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  • 99
    Thermo Fisher antiprotease halt protease inhibitor cocktail
    Peptidase activity assays of purified recombinant FliA(H)-hypervariable region and flagellar filaments from C. haemolyticum . a 12% SDS-PAGE of purified FliA(H)-hypervariable region (band “i”), electrophoresing close to that predicted for recombinant thioredoxin-tagged flagellin hypervariable region (50.14 kDa). b Amino acid occurrence heat map based on FliA(H)-hypervariable region protease cleaved peptide alignments of 391 cleavage sites identified in a tryptic E. coli K12 library. c IceLogos of FliA(H)-hypervariable region protease cleaved peptide specificity profiles showing percent differences compared to natural amino acid abundance, with significantly over-represented amino acids shown above the x -axis and under-represented residues below the x -axis. Amino acids that have not been identified are depicted in pink . d Fluorometric peptidase assays for FliA(H)-hypervariable region protease against three different peptidic substrates (ALG↓L, PLG↓L, PLG↓V) and + /– <t>EDTA</t> as indicated. e 10% SDS-PAGE of purified flagellar sheared filaments from C. haemolyticum . Band “ii” and “iii” were identified by mass spectrometry as FliA(H) (proteolytic flagellin) and the non-protease-containing structural flagellin (WP_039229459), respectively (Supplementary Fig. 7 ). f Amino acid occurrence heat map and g IceLogo based on cleaved peptide alignments of 269 cleavage sites identified in a tryptic E. coli K12 library using purified flagellar filaments. h Fluorometric peptidase assays for flagellar filaments using the ALG↓L peptide in three assay conditions including EDTA-free <t>HALT</t> protease inhibitors
    Antiprotease Halt Protease Inhibitor Cocktail, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 537 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher protease inhibitor cocktail
    Peptidase activity assays of purified recombinant FliA(H)-hypervariable region and flagellar filaments from C. haemolyticum . a 12% SDS-PAGE of purified FliA(H)-hypervariable region (band “i”), electrophoresing close to that predicted for recombinant thioredoxin-tagged flagellin hypervariable region (50.14 kDa). b Amino acid occurrence heat map based on FliA(H)-hypervariable region protease cleaved peptide alignments of 391 cleavage sites identified in a tryptic E. coli K12 library. c IceLogos of FliA(H)-hypervariable region protease cleaved peptide specificity profiles showing percent differences compared to natural amino acid abundance, with significantly over-represented amino acids shown above the x -axis and under-represented residues below the x -axis. Amino acids that have not been identified are depicted in pink . d Fluorometric peptidase assays for FliA(H)-hypervariable region protease against three different peptidic substrates (ALG↓L, PLG↓L, PLG↓V) and + /– <t>EDTA</t> as indicated. e 10% SDS-PAGE of purified flagellar sheared filaments from C. haemolyticum . Band “ii” and “iii” were identified by mass spectrometry as FliA(H) (proteolytic flagellin) and the non-protease-containing structural flagellin (WP_039229459), respectively (Supplementary Fig. 7 ). f Amino acid occurrence heat map and g IceLogo based on cleaved peptide alignments of 269 cleavage sites identified in a tryptic E. coli K12 library using purified flagellar filaments. h Fluorometric peptidase assays for flagellar filaments using the ALG↓L peptide in three assay conditions including EDTA-free <t>HALT</t> protease inhibitors
    Protease Inhibitor Cocktail, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 17919 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore protease inhibitor cocktail
    Peptidase activity assays of purified recombinant FliA(H)-hypervariable region and flagellar filaments from C. haemolyticum . a 12% SDS-PAGE of purified FliA(H)-hypervariable region (band “i”), electrophoresing close to that predicted for recombinant thioredoxin-tagged flagellin hypervariable region (50.14 kDa). b Amino acid occurrence heat map based on FliA(H)-hypervariable region protease cleaved peptide alignments of 391 cleavage sites identified in a tryptic E. coli K12 library. c IceLogos of FliA(H)-hypervariable region protease cleaved peptide specificity profiles showing percent differences compared to natural amino acid abundance, with significantly over-represented amino acids shown above the x -axis and under-represented residues below the x -axis. Amino acids that have not been identified are depicted in pink . d Fluorometric peptidase assays for