or...C-like protease; calicivirus endopeptidase; rabbit hemorrhagic disease virus 3C endopeptidase. Enzyme Commission Number: EC 3.4.22.66. 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-4242; calicivirin; EC 3.4.22.66; Camberwell virus processing peptidase; Chiba virus processing peptidase; Norwalk virus processing peptidase; Southampton virus processing peptidase; Southampton virus; norovirus virus processing peptidase; calicivirus trypsin-like cysteine protease; calicivirus TCP; calicivirus 3C-like protease; calicivirus endopeptidase; rabbit hemorrhagic disease virus 3C endopeptidase. Cat No: EXWM-4242. | |
| calpain-1 | In peptidase family C2. Requires Ca2+ at micromolar concentrations for activity. Cytosolic in animal cells. The active enzyme molecule is a heterodimer in which the large subunit contains the peptidase unit, and the small subunit is also a component of EC 3.4.22.53, calpain-2. Group: Enzymes. Synonyms: μ-calpain; calcium-activated neutral protease I. Enzyme Commission Number: EC 3.4.22.52. CAS No. 78990-62-2. Calpain 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-4227; calpain-1; EC 3.4.22.52; 78990-62-2; μ-calpain; calcium-activated neutral protease I. Cat No: EXWM-4227. | |
| calpain-2 | Type example of peptidase family C2. Requires Ca2+ at millimolar concentrations for activity. Cytosolic in animal cells. The active enzyme molecule is a heterodimer in which the large subunit contains the peptidase unit, and the small subunit is also a component of EC 3.4.22.52, calpain-1. Group: Enzymes. Synonyms: calcium-activated neutral protease II; m-calpain; milli-calpain. Enzyme Commission Number: EC 3.4.22.53. CAS No. 702693-80-9. 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-4228; calpain-2; EC 3.4.22.53; 702693-80-9; calcium-activated neutral protease II; m-calpain; milli-calpain. Cat No: EXWM-4228. | |
| calpain-3 | This Ca2+-dependent enzyme is found in skeletal muscle and is genetically linked to limb girdle muscular dystrophy type 2A. The enzyme is activated by autoproteolytic cleavage of insertion sequence 1 (IS1),which allows substrates and inhibitors gain access to the active site. Substrates include the protein itself and connectin/titin. Belongs in peptidase family C2. Group: Enzymes. Synonyms: p94; calpain p94; CAPN3; muscle calpain;calpain 3; calcium-activated neutral proteinase 3; muscle-specific calcium-activated neutral protease 3; CANP 3; calpain L3. Enzyme Commission Number: EC 3.4.22.54. 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-4229; calpain-3; EC 3.4.22.54; p94; calpain p94; CAPN3; muscle calpain;calpain 3; calcium-activated neutral proteinase 3; muscle-specific calcium-activated neutral protease 3; CANP 3; calpain L3. Cat No: EXWM-4229. | |
| Camostat Mesylate | Camostat (INN) or FOY-305 is a serine protease inhibitor. Serine protease enzymes have a variety of functions in the body, and so camostat has a diverse range of uses. It is used in the treatment of some forms of cancer and is also effective against some viral infections, as well as inhibiting fibrosis in liver or kidney disease orpancreatitis. Uses: Trypsin inhibitors. Synonyms: 4-(2-(2-(dimethylamino)-2-oxoethoxy)-2-oxoethyl)phenyl 4-guanidinobenzoate methanesulfonate; Camostat Mesilate; Camostat Mesylate; FOY 305; FOY-305; FOY305. Grades: >98%. CAS No. 59721-29-8. Molecular formula: C20H22N4O5.CH4O3S. Mole weight: 494.52. | |
| Camostat Mesylate | Orally active, non-peptide proteolitic enzyme inhibitor with anti-trypsin and anti-plasmin activities, related structurally to gabexate. Protease inhibitor. Camostat mesilate is a serine protease inhibitor that inhibits plasmin, kallikrein, thrombin as well as trypsin, which attenuates pancreatic fibrosis. It reduces weight gain and improves metabolism in obese rodent models. It is in clinical use (in Japan) for pancreatitis. Camostat has been found to inhibit influenza virus replication in human tracheal epithelial cells and is also a direct prostasin inhibitor which may be useful in reducing sodium transport in cystic fibrosis. Additionally it has been shown to reduce infection of Calu-3 lung cells by SARS-CoV-2 (the coronavirus responsible for COVID-19) via inhibition of the serine protease TMPRSS2 required for viral spike protein priming. Group: Biochemicals. Alternative Names: 4- [ [4- [ (Aminoiminomethyl) amino] benzoyl] oxy] benzeneacetic Acid 2-(Dimethylamino)-2-oxoethyl Ester Methanesulfonate; FOY 305; FOY-S 980; Foipan. Grades: Highly Purified. CAS No. 59721-29-8. Pack Sizes: 5mg, 10mg, 25mg, 50mg, 100mg. Molecular Formula: C??H??N?O?S. US Biological Life Sciences. | Worldwide |
