endoproteinase lys-c Search Results


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  • 94
    New England Biolabs endoproteinase lys c
    Endoproteinase Lys C, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 94 stars, based on 7 article reviews
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    93
    Millipore endoproteinase lysc
    Endoproteinase Lysc, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Roche endoproteinase lys c lysc
    Endoproteinase Lys C Lysc, supplied by Roche, used in various techniques. Bioz Stars score: 85/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Promega endoproteinase lys c
    Western blot analysis of limited proteolytically digested CAP fragments with MAb CAP1. CAP was partially digested with proteinases, resulting in the production of peptides that had molecular masses of 16.2 and 18.7 kDa and that were reactive with MAb CAP1. Lane 1, CAP control; lane 2, alkaline protease; lane 3, <t>endoproteinase</t> Glu-C; lane 4, endoproteinase <t>Lys-C.</t>
    Endoproteinase Lys C, supplied by Promega, used in various techniques. Bioz Stars score: 93/100, based on 165 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 93 stars, based on 165 article reviews
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    92
    Roche endoproteinase lys c
    Partial proteolysis assays of Dm PBP bound to U1 or U6 PSEAs. Labeled DNA fragments that contained the U1 or U6 PSEAs (as indicated by a 1 or 6 above each individual lane) were incubated with Dm PBP followed by the addition of increasing amounts of an <t>endoproteinase</t> to partially digest the Dm PBP. The free and protein-bound fragments were then separated by native gel electrophoresis and the bands detected by autoradiography. ( A ) Lanes 3–8, 0.26, 1.3 or 6.4 µg/ml <t>Lys-C;</t> lanes 1, 2, 9 and 10, no proteinase. ( B ) Lanes 3–12, 0.037, 0.18, 0.91, 4.6 or 23 µg/ml Glu-C; lanes 1, 2, 13 and 14, no proteinase. ( C ) Lanes 3 and 5, 5.9 µg/ml Lys-C; lanes 4 and 6, 31 µg/ml Glu-C; lanes 1, 2, 7 and 8, no proteinase. ( D ) Lanes 3–12, 0.17, 0.34, 0.69, 1.4 or 2.8 µg/ml chymotrypsin; lanes 1 and 2, no proteinase. ( E ) Lanes 3–12, 0.10, 0.31, 0.92, 2.8 or 8.3 µg/ml Asp-N; lanes 1 and 2, no proteinase.
    Endoproteinase Lys C, supplied by Roche, used in various techniques. Bioz Stars score: 92/100, based on 635 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    FUJIFILM endoproteinase lys c
    Fractionation of an <t>Lys-C</t> digest of fibromodulin on Mono Q. Bovine fibromodulin, cleaved by the enzyme <t>endoproteinase</t> Lys-C, was applied onto a 1-ml Mono Q column and eluted with a salt gradient (0 to 1.5 m NaCl). The tyrosine sulfate-rich 10-kDa fragments
    Endoproteinase Lys C, supplied by FUJIFILM, used in various techniques. Bioz Stars score: 93/100, based on 556 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Boehringer Mannheim endoproteinase lys c
    The 190-kD polypeptide is equivalent to IQGAP1. The 190-kD polypeptide was purified in denatured form by preparative SDS-PAGE, electroeluted from the gel, and digested in solution with <t>endoproteinase</t> lys C. Four peptides were purified by HPLC and sequenced. Comparison of the peptide sequences with the GenBank/EMBL/DDBJ data bank indicated high identity of the bovine adrenal protein with human IQGAP1, a 1,658–amino acid residue protein that contains four potential calmodulin-binding IQ domains, and a region homologous to catalytic domains of GAPs ( 40 ). Sequences corresponding to peptides 1 and 4 are also found in human IQGAP2, a protein which is 62% identical to IQGAP1, but is reportedly abundant only in liver ( 8 ). A 9-mer peptide corresponding to the highlighted residues within peptide 3 was used as an immunogen for the production of an anti-IQGAP1 antibody.
    Endoproteinase Lys C, supplied by Boehringer Mannheim, used in various techniques. Bioz Stars score: 92/100, based on 127 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Thermo Fisher endoproteinase lys c
    The 190-kD polypeptide is equivalent to IQGAP1. The 190-kD polypeptide was purified in denatured form by preparative SDS-PAGE, electroeluted from the gel, and digested in solution with <t>endoproteinase</t> lys C. Four peptides were purified by HPLC and sequenced. Comparison of the peptide sequences with the GenBank/EMBL/DDBJ data bank indicated high identity of the bovine adrenal protein with human IQGAP1, a 1,658–amino acid residue protein that contains four potential calmodulin-binding IQ domains, and a region homologous to catalytic domains of GAPs ( 40 ). Sequences corresponding to peptides 1 and 4 are also found in human IQGAP2, a protein which is 62% identical to IQGAP1, but is reportedly abundant only in liver ( 8 ). A 9-mer peptide corresponding to the highlighted residues within peptide 3 was used as an immunogen for the production of an anti-IQGAP1 antibody.
    Endoproteinase Lys C, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 29 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Roche endoproteinase lys c endolys c