FliA(H)-hypervariable region protease against three different peptidic substrates (ALG↓L, PLG↓L, PLG↓V) and + /– <t>EDTA</t> as indicated. e 10% SDS-PAGE of purified flagellar sheared filaments from C. haemolyticum . Band “ii” and “iii” were identified by mass spectrometry as FliA(H) (proteolytic flagellin) and the non-protease-containing structural flagellin (WP_039229459), respectively (Supplementary Fig. 7 ). f Amino acid occurrence heat map and g IceLogo based on cleaved peptide alignments of 269 cleavage sites identified in a tryptic E. coli K12 library using purified flagellar filaments. h Fluorometric peptidase assays for flagellar filaments using the ALG↓L peptide in three assay conditions including EDTA-free <t>HALT</t> protease inhibitors
    Protease Inhibitor Cocktail, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 134786 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Thermo Fisher 1x protease inhibitor cocktail
    Peptidase activity assays of purified recombinant FliA(H)-hypervariable region and flagellar filaments from C. haemolyticum . a 12% SDS-PAGE of purified FliA(H)-hypervariable region (band “i”), electrophoresing close to that predicted for recombinant thioredoxin-tagged flagellin hypervariable region (50.14 kDa). b Amino acid occurrence heat map based on FliA(H)-hypervariable region protease cleaved peptide alignments of 391 cleavage sites identified in a tryptic E. coli K12 library. c IceLogos of FliA(H)-hypervariable region protease cleaved peptide specificity profiles showing percent differences compared to natural amino acid abundance, with significantly over-represented amino acids shown above the x -axis and under-represented residues below the x -axis. Amino acids that have not been identified are depicted in pink . d Fluorometric peptidase assays for FliA(H)-hypervariable region protease against three different peptidic substrates (ALG↓L, PLG↓L, PLG↓V) and + /– <t>EDTA</t> as indicated. e 10% SDS-PAGE of purified flagellar sheared filaments from C. haemolyticum . Band “ii” and “iii” were identified by mass spectrometry as FliA(H) (proteolytic flagellin) and the non-protease-containing structural flagellin (WP_039229459), respectively (Supplementary Fig. 7 ). f Amino acid occurrence heat map and g IceLogo based on cleaved peptide alignments of 269 cleavage sites identified in a tryptic E. coli K12 library using purified flagellar filaments. h Fluorometric peptidase assays for flagellar filaments using the ALG↓L peptide in three assay conditions including EDTA-free <t>HALT</t> protease inhibitors
    1x Protease Inhibitor Cocktail, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 434 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher protease inhibitor cocktails
    Peptidase activity assays of purified recombinant FliA(H)-hypervariable region and flagellar filaments from C. haemolyticum . a 12% SDS-PAGE of purified FliA(H)-hypervariable region (band “i”), electrophoresing close to that predicted for recombinant thioredoxin-tagged flagellin hypervariable region (50.14 kDa). b Amino acid occurrence heat map based on FliA(H)-hypervariable region protease cleaved peptide alignments of 391 cleavage sites identified in a tryptic E. coli K12 library. c IceLogos of FliA(H)-hypervariable region protease cleaved peptide specificity profiles showing percent differences compared to natural amino acid abundance, with significantly over-represented amino acids shown above the x -axis and under-represented residues below the x -axis. Amino acids that have not been identified are depicted in pink . d Fluorometric peptidase assays for FliA(H)-hypervariable region protease against three different peptidic substrates (ALG↓L, PLG↓L, PLG↓V) and + /– <t>EDTA</t> as indicated. e 10% SDS-PAGE of purified flagellar sheared filaments from C. haemolyticum . Band “ii” and “iii” were identified by mass spectrometry as FliA(H) (proteolytic flagellin) and the non-protease-containing structural flagellin (WP_039229459), respectively (Supplementary Fig. 7 ). f Amino acid occurrence heat map and g IceLogo based on cleaved peptide alignments of 269 cleavage sites identified in a tryptic E. coli K12 library using purified flagellar filaments. h Fluorometric peptidase assays for flagellar filaments using the ALG↓L peptide in three assay conditions including EDTA-free <t>HALT</t> protease inhibitors
    Protease Inhibitor Cocktails, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1021 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Abcam protease inhibitor cocktail