| Carboxypeptidase-B from rat, Recombinant | Carboxypeptidase B, recombinant, is intended to use in highly regulated production processes at pharmaceutical companies. Carboxypeptidase B is a widely used metalloprotease, typically isolated from pancreas of different animals, that specifically releases arginine and lysine from the C-terminus of peptides and proteins. Roche has chemically synthesized a gene encoding for the amino acid sequence of the rat Carboxypeptidase B and has transformed the gene into the expression host Pichia pastoris, which expresses the recombinant Carboxypeptidase B as active protease with identical properties compared to the native Carboxypeptidase B. The product is manufactured according to...terial for the production of active pharmaceutical ingredients (api), i.e., insulin. Group: Enzymes. Synonyms: protaminase; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine] hydrolase. Purity: >85%. CPB1. Activity: >210 U/mg. Stability: At -15 to -25°C within specification range for 24 months. Appearance: Clear, colorless to slightly yellowish solution. Storage: Tris/HCl, 33 mmol/l; ZnCl2, 0.1 mmol/l; pH 7.5-8.5 at +25°C. Source: Pichia pastoris. Species: Rat pancreas. carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5. Cat N | |
| caspase-1 | From mammalian monocytes. This enzyme is part of the family of inflammatory caspases, which also includes caspase-4 (EC 3.4.22.57) and caspase-5 (EC 3.4.22.58) in humans and caspase-11 (EC 3.4.22.64), caspase-12, caspase-13 and caspase-14 in mice. Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation. Cleaves pro-interleukin-1β (pro-IL-1β) to form mature IL-1β, a potent mediator of inflammation. Also activates the proinflammatory cytokine, IL-18, which is also known as interferon-γ-inducing factor. Inhibited by Ac-Tyr-Val-Ala-Asp-CHO. Caspase-11 plays a critical role in the activation of caspase-1 in mi...proteinase; ICE. Enzyme Commission Number: EC 3.4.22.36. CAS No. 122191-40-6. 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-4211; caspase-1; EC 3.4.22.36; 122191-40-6; interleukin 1β-converting enzyme; protease VII; protease A; interleukin 1β precursor proteinase; interleukin 1 converting enzyme; interleukin 1β-converting endopeptidase; interleukin-1β convertase; interleukin-1β converting enzyme; interleukin-1β precursor proteinase; prointerleukin 1β protease; precursor interleukin-1β converting enzyme; pro-interleukin 1β proteinase; ICE. Cat No: EXWM-4211. | |
| caspase-10 | Caspase-10 is an initiator caspase, as are caspase-2 (EC 3.4.22.55), caspase-8 (EC 3.4.22.61) and caspase-9 (EC 3.4.22.62). Like caspase-8, caspase-10 contains two tandem death effector domains (DEDs) in its N-terminal prodomain, and these play a role in procaspase activation. The enzyme has many overlapping substrates in common with caspase-8, such as RIP (the cleavage of which impairs NF-κB survival signalling and starts the cell-death process) and PAK2 (associated with some of the morphological features of apoptosis, such as cell rounding and apoptotic body formation). Bid, a Bcl2 protein, can be cleaved by caspase-3 (EC 3.4.22.56), caspase-8 and caspase-10 at Lys-Gln-Thr-Asp? ...u-Thr-Asp? to yield a p13 fragment that is not N-myristoylated. Belongs in peptidase family C14. Group: Enzymes. Synonyms: FLICE2, Mch4; CASP-10; ICE-like apoptotic protease 4; apoptotic protease Mch-4; FAS-associated death domain protein interleukin-1β-converting enzyme 2. Enzyme Commission Number: EC 3.4.22.63. CAS No. 189088-85-5. 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-4239; caspase-10; EC 3.4.22.63; 189088-85-5; FLICE2, Mch4; CASP-10; ICE-like apoptotic protease 4; apoptotic protease Mch-4; FAS-associated death domain protein interleukin-1β-converting enzyme 2. Cat No: EXWM-4239. | |
| caspase-2 | Caspase-2 is an initiator caspase, as are caspase-8 (EC 3.4.22.61), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63). Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation. Two forms of caspase-2 with antagonistic effects exist: caspase-2L induces programmed cell death and caspase-2S suppresses cell death. Caspase-2 is activated by caspase-3 (EC 3.4.22.56), or by a caspase-3-like protease. Activation involves cleavage of the N-terminal prodomain, followed by self-proteolysis between the large and small subunits of pro-caspase-2 and further proteolysis into smaller fragments. Proteolysis occurs at Asp residues and the ...s a substrate of the large isoform of pro-caspase-2 (caspase-2L) but not of the short isoform (caspase-2S). Belongs in peptidase family C14. Group: Enzymes. Synonyms: ICH-1; NEDD-2; caspase-2L; caspase-2S; neural precursor cell expressed developmentally down-regulated protein 2; CASP-2; NEDD2 protein. Enzyme Commission Number: EC 3.4.22.55. CAS No. 182372-14-1. 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-4230; caspase-2; EC 3.4.22.55; 182372-14-1; ICH-1; NEDD-2; caspase-2L; caspase-2S; neural precursor cell expressed developmentally down-regulated protein 2; CASP-2; NEDD2 protein. Cat No: EXWM-4230. | |