    The 190-kD polypeptide is equivalent to IQGAP1. The 190-kD polypeptide was purified in denatured form by preparative SDS-PAGE, electroeluted from the gel, and digested in solution with <t>endoproteinase</t> lys C. Four peptides were purified by HPLC and sequenced. Comparison of the peptide sequences with the GenBank/EMBL/DDBJ data bank indicated high identity of the bovine adrenal protein with human IQGAP1, a 1,658–amino acid residue protein that contains four potential calmodulin-binding IQ domains, and a region homologous to catalytic domains of GAPs ( 40 ). Sequences corresponding to peptides 1 and 4 are also found in human IQGAP2, a protein which is 62% identical to IQGAP1, but is reportedly abundant only in liver ( 8 ). A 9-mer peptide corresponding to the highlighted residues within peptide 3 was used as an immunogen for the production of an anti-IQGAP1 antibody.
    Endoproteinase Lys C Endolys C, supplied by Roche, used in various techniques. Bioz Stars score: 88/100, based on 36 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 88 stars, based on 36 article reviews
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    91
    Valiant endoproteinase lys c endolys c
    The 190-kD polypeptide is equivalent to IQGAP1. The 190-kD polypeptide was purified in denatured form by preparative SDS-PAGE, electroeluted from the gel, and digested in solution with <t>endoproteinase</t> lys C. Four peptides were purified by HPLC and sequenced. Comparison of the peptide sequences with the GenBank/EMBL/DDBJ data bank indicated high identity of the bovine adrenal protein with human IQGAP1, a 1,658–amino acid residue protein that contains four potential calmodulin-binding IQ domains, and a region homologous to catalytic domains of GAPs ( 40 ). Sequences corresponding to peptides 1 and 4 are also found in human IQGAP2, a protein which is 62% identical to IQGAP1, but is reportedly abundant only in liver ( 8 ). A 9-mer peptide corresponding to the highlighted residues within peptide 3 was used as an immunogen for the production of an anti-IQGAP1 antibody.
    Endoproteinase Lys C Endolys C, supplied by Valiant, used in various techniques. Bioz Stars score: 91/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 91 stars, based on 12 article reviews
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    93
    Promega sequencing grade endoproteinase lys c
    The 190-kD polypeptide is equivalent to IQGAP1. The 190-kD polypeptide was purified in denatured form by preparative SDS-PAGE, electroeluted from the gel, and digested in solution with <t>endoproteinase</t> lys C. Four peptides were purified by HPLC and sequenced. Comparison of the peptide sequences with the GenBank/EMBL/DDBJ data bank indicated high identity of the bovine adrenal protein with human IQGAP1, a 1,658–amino acid residue protein that contains four potential calmodulin-binding IQ domains, and a region homologous to catalytic domains of GAPs ( 40 ). Sequences corresponding to peptides 1 and 4 are also found in human IQGAP2, a protein which is 62% identical to IQGAP1, but is reportedly abundant only in liver ( 8 ). A 9-mer peptide corresponding to the highlighted residues within peptide 3 was used as an immunogen for the production of an anti-IQGAP1 antibody.
    Sequencing Grade Endoproteinase Lys C, supplied by Promega, used in various techniques. Bioz Stars score: 93/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Wilkens-Anderson endoproteinase lys c
    The 190-kD polypeptide is equivalent to IQGAP1. The 190-kD polypeptide was purified in denatured form by preparative SDS-PAGE, electroeluted from the gel, and digested in solution with <t>endoproteinase</t> lys C. Four peptides were purified by HPLC and sequenced. Comparison of the peptide sequences with the GenBank/EMBL/DDBJ data bank indicated high identity of the bovine adrenal protein with human IQGAP1, a 1,658–amino acid residue protein that contains four potential calmodulin-binding IQ domains, and a region homologous to catalytic domains of GAPs ( 40 ). Sequences corresponding to peptides 1 and 4 are also found in human IQGAP2, a protein which is 62% identical to IQGAP1, but is reportedly abundant only in liver ( 8 ). A 9-mer peptide corresponding to the highlighted residues within peptide 3 was used as an immunogen for the production of an anti-IQGAP1 antibody.
    Endoproteinase Lys C, supplied by Wilkens-Anderson, used in various techniques. Bioz Stars score: 92/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Merck & Co endoproteinase lys c
    Limited proteolytic digestion of IFNAR1. ( A ) Coomassie-stained SDS-PAGE and Western blot of fragmented human IFNAR1. Recombinant soluble IFNAR1 was treated with <t>endoproteinase</t> <t>Lys-C</t> for 15 min or 1h. The resulting fragments were separated as 8 bands (with 15 min treatment) labeled by arrows on the SDS-PAGE gel. Anifrolumab retained binding to 3 protein bands (1, 4, and 5). Western blot band number 4 after 15 min digestion appears as a so-called “ghost band” likely due to sample or detection antibody overloading as previously described. 42 A ∼38 kDa band observed in the untreated IFNAR1 lane of the western blot was not detectable in the SDS-PAGE gel. This band is likely a minor degradation product that pre-existed in the initial protein preparation and was digested into smaller fragments upon endoproteinase treatment. ( B ) Schematic representation of the positions of digested IFNAR1 fragments as determined by N-terminal Edman sequencing. Apparent molecular weight (as estimated by SDS-PAGE) of all protein fragments are in parentheses. The positive fragments which were recognized by anifrolumab are shown in solid lines, and the negative bands are shown in dotted lines. The smallest ∼12 kDa fragment recognized by anifrolumab was approximately mapped to SD3-4 after the cleavage of K 240 .