    Peptidase activity assays of purified recombinant FliA(H)-hypervariable region and flagellar filaments from C. haemolyticum . a 12% SDS-PAGE of purified FliA(H)-hypervariable region (band “i”), electrophoresing close to that predicted for recombinant thioredoxin-tagged flagellin hypervariable region (50.14 kDa). b Amino acid occurrence heat map based on FliA(H)-hypervariable region protease cleaved peptide alignments of 391 cleavage sites identified in a tryptic E. coli K12 library. c IceLogos of FliA(H)-hypervariable region protease cleaved peptide specificity profiles showing percent differences compared to natural amino acid abundance, with significantly over-represented amino acids shown above the x -axis and under-represented residues below the x -axis. Amino acids that have not been identified are depicted in pink . d Fluorometric peptidase assays for FliA(H)-hypervariable region protease against three different peptidic substrates (ALG↓L, PLG↓L, PLG↓V) and + /– <t>EDTA</t> as indicated. e 10% SDS-PAGE of purified flagellar sheared filaments from C. haemolyticum . Band “ii” and “iii” were identified by mass spectrometry as FliA(H) (proteolytic flagellin) and the non-protease-containing structural flagellin (WP_039229459), respectively (Supplementary Fig. 7 ). f Amino acid occurrence heat map and g IceLogo based on cleaved peptide alignments of 269 cleavage sites identified in a tryptic E. coli K12 library using purified flagellar filaments. h Fluorometric peptidase assays for flagellar filaments using the ALG↓L peptide in three assay conditions including EDTA-free <t>HALT</t> protease inhibitors
    Protease Inhibitor Cocktail, supplied by Abcam, used in various techniques. Bioz Stars score: 93/100, based on 501 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Promega protease inhibitor cocktail
    Peptidase activity assays of purified recombinant FliA(H)-hypervariable region and flagellar filaments from C. haemolyticum . a 12% SDS-PAGE of purified FliA(H)-hypervariable region (band “i”), electrophoresing close to that predicted for recombinant thioredoxin-tagged flagellin hypervariable region (50.14 kDa). b Amino acid occurrence heat map based on FliA(H)-hypervariable region protease cleaved peptide alignments of 391 cleavage sites identified in a tryptic E. coli K12 library. c IceLogos of FliA(H)-hypervariable region protease cleaved peptide specificity profiles showing percent differences compared to natural amino acid abundance, with significantly over-represented amino acids shown above the x -axis and under-represented residues below the x -axis. Amino acids that have not been identified are depicted in pink . d Fluorometric peptidase assays for FliA(H)-hypervariable region protease against three different peptidic substrates (ALG↓L, PLG↓L, PLG↓V) and + /– <t>EDTA</t> as indicated. e 10% SDS-PAGE of purified flagellar sheared filaments from C. haemolyticum . Band “ii” and “iii” were identified by mass spectrometry as FliA(H) (proteolytic flagellin) and the non-protease-containing structural flagellin (WP_039229459), respectively (Supplementary Fig. 7 ). f Amino acid occurrence heat map and g IceLogo based on cleaved peptide alignments of 269 cleavage sites identified in a tryptic E. coli K12 library using purified flagellar filaments. h Fluorometric peptidase assays for flagellar filaments using the ALG↓L peptide in three assay conditions including EDTA-free <t>HALT</t> protease inhibitors
    Protease Inhibitor Cocktail, supplied by Promega, used in various techniques. Bioz Stars score: 99/100, based on 954 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    98
    Thermo Fisher protease inhibitors
    Peptidase activity assays of purified recombinant FliA(H)-hypervariable region and flagellar filaments from C. haemolyticum . a 12% SDS-PAGE of purified FliA(H)-hypervariable region (band “i”), electrophoresing close to that predicted for recombinant thioredoxin-tagged flagellin hypervariable region (50.14 kDa). b Amino acid occurrence heat map based on FliA(H)-hypervariable region protease cleaved peptide alignments of 391 cleavage sites identified in a tryptic E. coli K12 library. c IceLogos of FliA(H)-hypervariable region protease cleaved peptide specificity profiles showing percent differences compared to natural amino acid abundance, with significantly over-represented amino acids shown above the x -axis and under-represented residues below the x -axis. Amino acids that have not been identified are depicted in pink . d Fluorometric peptidase assays for FliA(H)-hypervariable region protease against three different peptidic substrates (ALG↓L, PLG↓L, PLG↓V) and + /– <t>EDTA</t> as indicated. e 10% SDS-PAGE of purified flagellar sheared filaments from C. haemolyticum . Band “ii” and “iii” were identified by mass spectrometry as FliA(H) (proteolytic flagellin) and the non-protease-containing structural flagellin (WP_039229459), respectively (Supplementary Fig. 7 ). f Amino acid occurrence heat map and g IceLogo based on cleaved peptide alignments of 269 cleavage sites identified in a tryptic E. coli K12 library using purified flagellar filaments. h Fluorometric peptidase assays for flagellar filaments using the ALG↓L peptide in three assay conditions including EDTA-free <t>HALT</t> protease inhibitors