| caspase-3 | Caspase-3 is an effector/executioner caspase, as are caspase-6 (EC 3.4.22.59) and caspase-7 (EC 3.4.22.60). These caspases are responsible for the proteolysis of the majority of cellular polypeptides [e.g. poly(ADP-ribose) polymerase (PARP)], which leads to the apoptotic phenotype. Procaspase-3 can be activated by caspase-1 (EC 3.4.22.36), caspase-8 (EC 3.4.22.61), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63) as well as by the serine protease granzyme B. Caspase-3 can activate procaspase-2 (EC 3.4.22.55). Activation occurs by inter-domain cleavage followed by removal of the N-terminal prodomain. Although Asp-Glu-(Val/Ile)-Asp is thought to be the preferred cleavage sequence, the enzyme can accommodate different residues at P2 and P3 of the substrate. Like caspase-2, a hydrophobic residue at P5 of caspase-3 leads to more efficient hydrolysis, e.g. (Val/Leu)-Asp-Val-Ala-Asp? is a better substrate than Asp-Val-Ala-Asp?. This is not the case for caspase-7. Belongs in peptidase family C14. Group: Enzymes. Synonyms: CPP32; apopain; yama protein. Enzyme Commission Number: EC 3.4.22.56. CAS No. 169592-56-7. 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-4231; caspase-3; EC 3.4.22.56; 169592-56-7; CPP32; apopain; yama protein. Cat No: EXWM-4231. | |
| caspase-4 | This enzyme is part of the family of inflammatory caspases, which also includes caspase-1 (EC 3.4.22.36) and caspase-5 (EC 3.4.22.58) in humans and caspase-11 (EC 3.4.22.64), caspase-12, caspase-13 and caspase-14 in mice. Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation. The enzyme is able to cleave itself and the p30 caspase-1 precursor, but, unlike caspase-1, it is very inefficient at generating mature interleukin-1β (IL-1β) from pro-IL-1&beta. Both this enzyme and caspase-5 can cleave pro-caspase-3 to release the small subunit (p12) but not the large subunit (p17). The caspase-1 inhibitor Ac-Tyr-Val-Ala-Asp-CHO can also inhibit this enzyme, but more slowly. Belongs in peptidase family C14. Group: Enzymes. Synonyms: ICErelII; ICErel-II; Ich-2; transcript X; TX; TX protease; caspase 4; CASP-4. Enzyme Commission Number: EC 3.4.22.57. CAS No. 182762-08-9. 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-4232; caspase-4; EC 3.4.22.57; 182762-08-9; ICErelII; ICErel-II; Ich-2; transcript X; TX; TX protease; caspase 4; CASP-4. Cat No: EXWM-4232. | |
| caspase-5 | This enzyme is part of the family of inflammatory caspases, which also includes caspase-1 (EC 3.4.22.36) and caspase-4 (EC 3.4.22.57) in humans and caspase-11 (EC 3.4.22.64), caspase-12, caspase-13 and caspase-14 in mice. Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation. The enzyme is able to cleave itself and the p30 caspase-1 precursor, but is very inefficient at generating mature interleukin-1β (IL-1β) from pro-IL-1&beta. Both this enzyme and caspase-4 can cleave pro-caspase-3 to release the small subunit (p12) but not the large subunit (p17). Unlike caspase-4, this enzyme can be induced by lipopolysaccharide. Belongs in peptidase family C14. Group: Enzymes. Synonyms: ICErel-III; Ich-3; ICH-3 protease; transcript Y; TY; CASP-5. Enzyme Commission Number: EC 3.4.22.58. CAS No. 192465-11-5. 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-4233; caspase-5; EC 3.4.22.58; 192465-11-5; ICErel-III; Ich-3; ICH-3 protease; transcript Y; TY; CASP-5. Cat No: EXWM-4233. | |
| caspase-6 | Caspase-6 is an effector/executioner caspase, as are caspase-3 (EC 3.4.22.56) and caspase-7 (EC 3.4.22.60). These caspases are responsible for the proteolysis of the majority of cellular polypeptides [e.g. poly(ADP-ribose) polymerase (PARP)], which leads to the apoptotic phenotype. Caspase-6 can cleave its prodomain to produce mature caspase-6, which directly activates caspase-8 (EC 3.4.22.61) and leads to the release of cytochrome c from the mitochondria. The release of cytochrome c is an essential component of the intrinsic apoptosis pathway. The enzyme can also cleave and inactivate lamins, the intermediate filament scaffold proteins of the nuclear envelope, leading to nuclear fragmentation in the final phases of apoptosis. Belongs in peptidase family C14. Group: Enzymes. Synonyms: CASP-6; apoptotic protease Mch-2; Mch2. Enzyme Commission Number: EC 3.4.22.59. CAS No. 182372-15-2. 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-4234; caspase-6; EC 3.4.22.59; 182372-15-2; CASP-6; apoptotic protease Mch-2; Mch2. Cat No: EXWM-4234. | |
| Caspase-6 (Active) from Human, Recombinant | Caspase-6 is an enzyme that in humans is encoded by the CASP6 gene. This gene encodes a protein that is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes that undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein is processed by caspases 7, 8 and 10, and is thought to function as a downstream enzyme in the caspase activation cascade. Caspase 6 can also undergo self-processing without other members of the caspase family. Alternative splicing of this gene results in two transcript variants that encode different isoforms. Group: Enzymes. Synonyms: CASP6; MCH2; Caspase-6 (Active); Caspase-6. Caspase 6. Appearance: Liquid. Storage: -80°C. Form: Liquid. 5μg in 25μl of 50mM TRIS (pH 8.0) containing 100mM sodium chloride and 50mM imidazole. Source: E. coli. Species: Human. CASP6; MCH2; Caspase-6 (Active); Caspase-6. Cat No: NATE-0814. | |