    Endoproteinase Lys C, supplied by Merck & Co, used in various techniques. Bioz Stars score: 92/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Alpha Laboratories endoproteinase lys c
    Limited proteolytic digestion of IFNAR1. ( A ) Coomassie-stained SDS-PAGE and Western blot of fragmented human IFNAR1. Recombinant soluble IFNAR1 was treated with <t>endoproteinase</t> <t>Lys-C</t> for 15 min or 1h. The resulting fragments were separated as 8 bands (with 15 min treatment) labeled by arrows on the SDS-PAGE gel. Anifrolumab retained binding to 3 protein bands (1, 4, and 5). Western blot band number 4 after 15 min digestion appears as a so-called “ghost band” likely due to sample or detection antibody overloading as previously described. 42 A ∼38 kDa band observed in the untreated IFNAR1 lane of the western blot was not detectable in the SDS-PAGE gel. This band is likely a minor degradation product that pre-existed in the initial protein preparation and was digested into smaller fragments upon endoproteinase treatment. ( B ) Schematic representation of the positions of digested IFNAR1 fragments as determined by N-terminal Edman sequencing. Apparent molecular weight (as estimated by SDS-PAGE) of all protein fragments are in parentheses. The positive fragments which were recognized by anifrolumab are shown in solid lines, and the negative bands are shown in dotted lines. The smallest ∼12 kDa fragment recognized by anifrolumab was approximately mapped to SD3-4 after the cleavage of K 240 .
    Endoproteinase Lys C, supplied by Alpha Laboratories, used in various techniques. Bioz Stars score: 92/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Roche sequencing grade endoproteinase lys c
    Limited proteolytic digestion of IFNAR1. ( A ) Coomassie-stained SDS-PAGE and Western blot of fragmented human IFNAR1. Recombinant soluble IFNAR1 was treated with <t>endoproteinase</t> <t>Lys-C</t> for 15 min or 1h. The resulting fragments were separated as 8 bands (with 15 min treatment) labeled by arrows on the SDS-PAGE gel. Anifrolumab retained binding to 3 protein bands (1, 4, and 5). Western blot band number 4 after 15 min digestion appears as a so-called “ghost band” likely due to sample or detection antibody overloading as previously described. 42 A ∼38 kDa band observed in the untreated IFNAR1 lane of the western blot was not detectable in the SDS-PAGE gel. This band is likely a minor degradation product that pre-existed in the initial protein preparation and was digested into smaller fragments upon endoproteinase treatment. ( B ) Schematic representation of the positions of digested IFNAR1 fragments as determined by N-terminal Edman sequencing. Apparent molecular weight (as estimated by SDS-PAGE) of all protein fragments are in parentheses. The positive fragments which were recognized by anifrolumab are shown in solid lines, and the negative bands are shown in dotted lines. The smallest ∼12 kDa fragment recognized by anifrolumab was approximately mapped to SD3-4 after the cleavage of K 240 .
    Sequencing Grade Endoproteinase Lys C, supplied by Roche, used in various techniques. Bioz Stars score: 88/100, based on 36 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    FUJIFILM sequencing grade endoproteinase lys c
    Limited proteolytic digestion of IFNAR1. ( A ) Coomassie-stained SDS-PAGE and Western blot of fragmented human IFNAR1. Recombinant soluble IFNAR1 was treated with <t>endoproteinase</t> <t>Lys-C</t> for 15 min or 1h. The resulting fragments were separated as 8 bands (with 15 min treatment) labeled by arrows on the SDS-PAGE gel. Anifrolumab retained binding to 3 protein bands (1, 4, and 5). Western blot band number 4 after 15 min digestion appears as a so-called “ghost band” likely due to sample or detection antibody overloading as previously described. 42 A ∼38 kDa band observed in the untreated IFNAR1 lane of the western blot was not detectable in the SDS-PAGE gel. This band is likely a minor degradation product that pre-existed in the initial protein preparation and was digested into smaller fragments upon endoproteinase treatment. ( B ) Schematic representation of the positions of digested IFNAR1 fragments as determined by N-terminal Edman sequencing. Apparent molecular weight (as estimated by SDS-PAGE) of all protein fragments are in parentheses. The positive fragments which were recognized by anifrolumab are shown in solid lines, and the negative bands are shown in dotted lines. The smallest ∼12 kDa fragment recognized by anifrolumab was approximately mapped to SD3-4 after the cleavage of K 240 .
    Sequencing Grade Endoproteinase Lys C, supplied by FUJIFILM, used in various techniques. Bioz Stars score: 90/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Western blot analysis of limited proteolytically digested CAP fragments with MAb CAP1. CAP was partially digested with proteinases, resulting in the production of peptides that had molecular masses of 16.2 and 18.7 kDa and that were reactive with MAb CAP1. Lane 1, CAP control; lane 2, alkaline protease; lane 3, endoproteinase Glu-C; lane 4, endoproteinase Lys-C.

