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PMSF is an irreversible serine/cysteine protease inhibitor commonly used in the preparation of cell lysates. Uses: Scientific research. Group: Signaling pathways. Alternative Names: Phenylmethylsulfonyl fluoride; Benzylsulfonyl fluoride. CAS No. 329-98-6. Pack Sizes: 10 mM * 1 mL; 100 mg; 500 mg. Product ID: HY-B0496.
PMSF
Used as a Protease inhibitor such as Chymotrypsin, Trypsin and Thrombin as well as Acetylcholineesterase. Synonyms: Phenylmethylsulfonyl Fluoride. Grades: ≥ 99% (GC). CAS No. 329-98-6. Molecular formula: C7H7FO2S. Mole weight: 174.19.
Phenylmethanesulfonyl fluoride (PMSF)
25g Pack Size. Group: Analytical Reagents, Biochemicals, Research Organics & Inorganics. Formula: C7H7FO2S. CAS No. 329-98-6. Prepack ID 13342346-25g. Molecular Weight 174.19. See USA prepack pricing.
Phenylmethanesulfonyl fluoride (PMSF)
5g Pack Size. Group: Analytical Reagents, Biochemicals, Research Organics & Inorganics. Formula: C7H7FO2S. CAS No. 329-98-6. Prepack ID 13342346-5g. Molecular Weight 174.19. See USA prepack pricing.
Phenylmethylsulfonyl fluoride 99+% (PMSF) (GC)
Phenylmethylsulfonyl Fluoride Is a Phospholipase C inhibitor that ameliorates post-ischemic neuronal damage, nonspecific irreversible inhibitor of serine protease and other enzymes, including trypsin, chymotrypsin, thrombin and papain. Protease Inhibitors, detecting and measuring antibodies in human intestinal aspirate. Group: Biochemicals. Alternative Names: α-Toluenesulfonyl Fluoride; Benzylsulfonyl Fluoride; NSC 88499; PMSF; Phenylmethanesulfonyl Fluoride. Grades: Highly Purified. CAS No. 329-98-6. Pack Sizes: 5g, 25g, 100g. Molecular Formula: C?H?FO?S, Molecular Weight: 174.19. US Biological Life Sciences.
Worldwide
Phenylmethylsulfonyl Fluoride (PMSF)
Phenylmethylsulfonyl Fluoride Is a Phospholipase C inhibitor that ameliorates post-ischemic neuronal damage, nonspecific irreversible inhibitor of serine protease and other enzymes, including trypsin, chymotrypsin, thrombin and papain. Protease Inhibitors, detecting and measuring antibodies in human intestinal aspirate. Group: Biochemicals. Alternative Names: α-Toluenesulfonyl Fluoride; Benzylsulfonyl Fluoride; NSC 88499; PMSF; Phenylmethanesulfonyl Fluoride. Grades: Highly Purified. CAS No. 329-98-6. Pack Sizes: 10g, 25g, 50g, 100g. Molecular Formula: C?H?FO?S, Molecular Weight: 174.19. US Biological Life Sciences.
Worldwide
α amylase
α-Amylase isolated from porcine pancreas is a glycoprotein.2 It is a single polypeptide chain of approximately 475 residues containing 2 SH groups and four disulfide bridges and a tightly bound Ca2+ necessary for stability.3,4 Chloride ions are necessary for activity and stability5 The pH range for activity is 5.5 to 8.0, with the pH optimum at 7.6. Α-amylase from porcine pancreas. Applications: Α-amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. product is from porcine pancreas and is type i-a. α-amylase has been used in various plant studies, such as metabolism studies in arabidopsis. Group: Enzymes. S...mission Number: EC 3.2.1.1. CAS No. 9000-90-2. α-Amylase. Mole weight: 51-54 kDa. Activity: 700-1400 units/mg protein (E1%/280). Stability: α-Amylase is stable in 25 mM Tris-HCl, pH 7.5, with 100 mM KCl, at 0 °C or at -20 °C for at least 9 days.8 Another recommended storage condition is in 1 mM phosphate, pH 7.3, with 30 mM CaCl2 at -15 °C. Appearance: Appearance (Color): White to Light Yellow Appearance (Form): Suspension. Form: PMSF treated, saline suspension. Alpha amylase enzyme; for flour; fungal alpha amylase enzyme; enhance quality of flour enzyme; enhance quality; alpha amylase enzyme; flour; alpha amylase; Alpha amylase enzyme for flour; FLO-1301. Cat No: BAK-250.