| caspase-7 | Caspase-7 is an effector/executioner caspase, as are caspase-3 (EC 3.4.22.56) and caspase-6 (EC 3.4.22.59). These caspases are responsible for the proteolysis of the majority of cellular polypeptides [e.g. poly(ADP-ribose) polymerase (PARP)], which leads to the apoptotic phenotype. Although a hydrophobic residue at P5 of caspase-2 (EC 3.4.22.55) and caspase-3 leads to more efficient hydrolysis, the amino-acid residue at this location in caspase-7 has no effect. Caspase-7 is activated by the initiator caspases [caspase-8 (EC 3.4.22.61), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63)]. Removal of the N-terminal prodomain occurs before cleavage in the linker region between the large and small subunits. Belongs in peptidase family C14. Group: Enzymes. Synonyms: CASP-7; ICE-like apoptotic protease 3; ICE-LAP3; apoptotic protease Mch-3; Mch3; CMH-1. Enzyme Commission Number: EC 3.4.22.60. CAS No. 189258-14-8. 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-4236; caspase-7; EC 3.4.22.60; 189258-14-8; CASP-7; ICE-like apoptotic protease 3; ICE-LAP3; apoptotic protease Mch-3; Mch3; CMH-1. Cat No: EXWM-4236. | |
| Caspase-7 from Human, Recombinant | Caspase-7 is a member of the caspase (cysteine aspartate protease) family of proteins, and has been shown to be an executioner protein of apoptosis. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes that undergo proteolytic processing by upstream caspases (caspase-8, -9) at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme in the form of a heterotetramer. The precursor of this caspase is cleaved by caspase 3, caspase 10, and caspase 9. It is activated upon cell death stimuli and induces apoptosis. Alternative splicing results in four transcript variants, encoding three distinct isoforms. Applications: Used to screen caspase inhibitors, study enzyme regulation, determine caspase substrate specificity, or as positive control in caspase activity assays. Group: Enzymes. Synonyms: CASP7; CASP-7; CMH-1; ICE-LAP3; LICE2; MCH3; Caspase-7. Enzyme Commission Number: EC 3.4.22.-. Purity: 90% (SDS-PAGE). Caspase 7. Activity: ~25,000U/mg protein. Appearance: Lyophilized. Storage: -80°C. Source: E. coli. Species: Human. CASP7; CASP-7; CMH-1; ICE-LAP3; LICE2; MCH3; Caspase-7. Cat No: NATE-0815. | |
| caspase-8 | Caspase-8 is an initiator caspase, as are caspase-2 (EC 3.4.22.55), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63). Caspase-8 is the apical activator of the extrinsic (death receptor) apoptosis pathway, triggered by death receptor ligation. It contains two tandem death effector domains (DEDs) in its N-terminal prodomain, and these play a role in procaspase activation. This enzyme is linked to cell surface death receptors such as Fas. When Fas is aggregated by the Fas ligand, procaspase-8 is recruited to the death receptor where it is activated. The enzyme has a preference for Glu at P3 and prefers small residues, such as Gly, Ser and Ala, at the P1' position. It has very broad P...ORT1-associated CED-3 homolog; Mch5; mammalian Ced-3 homolog 5; CASP-8; ICE-like apoptotic protease 5; FADD-homologous ICE/CED-3-like protease; apoptotic cysteine protease; apoptotic protease Mch-5; CAP4. Enzyme Commission Number: EC 3.4.22.61. CAS No. 179241-78-2. 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-4237; caspase-8; EC 3.4.22.61; 179241-78-2; FLICE, FADD-like ICE; MACH; MORT1-associated CED-3 homolog; Mch5; mammalian Ced-3 homolog 5; CASP-8; ICE-like apoptotic protease 5; FADD-homologous ICE/CED-3-like protease; apoptotic cysteine protease; apoptotic protease Mch-5; CAP4. Cat No: EXWM-4237. | |
| caspase-9 | Caspase-9 is an initiator caspase, as are caspase -2 (EC 3.4.22.55), caspase-8 (EC 3.4.22.61) and caspase-10 (EC 3.4.22.63). Caspase-9 contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation. An alternatively spliced version of caspase-9 also exists, caspase-9S, that inhibits apoptosis, similar to the situation found with caspase-2. Phosphorylation of caspase-9 from some species by Akt, a serine-threonine protein kinase, inhibits caspase activity in vitro and caspase activation in vivo. The activity of caspase-9 is increased dramatically upon association with the apoptosome but the enzyme can be activated without proteolytic cleavage. Procaspase-3 is the enzyme's physiological substrate. Belongs in peptidase family C14. Group: Enzymes. Synonyms: CASP-9; ICE-like apoptotic protease 6; ICE-LAP6; apoptotic protease Mch-6; apoptotic protease-activating factor 3; APAF-3. Enzyme Commission Number: EC 3.4.22.62. CAS No. 180189-96-2. 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-4238; caspase-9; EC 3.4.22.62; 180189-96-2; CASP-9; ICE-like apoptotic protease 6; ICE-LAP6; apoptotic protease Mch-6; apoptotic protease-activating factor 3; APAF-3. Cat No: EXWM-4238. | |