    Journal: Clinical and Diagnostic Laboratory Immunology

    Article Title: Production, Characterization, and Epitope Mapping of a Monoclonal Antibody against Aspartic Proteinase ofCandida albicans

    doi:

    Figure Lengend Snippet: Western blot analysis of limited proteolytically digested CAP fragments with MAb CAP1. CAP was partially digested with proteinases, resulting in the production of peptides that had molecular masses of 16.2 and 18.7 kDa and that were reactive with MAb CAP1. Lane 1, CAP control; lane 2, alkaline protease; lane 3, endoproteinase Glu-C; lane 4, endoproteinase Lys-C.

    Article Snippet: For further analysis of potential epitopes, the limited proteolytic digestion of CAP with proteinases, alkaline protease, endoproteinase Glu-C, and endoproteinase Lys-C and immunoblotting with MAb CAP1 were performed.

    Techniques: Western Blot

    Partial proteolysis assays of Dm PBP bound to U1 or U6 PSEAs. Labeled DNA fragments that contained the U1 or U6 PSEAs (as indicated by a 1 or 6 above each individual lane) were incubated with Dm PBP followed by the addition of increasing amounts of an endoproteinase to partially digest the Dm PBP. The free and protein-bound fragments were then separated by native gel electrophoresis and the bands detected by autoradiography. ( A ) Lanes 3–8, 0.26, 1.3 or 6.4 µg/ml Lys-C; lanes 1, 2, 9 and 10, no proteinase. ( B ) Lanes 3–12, 0.037, 0.18, 0.91, 4.6 or 23 µg/ml Glu-C; lanes 1, 2, 13 and 14, no proteinase. ( C ) Lanes 3 and 5, 5.9 µg/ml Lys-C; lanes 4 and 6, 31 µg/ml Glu-C; lanes 1, 2, 7 and 8, no proteinase. ( D ) Lanes 3–12, 0.17, 0.34, 0.69, 1.4 or 2.8 µg/ml chymotrypsin; lanes 1 and 2, no proteinase. ( E ) Lanes 3–12, 0.10, 0.31, 0.92, 2.8 or 8.3 µg/ml Asp-N; lanes 1 and 2, no proteinase.

