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Boc-LLR-AMC is a good substrate for the Kex2 endoprotease. Synonyms: Boc-LRR-AMC; N-[(1,1-dimethylethoxy)carbonyl]-L-leucyl-L-arginyl-N-(4-methyl-2-oxo-2H-1-benzopyran-7-yl)-L-argininamide; 7-[(Boc-Leu-Arg-Arg-)Amino]-4-methylcoumarin. Grade: 95%. CAS No. 109358-46-5. Molecular formula: C33H54Cl2N10O7. Mole weight: 773.75.
Boc-leu-lys-arg-amc hydrochloride salt
Boc-LKR-AMC is a good substrate for the Kex2 endoprotease. Synonyms: 4-Methyl-7-(Boc-L-Leu-L-Lys-L-Arg-amino)-2H-1-benzopyran-2-one; Boc-LKR-AMC. Grade: 95%. CAS No. 109358-47-6. Molecular formula: C33H52N8O7. Mole weight: 672.82.
Furin from Human, Recombinant
Furin is a dibasic endoprotease that is localized in the Golgi apparatus. It is responsible for the proteolytic maturation of many precursor proteins in the secretory and endocytic pathways of mammalian cells. Furin is a dibasic endoprotease that is localized in the Golgi apparatus. It has a molecular mass of 52.7 kDa. It is responsible for the proteolytic maturation of many precursor proteins in the secretory and endocytic pathways of mammalian cells. Furin cleaves precursor proteins at their paired basic amino acid processing sites. Some substrates of furin include von Willebrand factor, transforming growth factor beta 1 precursor, pro-beta-secretase and proparathyroid hormo.terial exotoxins, typically at sites marked by the consensus sequence arg-xaa-(lys/arg)-arg. Group: Enzymes. Synonyms: furin; prohormone convertase; dibasic processing enzyme; PACE; paired basic amino acid cleaving enzyme; paired basic amino acid converting enzyme; serine proteinase PACE; PC1; SPC3; proprotein convertase. Furin. Activity: > 2,000 unit/mL. Storage: -70°C. Form: buffered aqueous solution. Source: Baculovirus infected Sf9 cells. Species: Human. furin; prohormone convertase; dibasic processing enzyme; PACE; paired basic amino acid cleaving enzyme; paired basic amino acid converting enzyme; serine proteinase PACE; PC1; SPC3; proprotein convertase. Cat No: NATE-0268.
Furin Substrate, Fluorogenic
A fluorogenic substrate for furin, a mammalian homolog of the yeast Kex2 endoprotease (kcat/Km ~ 2 x 10? s?¹M?¹). Group: Fluorescence/luminescence spectroscopy.
Histatin-3 TFA
Histatin-3 TFA, a 32 amino acid peptide, possesses powerful antimicrobial properties. Histatin-3 TFA behaves as a substrate for proprotein convertase 1 (PC1), being cleaved by this endoprotease primarily at a site carboxy terminal to the single Arg25 residue (HRGYR decrease SN). Histatin-3 TFA is a moderately potent, reversible and competitive inhibitor of the furin-mediated cleavage of the pentapeptide pGlu-Arg-Thr-Lys-Arg-MCA fluorogenic substrate, with an estimated inhibition constant K i of 1.98 μM [1]. Uses: Scientific research. Group: Peptides. CAS No. 112844-49-2. Pack Sizes: 5 mg; 10 mg. Product ID: HY-P5272.