| Cathepsin B from Human, recombinant | Cathepsin B is a lysosomal cysteine protease. It is implicated in playing a role in protein degradation, arthritis, apoptosis, and cancer. Group: Enzymes. Synonyms: CTSB; 9047-22-7; APPS; CPSB; cathepsin B1 (obsolete); cathepsin II. Enzyme Commission Number: EC 3.4.22.1. CAS No. 9047-22-7. Purity: > 90% by SDS-PAGE. Cathepsin B. Mole weight: 27.8 kDa (80-333 aa). Activity: >7500 mU/mg. Storage: Stable for at least 1 year as supplied. Dilute in de-ionized water to 0.1 mg/ml and store at -80°C. Avoid repeated freezing and thawing cycles. Form: Liquid. Source: E. coli. Species: Human. CTSB; cathepsin B; 9047-22-7; APPS; CPSB; cathepsin B1 (obsolete); cathepsin II; EC 3.4.22.1. Cat No: NATE-1706. | |
| Cathepsin D from Human, recombinant | Cathepsin D is a lysosomal aspartyl protease composed of a protein dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. It is an estrogen-regulated protein associated with tissue breakdown. Levels of cathepsin D have been positively correlated with recurring breast cancers of both node negative and node positive types. Additionally cathepsin D has been associated with amyloid formation in Alzheimer's plaques. Cathepsin D is produced initially as a pre-pro-enzyme which gets transported to lysosomes via endosomes in most cell types. In endosomes, it gets proteolyzed by unidentified proteases by removal of the pro-peptide to generate...e cathepsins B and L generates mature, active double-chain Cathepsin D. Group: Enzymes. Synonyms: CTSD; 9025-26-7; EC 3.4.23.5; CLN10; CPSD; HEL-S-130P; Procathepsin D. Enzyme Commission Number: EC 3.4.23.5. CAS No. 9025-26-7. Purity: > 80% by SDS-PAGE. CTSD. Mole weight: 45.1 kDa. Activity: >100 pmol/min/mg. Storage: Store at -20°C. Stable for at least 6 months as supplied. Reconstitute to 1 mg/ml in sterile water, store at -80°C in aliquots and use within 6 months after reconstitution. Avoid repeated freeze-thaw cycles. Form: Freeze-Dried. Source: E. coli. Species: Human. CTSD; cathepsin D; 9025-26-7; EC 3.4.23.5; CLN10; CPSD; HEL-S-130P; Procathepsin D. Cat No: NATE-1707. | |
| Cathepsin S from Human, recombinant | Cathepsin S (CTSS) is a lysosomal cysteine protease of the papain family and may participate in the degradation of antigenic proteins to peptides for presentation on MHC class II molecules. CTSS is synthesized as inactive precursor of 331 amino acids consisting of a 15-aa signal peptide, a propeptide of 99 aa, and a mature polypeptide of 217 aa. It is activated in the lysosomes by a proteolytic cleavage of the propeptide. The deduced amino acid sequence contains only one potential N-glycosylation site located in the propeptide. Compared with the abundant cathepsins B, L and H, cathepsin S shows a restricted tissue distribution, with highest levels in spleen, heart, and lung...l compartment, and is implicated in the pathogenesis of Alzheimers disease and Down Syndrome. Group: Enzymes. Synonyms: CTSS; cathepsin S; EC 3.4.22.27; FLJ50259; MGC3886. Enzyme Commission Number: EC 3.4.22.27. CAS No. 71965-46-3. Purity: > 90% by SDS-PAGE. CTSS. Mole weight: 23.9 kDa (115-331 aa). Activity: >2000 mU/mg. Storage: Stable for at least 1 year as supplied. Briefly spin down the vial and reconstitute in 50 mM sodium acetate, 100 mM NaCl (pH 5.5) to 0.1-1 mg/ml and store at -80°C. Avoid repeated freeze and thaw cycles. Form: Lyophilized from proprietary buffer. Source: E. coli. Species: Human. CTSS; cathepsin S; EC 3.4.22.27; FLJ50259; MGC3886. Cat No: NATE-1702. | |
| Chicking biddy feed enzymes | It is developed according to the digestive physiology of chicks and typical diets. The results of experiments showed that the products could not only effectively supplement the digestive enzyme of chicks, but also inhibited the proliferation of pathogen, improved the health condition of chick, and then enhanced feed utilization ratio. Thus the growth rate was increased uniformly. Ingredients: Protease, amylase, lipase, xylanase, β-mannanase, α-galactosidase. Applications: 1. make up inadequate secretion of endogenous enzyme of chicks to improve animal feed intake and feed efficiency; 2. through inhibiting the proliferation of harmful microorganisms, to improve chick growth rate and colony homogeneity; 3. increase their survival rate by enhancing disease resistance of chicks; 4. by means of breaking down anti-nutritional factors in feed, to improve digestion and absorption of the dietary energy and protein; 5. it can reduce excretion of nitrogen and phosphorus, to reduce environmental pollution. Group: Enzymes. Synonyms: Chicking biddy feed enzymes; digestive enzymes; enhanced feed utilization ratio; impro. Chicking biddy feed enzymes. Appearance: pellet. Chicking biddy feed enzymes; digestive enzymes; enhanced feed utilization ratio; improve chick growth rate; FEED-2329. Pack: 25kg/barrel or subject to client requirement. Cat No: FEED-2329. | |