?-Amylase from porcine pancreas
Type I-A, PMSF treated, saline suspension, 700-1400 units/mg protein (E1%/280). Group: Fluorescence/luminescence spectroscopy.
CARBOXYPEPTIDASE A
CARBOXYPEPTIDASE A. Uses: Designed for use in research and industrial production. Additional or Alternative Names: PEPTIDYL-L-AMINO-ACID HYDROLASE;PEPTIDYL-L-AMINO-ACID HYDROLASE TYPE II-PMSF;EC 3.4.17.1;CARBOXYPOLYPEPTIDASE;CARBOXYPOLYPEPTIDASE TYPE II-PMSF;CARBOXYPEPTIDASE A;CARBOXYPEPTIDASE A, BOVINE PANCREAS;CARBOXYPEPTIDASE A, PMSF TREATED. Product Category: Heterocyclic Organic Compound. Appearance: suspension. CAS No. 11075-17-5. Molecular formula: NULL. Mole weight: 0. Density: 1.00g/mL at20°C. Product ID: ACM11075175. Alfa Chemistry ISO 9001:2015 Certified.
Kex2 Protease from Saccharomyces cerevisiae, Recombinant
Kex2 is a Ca2+-dependent serine protease and cleaves at C-terminal site of Lys-Arg, Arg-Arg, Pro-Arg in pro-α-factor and killer-toxin precursors maturing, it was discovered in Saccharomyces cerevisiae. But Kex2 cant recognize and cut a single basic amino acid,such as carboxyl end peptide bond of arginine and lysine. Recombinant Kex2 is a genetically engineered protein expressed in Pichia pastoris and purified by high pressure liquid chromatography. The activity of Kex2 is not affected by the conventional serine protease inhibitors such as PMSF, TPCK, TLCK inhibition. Group: Enzymes. Synonyms: KEX2 protease; KEX2; protease; kexin; EC 3.4.21.61. Enzyme Commission Number: EC 3.4.21.61. Mole weight: 67±6.7 kD. Activity: >10 unit/mg protein. Storage: Recommended storage temperature: 2°C-8°C.Transport condition: blue ice to keep the environment cool.It should be stored in 20mM NaAc-HAc (pH 5.0-5.5) and 2mM Ca2+. It is stable after 5 cycles freezing and thawing. Form: White lyophilized. Source: Pichia pastoris. Species: Saccharomyces cerevisiae. KEX2 protease; KEX2; protease; kexin; EC 3.4.21.61. Cat No: NATE-1891.
Native Bacillus licheniformis Alkaline Protease
Proteinase catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate. Subtilisin a is a member of the serine s8 endoproteinase family. it has broad specificity with a preference for a large uncharged residue in the p1 position. it hydrolyzes native and denatured proteins, and is active under alkaline conditions. Applications: The enzyme has been used to optimize release of all mitochondrial populations from homogenized ventricular tissue of rat heart.1 it has also been used in the pre-hybridisation treatment of formalin fixed, paraffin wax...ex); MCP; proteasome; large multicatalytic protease; multicatalytic proteinase; proteasome organelle; alkaline protease; 26S protease; triCorn proteinase; triCorn protease; EC 3.4.25.1. Enzyme Commission Number: EC 3.4.25.1. CAS No. 140879-24-9. Alkaline Protease. Mole weight: 27 Kda. Activity: 7.0-14.0 units/mg. Form: lyophilized powder. Source: Bacillus licheniformis. ingensin; macropain; multicatalytic endopeptidase complex; prosome; multicatalytic proteinase (complex); MCP; proteasome; large multicatalytic protease; multicatalytic proteinase; proteasome organelle; alkaline protease; 26S protease; triCorn proteinase; triCorn protease; EC 3.4.25.1. Cat No: NATE-0444.