HtrA2 peptidase
This enzyme is upregulated in mammalian cells in response to stress induced by both heat shock and tunicamycin treatment. It can induce apoptosis in a caspase-independent manner through its peptidase activity and in a caspase-dependent manner by disrupting the interaction between caspase and the inhibitor of apoptosis (IAP). Belongs in peptidase family S1C. Group: Enzymes. Synonyms: high temperature requirement protein A2; HtrA2; Omi stress-regulated endoprotease; serine proteinase OMI; HtrA2 protease; OMI/HtrA2 protease; HtrA2/Omi; Omi/HtrA2. Enzyme Commission Number: EC 3.4.21.108. 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-4103; HtrA2 peptidase; EC 3.4.21.108; high temperature requirement protein A2; HtrA2; Omi stress-regulated endoprotease; serine proteinase OMI; HtrA2 protease; OMI/HtrA2 protease; HtrA2/Omi; Omi/HtrA2. Cat No: EXWM-4103.
kexin
A Ca2+-activated peptidase of peptidase family S8, containing Cys near the active site His, and inhibited by p-mercuribenzoate. Similar enzymes occur in mammals. Group: Enzymes. Synonyms: yeast KEX2 protease; proteinase yscF; prohormone-processing endoprotease; paired-basic endopeptidase; yeast cysteine proteinase F (misleading); paired-basic endopeptidase; andrenorphin-Gly-generating enzyme; endoproteinase Kex2p; gene KEX2 dibasic proteinase; Kex 2p proteinase; Kex2 endopeptidase; Kex2 endoprotease; Kex2 endoproteinase; Kex2 protease; proteinase Kex2p; Kex. Enzyme Commission Number: EC 3.4.21.61. CAS No. 99676-46-7. 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-4152; kexin; EC 3.4.21.61; 99676-46-7; yeast KEX2 protease; proteinase yscF; prohormone-processing endoprotease; paired-basic endopeptidase; yeast cysteine proteinase F (misleading); paired-basic endopeptidase; andrenorphin-Gly-generating enzyme; endoproteinase Kex2p; gene KEX2 dibasic proteinase; Kex 2p proteinase; Kex2 endopeptidase; Kex2 endoprotease; Kex2 endoproteinase; Kex2 protease; proteinase Kex2p; Kex2-like precursor protein processing endoprotease; prohormone-processing KEX2 proteinase; prohormone-processing proteinase; proprotein convertase; protease KEX2; Kex2 proteinase; Kex2-like endoproteinase. Cat No: EXWM-4152.
Maculatin 1.1.1
Maculatin 1.1.1, which arises from the action of an endogenous endoprotease to remove the first two residues of maculatin 1.1, is essentially inactive.
Native Aspergillus aculeatus Pectinase
Pectinase is an active pectolytic enzyme preparation that is produced by a selected strain of Aspergillus aculeatus. It contains mainly pectintranseliminase, polygalacturonase and pectinesterase, along with small amounts of hemicellulases and cellulases. Pectinase hydrolyzes pectin, which is a component of the cell wall. They may attack methyl-esterified pectin or de-esterified pectin. Fungal protease/peptidase complex produced by submerged fermentation of a selected strain of aspergillus oryzae and contains both endoprotease and exopeptidase activities. Applications: Pectinase from aspergillus aculeatus is used in plant protoplast preparation to digest cell wall prior to organelle isolation. it has been used to conduct partial saccharification of sugars. pectinases are used to study their role in the invasion of plant tissues using phytopathogens, as well as various food processing and plant biotechnology applications. the enzyme from creative enzymes has been used to determine the content of quercetin produced and also to evaluate its rutinase activity. Group: Enzymes. Synonyms: Pectinase. CAS No. 9032-75-1. Pectinase. Activity: > 500 U/g. Form: aqueous solution. Source: Aspergillus aculeatus. Pectinase. Cat No: NATE-0534.