| Chondroitinase AC from Flavobacterium heparinum, Recombinant | Chondroitinase AC from Flavobacteriun heparinum is an eliminase that degrades chondroitin sulfates A and C, but not chondroitin sulfate B. The enzyme cleaves, via an elimination mechanism, both sulfated and non-sulfated polysaccharide chains that contain (1?4)-linkages between hexosamines and glucuronic acid residues. The reaction yields oligosaccharide products, mainly disaccharides, with unsaturated uronic acids that can be detected by UV spectroscopy at 232 nm. Applications: Chondroitinase ac was shown to inhibit melanoma invasion and proliferation, endothelial proliferation, and angiogenesis. chondroitinase ac, but not chondroitinase b, has also been shown t..., and protease activities. ChnAC. Activity: >200 units/mg protein. Appearance: Powder. Storage: Store the product at -20?C. When stored properly and unopened at -20?C, the enzyme has a recommended retest date of 2 years. After reconstitution, the product may be kept at 4?C for 4 days, but it is recommended to store the solution in working aliquots at -20 ?C. Form: The enzyme is supplied as a lyophilized powder containing potassium phosphate, NaCl, and a stabilizer. Source: E. coli. Species: Flavobacterium heparinum. chondroitinase (ambiguous); chondroitin sulfate lyase; chondroitin AC eliminase; chondroitinase AC; ChnAC; 9047-57-8; EC 4.2.2.5. Cat No: NATE-1738. | |
| chymase | In mast cell granules. In peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: mast cell protease I; skeletal muscle protease; skin chymotryptic proteinase; mast cell serine proteinase, chymase; skeletal muscle (SK) protease. Enzyme Commission Number: EC 3.4.21.39. CAS No. 97501-92-3. CMA1. 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-4133; chymase; EC 3.4.21.39; 97501-92-3; mast cell protease I; skeletal muscle protease; skin chymotryptic proteinase; mast cell serine proteinase, chymase; skeletal muscle (SK) protease. Cat No: EXWM-4133. | |
| Chymase from Human, Recombinant | Chymases are a family of serine proteases found primarily in mast cells, though also present in basophil granulocytes (e.g. alpha chymase mcpt8). They show broad peptidolytic activity and are involved in a variety of functions. For example, chymases are released by mucosal mast cells upon challenge with parasites and parasite antigens promoting an inflammatory response. Chymases are also known to convert angiotensin I to angiotensin II and thus play a role in hypertension and atherosclerosis. Because of its role in inflammation it has been investigated as a target in the treatment of asthma. Applications: Chymase has been implicated in generation of angiotensin ii and cleavag... Synonyms: mast cell protease I; skeletal muscle protease; skin chymotryptic proteinase; mast cell serine proteinase, chymase; skeletal muscle (SK) protease; chymase; EC 3.4.21.39; 97501-92-3. Enzyme Commission Number: EC 3.4.21.39. CAS No. 97501-92-3. Purity: >90% (SDS-PAGE). CMA1. Mole weight: ~30 kDa. Activity: >40 units/mg protein. Storage: Store at -20°C. Form: Supplied as a solution in 20 mM Tris, 0.8 M NaCl and 25% glycerol, pH 7.6. Source: Pichia pastoris. Species: Human. mast cell protease I; skeletal muscle protease; skin chymotryptic proteinase; mast cell serine proteinase, chymase; skeletal muscle (SK) protease; chymase; EC 3.4.21.39; 97501-92-3. Cat No: NATE-0817. | |
| Chymotrypsin | Chymotrypsin is a proteolytic enzyme. It can priority hydrolyze tyrosine containing l-isomer, phenylalanine and the peptide bond of tryptophan, the best effective condition is pH 8.0. Its activity can be restrained by heavy metal or natural trypsin inhibitor in some degrees. Applications: Practically used to heal cicatrisation caused by injuries, inflammation and it is also used for avoiding part dropsy, blood-gathering, haematoma caused by wrick, breast dropsy after operation, tympanitis and rhinitis brief introduction of production: the high purity chymotrypsin is extracted from bovine or porcine pancreas and purified by affinity chromatography in order to avoid being polluted by other protease. Group: Enzymes. Synonyms: Chymotrypsin; Alpha-chymotrypsin; Chymotrypsin A; Chymotrypsin B. CAS No. 9004-7-3. Chymotrypsin. Appearance: inquire. Chymotrypsin; Alpha-chymotrypsin; Chymotrypsin A; Chymotrypsin B. Pack: inquire. Cat No: BIO-1012. | |
| Chymotrypsin from Human, Recombinant | Chymotrypsin is a recombinant serine endopeptidase expressed in E.coli, purified with HPLC, the gene sequence is the same as human chymotrypsin. Recombinant chymotrypsin hydrolyzes at the carboxyl side of aromatic amino acids residues: Tyr, Phe and Trp. Cleavage may also be observed, but at a lower rate, at Leu and Met. Chymotrypsin activity is optimal in pH 7.0-9.0. Applications: Hydrolysis of proteins by chymotrypsin alone or in combination with other proteases. suitable for peptide mapping, fingerprinting, and sequence analysis. Group: Enzymes. Synonyms: EC 3.4.21.1; chymotrypsins A and B; alpha-chymar ophth; avazyme; chymar; chymotest; enzeon; quimar; quimotrase; alpha-chymar; alpha-chymotrypsin A; alpha-chymotrypsin; Chymotrypsin; &alpha. Enzyme Commission Number: EC 3.4.21.1. CAS No. 9004-7-3. Purity: > 95% by HPLC. Chymotrypsin. Mole weight: 26,950 Da. Activity: >1000 unit/mg protein. Storage: Recombinant Chymotrypsin lyophilized should be stored under 2°C-8°C in sealed container. It is stable within 24 months. After dissolved, it should be stored under -20°C. Form: White lyophilized. Source: E. coli. Species: Human. EC 3.4.21.1; chymotrypsins A and B; alpha-chymar ophth; avazyme; chymar; chymotest; enzeon; quimar; quimotrase; alpha-chymar; alpha-chymotrypsin A; alpha-chymotrypsin; Chymotrypsin; α-Chymotrypsin. Cat No: NATE-1890. | |