Native Bacillus licheniformis Protease
Protease catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate. Protease is a serine endoproteinase with a broad specificity towards native and denatured proteins, and is active under alkaline conditions. It is active in some organic solvents such as dry octane. The enzyme is found to be stable at ph 8-10, retaining activity of up to 90% for 24 hours. it shows maximum activity at temperatures between 55-60°c. Applications: The product has been used with other enzymes for in situ proteolysis to produce crystals suitable for structure determi...f bacillus licheniformis. it is a serine endoproteinase with a broad specificity towards native and denatured proteins, and is active under alkaline conditions. Group: Enzymes. Synonyms: Protease; 9014-01-1; Subtilisin A; EC 3.4.21.62; Alcalase. Enzyme Commission Number: EC 3.4.21.62. CAS No. 9001-92-7. Protease. Mole weight: Subtilisin is a non-glycosylated single polypeptide chain without disulfide bonds and has a molecular weight of 27 KDa. Activity: Type VIII, 7-15 units/mg solid; Type I, > 2.4 U/g. Form: Type VIII, lyophilized powder; Type I, aqueous solution. Source: Bacillus licheniformis. Protease; 9014-01-1; Subtilisin A; EC 3.4.21.62; Alcalase. Cat No: NATE-0633.
Native Bacillus licheniformis Proteinase
Proteinase catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate. Subtilisin is a non-glycosylated single polypeptide chain without disulfide bonds and has a molecular weight of 27 kda. Applications: The enzyme from creative enzymes has been used to optimize release of all mit ochondrial populations from homogenized ventricular tissue of rat heart. it has also been used in the pre-hybridisation treatment of formalin fixed, paraffin wax-embedded liver specimens for detecting human and viral dna. this is a proteolytic enzyme isolated from th...ls to study the silencing of cardiac mit ochondrial nhe1. Group: Enzymes. Synonyms: protease; peptidase; proteinase; EC 3.4.21.62; 9014-01-1; Alkaline Protease; Protease from Bacillus licheniformis; Proteinase from Bacillus licheniformis; Subtilo peptidase A. Enzyme Commission Number: EC 3.4.21.62. CAS No. 9001-92-7. Purity: crystallization. Proteinase. Mole weight: 27 KDa. Activity: 7.0-14.0 units/mg solid. Storage: -20°C. Form: lyophilized powder. Source: Bacillus licheniformis. protease; peptidase; proteinase; EC 3.4.21.62; 9014-01-1; Alkaline Protease; Protease from Bacillus licheniformis; Proteinase from Bacillus licheniformis; Subtilo peptidase A. Cat No: NATE-0639.
Native Bovine Protein Phosphatase 2A1
Protein Phosphatase 2A1 is a trimer consisting of the A, B, and C subunits of the PP2A family. It has a total molecular weight of 192 kDa. Protein Phosphatase 2A is a cytoplasmic protein, which colocalizes with mictotubule proteins and is involved in the dephosphorylation of the tau protein and oncoprotein 18. Protein Phosphatase 2A1 binds to polymerized microtubule proteins and may be targeted by tubulin in modulating phosphatase activity. Applications: Protein phosphatase 2a1 is a divalent cation-dependent protein serine/threonine phosphatase implicated as a growth suppressor and is associated with dis-regulation in cancer. the enzyme is involved in regulating numerous cellular processes and is used to study cell cycle, growth, and differentiation. the protein phosphatase 2a1 has been used to treat human fibroblast cells prior to western blot analysis. Group: Enzymes. Synonyms: Protein Phosphatase 2A1; PP2A1; PPA2A1. Purity: >90% (SDS-PAGE). Protein Phosphatase. Activity: > 1500 units/mg protein. Stability: -70°C. Form: Solution in 50 mM Tris-HCl, pH 7.0, containing 14 mM 2-mercaptoethanol, 1 mM benzamidine, 0.1 mM PMSF, 1 mM EDTA, and 50% glycerol. Source: Bovine. Protein Phosphatase 2A1; PP2A1; PPA2A1. Pack: vial of 1 μg. Cat No: NATE-0616.