Native Aspergillus oryzae Protease
Protease catabolizes proteins by hydrolysis of peptide bonds. Protease, from Aspergillus oryzae, contains both endoprotease and exopeptidase activities. Fungal protease/peptidase complex produced by submerged fermentation of a selected strain of aspergillus oryzae and contains both endoprotease and exopeptidase activities. 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. protease is used in nucleic acid isolation procedures in incubations. this product is a fungal protease/peptidase complex produced by submerged fermentation of a selected strain of aspergillus oryzae. it has been injected into flies with a nanoject apparatus for infection and survival experiments. the enzyme from creative enzymes has been used in the semi-purification of mouse colorectal mucins during protein digestion. Group: Enzymes. Synonyms: Protease; Flavourzyme. CAS No. 9001-92-7. Protease. Source: Aspergillus oryzae. Protease; Flavourzyme. Cat No: NATE-0631.
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 Streptomyces griseus Aminopeptidase I
Aminopeptidase I from S. griseus has a fairly broad specificity, being able to remove the N-terminal residue of most proteins, except where the penultimate residue is an imino acid. It contains two Zn2+ binding sites. Aminopeptidase I from S. griseus is inhibited by 1,10-phenanthroline and is activated six-fold by Ca2+, which also stabilizes it against heat inactivation. This monomeric zinc metalloprotein has an isoelectric point (pI) of 5.4. Applications: Aminopeptidase i from streptomyces griseus may be used as a reagent for the analysis of protein structure and as a model for studies of proteolytic enzyme activation by calcium ions. it may be used as a reagent in the assay of endoprotease activities with a synthetic substrate in a two-stage assay. the lyophilized powder also contains calcium acetate. Group: Enzymes. Synonyms: aminopeptidase III; aminopeptidase yscI; leucine aminopeptidase IV; yeast aminopeptidase I; EC 3.4.11.22; 9031-94-1; Aminopeptidase I. Enzyme Commission Number: EC 3.4.11.22. CAS No. 9031-94-1. Aminopeptidase I. Activity: > 200 units/mg protein. Storage: -20°C. Form: lyophilized powder. Contains calcium acetate. Source: Streptomyces griseus. aminopeptidase III; aminopeptidase yscI; leucine aminopeptidase IV; yeast aminopeptidase I; EC 3.4.11.22; 9031-94-1; Aminopeptidase I. Cat No: NATE-0070.
Boc-GKR-AMC is a substrate for the Kex2 endoprotease. Synonyms: Boc-Gly-Lys-Arg-Amc-HCl; tert-butyl 2-((S)-6-amino-1-((S)-5-guanidino-1-(4-methyl-2-oxo-2H-chromen-7-ylamino)-1-oxopentan-2-ylamino)-1-oxohexan-2-ylamino)-2-oxoethylcarbamate hydrochloride; Boc-GKR-AMC. Grade: 95%. CAS No. 133448-23-4. Molecular formula: C29H45ClN8O7. Mole weight: 653.18.
Protease S from Pyrococcus furiosus, Recombinant
Protease S is a serine endoprotease with broad specificity that will digest native and denatured proteins. Cleavage occurs mainly on the carboxy side of peptide bonds. The optimal temperature range is 85 to 95°C and the optimal pH range is 6.0 to 8.0. Protease S is inhibited by PMSF. Thermostable serine protease with broad specificity for native and denatured proteins. Applications: Protease s is from pyrococcus furiosus and is a recombinant protease that is expressed in bacillus sp. it is used for fragmentation of proteins and peptides required for primary structure analysis. Group: Enzymes. Synonyms: Protease S; peptidase S; proteinase S. Protease. Storage: 2-8°C. Form: Solution in 25 mM Tris-HCl, pH 7.6, containing 40% ethanol. Source: Bacillus sp. Species: Pyrococcus furiosus. Protease S; peptidase S; proteinase S. Cat No: NATE-0630.
Z-Pro-Pro-aldehyde-dimethyl acetal
Z-Pro-Pro-aldehyde-dimethyl acetal is a potent inhibitor of prolyl endopeptidase (PEP), a cytoplasmic serine endoprotease (IC50= 120 μM). Synonyms: Z-PP-CHO. Grade: >98%. CAS No. 170116-63-9. Molecular formula: C20H28N2O5. Mole weight: 376.45.
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