| Clostripain | Clostripain (Clostridiopeptidase B) is a proteolytic enzyme isolated from Clostridium histolyticum with esterase, amidase and protease activities and is a highly specific carboxypeptide targeting arginine key protease [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: Clostridiopeptidase B. CAS No. 9028-00-6. Pack Sizes: 1 mg. Product ID: HY-P2895. | |
| Collagenase AF-1 GMP Grade | Collagenase AF-1 GMP Grade, often in combination with Neutral Protease AF GMP Grade, is suitable for the dissociation of sensitive cells from several tissues, such as pancreas, liver and dental pulp. It has been shown to be highly effective for the isolation of islets of Langerhans from human pancreas intended for transplantation. Applications: Collagenase af-1 gmp grade is suitable for cell isolation from several tissue types intended for clinical applications. it is often used in combination with neutral protease af gmp grade. Group: Enzymes. Synonyms: Collagenase AF-1; Collagenase; Collagenase AF-1 GMP; Collagenase GMP. Enzyme Commission Number: EC 3.4.24.3. CAS No. 9001-12-1. Collagenase. Activity: ≥ 3.00 U/mg. Storage: 2 to 8 °C. Form: Lyophilized powder. Source: Clostridium histolyticum. Collagenase AF-1; Collagenase; Collagenase AF-1 GMP; Collagenase GMP. Cat No: NATE-1919. | |
| Collagenase (food grade) | Collagenase is an enzyme complex to hydrolyzed gelatin and collagen, mainly composed by endo-proteases, exo-protease and flavor enzymes. Group: Enzymes. Synonyms: Endo-protease; Exo-protease; flavor enzyme; Collagenase. Collagenase. Activity: >100,000 u/g. Appearance: White or yellowish, odorless, powder. Endo-protease; Exo-protease; flavor enzyme; Collagenase. Cat No: NATE-1594. | |
| Collagenase/Neutral Protease Blend (GMP Grade) | NATE-1917 is an avian and mammalian tissue-free Collagenase and neutral protease enzyme blend produced under GMP quality conditions. Applications: Nate-1917 is specifically designed for stem cell isolation from human and other adipose tissue with following advantages:o a single, sterile, ready-to-use vial containing both collagenase and neutral protease can digest up to 280g of adipose tissue with best-in-class gmp quality and shelf life of up to 72 months.o currently included in ide applications approved by the u.s. fda for alopecia, chronic heart failure, hamstring injuries, osteoarthritis of the knee, and hand manifestations of scleroderma.o research protocols are a...sociation of nucleated cells from adipose tissue.o produced using avian and mammalian tissue-free raw materials, aseptic processes and sterile filtration under gmp guidelines to assure the lowest levels of impurities and stringent quality standards. Group: Enzymes. Synonyms: Collagenase/Neutral Protease Blend; GMP, Collagenase/Neutral Protease Blend; Collagenase; Neutral Protease; GMP. Collagenase. Stability: 48 months at -15 to -25° C. Appearance: White lyophilizate. Source: Clostridium histolyticum/Bacillus polymyxa. Collagenase/Neutral Protease Blend; GMP, Collagenase/Neutral Protease Blend; Collagenase; Neutral Protease; GMP. Pack: 1 vial, 35 mg. Cat No: NATE-1917. | |
| 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. | |
| 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. | |
| C-terminal processing peptidase | Proteolytic processing of the D1 protein of photosystem II is necessary to allow the light-driven assembly of the tetranuclear manganese cluster, which is responsible for photosynthetic water oxidation. The recognition of the substrate is mediated by a PDZ domain, a small protein module that promotes protein-protein interactions by binding to internal or C-terminal sequences of their partner proteins. Type example of peptidase family S41. Group: Enzymes. Synonyms: CtpA gene product (Synechocystis sp.); photosystem II D1 protein processing peptidase; protease Re; tail-specific protease; Tsp protease. Enzyme Commission Number: EC 3.4.21.102. CAS No. 216484-75-2, 92480-11-0. 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-4097; C-terminal processing peptidase; EC 3.4.21.102; 216484-75-2, 92480-11-0; CtpA gene product (Synechocystis sp.); photosystem II D1 protein processing peptidase; protease Re; tail-specific protease; Tsp protease. Cat No: EXWM-4097. | |