Native Human Topoisomerase II α
Topoisomerase II α (TopoIIα) is a gene product with conserved catalytic activities and it promotes the progression of DNA damage. The α isoform is present in proliferating cells. Applications: Topoisomerase ii α has been used in a study to assess aging pr ocesses in the human brain. topoisomerase ii α has also been used in a study to investigate its activity in hiv-1 replication. Group: Enzymes. Synonyms: type II DNA topoisomerase; DNA-gyrase; deoxyribonucleate topoisomerase; deoxyribonucleic topoisomerase; topoisomerase; DNA topoisomerase II; DNA topoisomerase (ATP-hydrolysing); EC 5.99.1.3; Topoisomerase II α; TOPO II. Enzyme Commission Number: EC 5.99.1.3. CAS No. 37318-49-3. TOPO II. Mole weight: mol wt 170 kDa. Storage: -70°C. Form: liquid; Solution in 10 mM Tris-HCl, pH 7.1, 0.25 M NaCl, 1 mM EDTA, 0.5 mM PMSF, 1 mM 2-mercaptoethanol, 10% glycerol. Source: Human. type II DNA topoisomerase; DNA-gyrase; deoxyribonucleate topoisomerase; deoxyribonucleic topoisomerase; topoisomerase; DNA topoisomerase II; DNA topoisomerase (ATP-hydrolysing); EC 5.99.1.3; Topoisomerase II α; TOPO II. Cat No: NATE-0710.
Native Tritirachium album limber Proteinase K
Proteinase K (PROK) is a serine protease with broad specificity towards aliphatic, aromatic and other hydrophobic amino acids. PROK has a molecular weight of 27,000 daltons and is Ca2+ dependent. It is not inactivated by metal ion chelating agents such as EDTA, sulfhydryl reagents, PCMB, TLCK, or TPCK. It also retains activity in 0.5% SDS. It can be inhibited by PMSF or DFP. Applications: Useful for the proteolytic inactivation of nucleases during the isolation of dna and rna. removes endotoxins that bind to cationic proteins such as lysozyme and ribonuclease a. reported useful for the isolation of hepatic, yeast, and mung bean mit ochondria determination of enzyme l o...oteinase; Tritirachium album proteinase K; endopeptidase K; 39450-01-6; protease K. Enzyme Commission Number: EC 3.4.21.64. CAS No. 39450-01-6. Purity: Purified to remove DNase and RNase. Proteinase K. Mole weight: 27 kDa. Activity: Type I, > 20 units per mg dry weight; Type II, > 400 u/ml. Storage: Powder: 2-8°C; Liquid: -20°C. Form: Type I, powder; Type II, Liquid in 20mg/ml in 10mM Tris-HCl, 1mM calcium acetate, pH 7.5 containing 50% glycerol. Source: Tritirachium album limber. Proteinase K; EC 3.4.21.64; Tritirachium alkaline proteinase; Tritirachium album serine proteinase; Tritirachium album proteinase K; endopeptidase K; 39450-01-6; protease K. Cat No: NATE-0637.
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.
Trypsin from Human, Recombinant
Trypsin is a member of the serine protease family. Trypsin cleaves peptides on the C-terminal end of lysine and arginine amino acid residues. The optimum pH is pH 7.0 - 8.0. The enzyme is inhibited by serine protease inhibitors, e.g. PMSF, and by metal chelating agents, e.g., EDTA.Recombinant human trypsin is a genetically engineered protein expressed in E.coli and purified by high pressure liquid chromatography. There are no contaminating enzyme activities such as carboxypeptidase A and chymotrypsin. No protease inhibitors such as PMSF are contained in the preparation. Group: Enzymes. Synonyms: α-trypsin; β-trypsin; coc. Enzyme Commission Number: EC 3.4.21.4. CAS No. 9002-7-7. Purity: ≥ 95% by HPLC. Trypsin. Activity: >2500 USP u/mg protein. Storage: Recombinant human trypsin 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. It is stable within 24 months and above 90% activity remained after 10 times repeated freezing and thawing. Form: White or White-like lyophilized powder. Source: E. Coli. Species: Human. 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-1863.
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