    Protease Inhibitors, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 98/100, based on 10647 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Peptidase activity assays of purified recombinant FliA(H)-hypervariable region and flagellar filaments from C. haemolyticum . a 12% SDS-PAGE of purified FliA(H)-hypervariable region (band “i”), electrophoresing close to that predicted for recombinant thioredoxin-tagged flagellin hypervariable region (50.14 kDa). b Amino acid occurrence heat map based on FliA(H)-hypervariable region protease cleaved peptide alignments of 391 cleavage sites identified in a tryptic E. coli K12 library. c IceLogos of FliA(H)-hypervariable region protease cleaved peptide specificity profiles showing percent differences compared to natural amino acid abundance, with significantly over-represented amino acids shown above the x -axis and under-represented residues below the x -axis. Amino acids that have not been identified are depicted in pink . d Fluorometric peptidase assays for FliA(H)-hypervariable region protease against three different peptidic substrates (ALG↓L, PLG↓L, PLG↓V) and + /– EDTA as indicated. e 10% SDS-PAGE of purified flagellar sheared filaments from C. haemolyticum . Band “ii” and “iii” were identified by mass spectrometry as FliA(H) (proteolytic flagellin) and the non-protease-containing structural flagellin (WP_039229459), respectively (Supplementary Fig. 7 ). f Amino acid occurrence heat map and g IceLogo based on cleaved peptide alignments of 269 cleavage sites identified in a tryptic E. coli K12 library using purified flagellar filaments. h Fluorometric peptidase assays for flagellar filaments using the ALG↓L peptide in three assay conditions including EDTA-free HALT protease inhibitors

    Journal: Nature Communications

    Article Title: Discovery of a proteolytic flagellin family in diverse bacterial phyla that assembles enzymatically active flagella

    doi: 10.1038/s41467-017-00599-0

    Figure Lengend Snippet: Peptidase activity assays of purified recombinant FliA(H)-hypervariable region and flagellar filaments from C. haemolyticum . a 12% SDS-PAGE of purified FliA(H)-hypervariable region (band “i”), electrophoresing close to that predicted for recombinant thioredoxin-tagged flagellin hypervariable region (50.14 kDa). b Amino acid occurrence heat map based on FliA(H)-hypervariable region protease cleaved peptide alignments of 391 cleavage sites identified in a tryptic E. coli K12 library. c IceLogos of FliA(H)-hypervariable region protease cleaved peptide specificity profiles showing percent differences compared to natural amino acid abundance, with significantly over-represented amino acids shown above the x -axis and under-represented residues below the x -axis. Amino acids that have not been identified are depicted in pink . d Fluorometric peptidase assays for FliA(H)-hypervariable region protease against three different peptidic substrates (ALG↓L, PLG↓L, PLG↓V) and + /– EDTA as indicated. e 10% SDS-PAGE of purified flagellar sheared filaments from C. haemolyticum . Band “ii” and “iii” were identified by mass spectrometry as FliA(H) (proteolytic flagellin) and the non-protease-containing structural flagellin (WP_039229459), respectively (Supplementary Fig. 7 ). f Amino acid occurrence heat map and g IceLogo based on cleaved peptide alignments of 269 cleavage sites identified in a tryptic E. coli K12 library using purified flagellar filaments. h Fluorometric peptidase assays for flagellar filaments using the ALG↓L peptide in three assay conditions including EDTA-free HALT protease inhibitors

    Article Snippet: Purified recombinant FliA(H)-hypervariable region protease was incubated at a final concentration of 0.5 µM with 10 µM QF-peptide substrate in 100 µl of 150 mM NaCl, 10 mM CaCl2 , 50 mM HEPES, pH 7.5, in the presence of HALT protease inhibitor cocktail (Life Technologies) plus/minus 20 mM EDTA at 37 °C.

    Techniques: Activity Assay, Purification, Recombinant, SDS Page, Mass Spectrometry