| Cysteine protease from Streptococcus pyogenes, Recombinant | Cysteine protease is an enzyme for single site digestion of antibodies in the hinge region. Incubation for one hour at 37°C under reducing conditions is enough for cysteine protease to cleave all subclasses of human, mouse, rat, goat and sheep IgG. Cysteine protease is supplied as lyophilized powder with no preservatives added and is available in a 2000 units pack size. Cysteine protease contains a His-tag and can easily be removed after digestion. Group: Enzymes. Synonyms: Cysteine protease; FabULOUS. Purity: > 95% homogeneity as determined by SDS-PAGE analysis using Coomassie Blue detection. Cysteine protease. Stability: The enzyme is reconstituted by addition of water and after reconstitution it is stable for 1 month at +4-8°C. The product is shipped on ice and should be stored at -20°C upon arrival. Appearance: White to light yellow powder. Storage: at -20°C. Form: Lyophilized powder with no preservatives added. Source: E.coli. Species: Streptocoocus pyogenes. Cysteine protease; FabULOUS Enzyme; FabULOUS; protease. Cat No: NATE-1600. | |
| desampylase | The enzyme, characterized from the archaeon Haloferax volcanii, specifically cleaves the ubiquitin-like small modifier proteins SAMP1 and SAMP2 from protein conjugates, hydrolysing the isopeptide bond between a lysine residue of the target protein and the C-terminal glycine of the modifier protein. The enzyme contains Zn2+. cf. EC 3.4.19.12, ubiquitinyl hydrolase 1. In peptidase family M67. Group: Enzymes. Synonyms: SAMP-protein conjugate cleaving protease; HvJAMM1. Enzyme Commission Number: EC 3.4.24.88. 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-4372; desampylase; EC 3.4.24.88; SAMP-protein conjugate cleaving protease; HvJAMM1. Cat No: EXWM-4372. | |
| deuterolysin | Proteolytic activity found in Penicillium roqueforti, P. caseicolum, Aspergillus sojae and A. oryzae. Optimum pH of 5 for digesting various proteins. Strong action on protamine and histones. Insensitive to phosphoramidon. About 20 kDa. A distinct Aspergillus sojae endopeptidase is larger and has a neutral pH optimum. Type example of peptidase family M35. Formerly included in EC 3.4.24.4. Group: Enzymes. Synonyms: Penicillium roqueforti protease II; microbial neutral proteinase II; acid metalloproteinase; neutral proteinase II; Penicillium roqueforti metalloproteinase. Enzyme Commission Number: EC 3.4.24.39. CAS No. 247028-11-1. 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-4321; deuterolysin; EC 3.4.24.39; 247028-11-1; Penicillium roqueforti protease II; microbial neutral proteinase II; acid metalloproteinase; neutral proteinase II; Penicillium roqueforti metalloproteinase. Cat No: EXWM-4321. | |
| Dipeptidyl Peptidase IV from Human, Recombinant | Native DPPIV is a ubiquitous type II transmembrane glycoprotein and a serine protease of the S9 prolyl-oligopeptidase family. In vivo, it is synthesized with a signal peptide, which functions as the membrane anchoring domain. There is an 88% sequence homology between the human and porcine kidney enzymes. Both exist as homodimers with a subunit molecular weight of ~30 kDa. The high mannose 100 kDa DPPIV precursor is processed in the Golgi to yield a 124 kDa heavily N-and O-linked mature glycoprotein. It is then sorted to the apical membrane through the concerted action of both N-and O-linked glycans and its association with lipid microdomains. The porcine enzyme contai...zyme from creative enzymes has been used to study the lc-ms (liquid chromatography-mass spectrometry) based assay method for dpp-iv inhibitor screening and substrate discovery. Group: Enzymes. Synonyms: EC 3.4.14.5; 54249-88-6; DPPIV; DPP4; dipeptidyl aminopeptidase IV; Xaa-Pro-dipeptidyl-aminopeptidase; Gly-Pro naphthylamidase; postproline dipeptidyl aminopeptidase IV; lymphocyte antigen CD26; glycoprotein GP110; dipeptidyl peptidase IV; glycylproline aminopeptidase; glycylproline aminopeptidase; X-prolyl dipeptidyl aminopeptidase; pep X; leukocyte antigen CD26; glycylprolyl dipeptidylaminopeptidase; dipeptidyl-peptide hydrolase; glycylprolyl aminopeptidase; dipeptidy | |
| Dispase II | Dispase II is a neutral protease that hydrolyzes the N-terminal peptide bonds of non-polar amino acid residues. It may be used for separating many tissues and cells grown in vitro. The enzyme is very gentle and does not damage cell membranes. It can also be used to prevent clumping in suspension cultures. This protease cleaves fibronectin and type IV collagen, but not laminin, type V collagen, serum albumin, or transferrin.[3] Dispase II is specific for the cleavage of Leucine-Phenylalanine bonds. Ca2+, Mg2+, Mn2+, Fe2+, Fe3+ and Al3+ activate the enzyme. EDTA, EGTA, Hg2+ and other heavy metals inhibit the enzyme activity.[6] The enzyme contains 1g-atom of zinc per g-mol of purified enzyme. If this zinc component is removed by chelating agents such as EDTA or EGTA, an inactive apoenzyme is obtained. The enzyme is not inhibited by serum. Group: Biochemicals. Grades: Highly Purified. CAS No. 42613-33-2. Pack Sizes: 50mg, 100mg, 250mg, 500mg, 1g. US Biological Life Sciences. | Worldwide |
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