    Journal: Nucleic Acids Research

    Article Title: Similarities and differences in the conformation of protein-DNA complexes at the U1 and U6 snRNA gene promoters

    doi:

    Figure Lengend Snippet: Partial proteolysis assays of Dm PBP bound to U1 or U6 PSEAs. Labeled DNA fragments that contained the U1 or U6 PSEAs (as indicated by a 1 or 6 above each individual lane) were incubated with Dm PBP followed by the addition of increasing amounts of an endoproteinase to partially digest the Dm PBP. The free and protein-bound fragments were then separated by native gel electrophoresis and the bands detected by autoradiography. ( A ) Lanes 3–8, 0.26, 1.3 or 6.4 µg/ml Lys-C; lanes 1, 2, 9 and 10, no proteinase. ( B ) Lanes 3–12, 0.037, 0.18, 0.91, 4.6 or 23 µg/ml Glu-C; lanes 1, 2, 13 and 14, no proteinase. ( C ) Lanes 3 and 5, 5.9 µg/ml Lys-C; lanes 4 and 6, 31 µg/ml Glu-C; lanes 1, 2, 7 and 8, no proteinase. ( D ) Lanes 3–12, 0.17, 0.34, 0.69, 1.4 or 2.8 µg/ml chymotrypsin; lanes 1 and 2, no proteinase. ( E ) Lanes 3–12, 0.10, 0.31, 0.92, 2.8 or 8.3 µg/ml Asp-N; lanes 1 and 2, no proteinase.

    Article Snippet: After 30 min incubation, various amounts of endoproteinase Lys-C, Glu-C, chymotrypsin or Asp-N (sequencing grade; Roche Molecular Biochemicals, Indianapolis, IN) were added as described in the legend to Figure and incubation was continued for 10–30 min depending upon the proteinase.

    Techniques: Labeling, Incubation, Nucleic Acid Electrophoresis, Autoradiography

    Fractionation of an Lys-C digest of fibromodulin on Mono Q. Bovine fibromodulin, cleaved by the enzyme endoproteinase Lys-C, was applied onto a 1-ml Mono Q column and eluted with a salt gradient (0 to 1.5 m NaCl). The tyrosine sulfate-rich 10-kDa fragments

    Journal:

    Article Title: The Tyrosine Sulfate-rich Domains of the LRR Proteins Fibromodulin and Osteoadherin Bind Motifs of Basic Clusters in a Variety of Heparin-binding Proteins, Including Bioactive Factors *

    doi: 10.1074/jbc.M109.047076

    Figure Lengend Snippet: Fractionation of an Lys-C digest of fibromodulin on Mono Q. Bovine fibromodulin, cleaved by the enzyme endoproteinase Lys-C, was applied onto a 1-ml Mono Q column and eluted with a salt gradient (0 to 1.5 m NaCl). The tyrosine sulfate-rich 10-kDa fragments

    Article Snippet: This fragment was prepared by digestion of fibromodulin purified from bovine cartilage ( ) with endoproteinase Lys-C (Wako Chemicals GmbH, Germany) as described ( ).

    Techniques: Fractionation

    The 190-kD polypeptide is equivalent to IQGAP1. The 190-kD polypeptide was purified in denatured form by preparative SDS-PAGE, electroeluted from the gel, and digested in solution with endoproteinase lys C. Four peptides were purified by HPLC and sequenced. Comparison of the peptide sequences with the GenBank/EMBL/DDBJ data bank indicated high identity of the bovine adrenal protein with human IQGAP1, a 1,658–amino acid residue protein that contains four potential calmodulin-binding IQ domains, and a region homologous to catalytic domains of GAPs ( 40 ). Sequences corresponding to peptides 1 and 4 are also found in human IQGAP2, a protein which is 62% identical to IQGAP1, but is reportedly abundant only in liver ( 8 ). A 9-mer peptide corresponding to the highlighted residues within peptide 3 was used as an immunogen for the production of an anti-IQGAP1 antibody.

    Journal: The Journal of Cell Biology

    Article Title: IQGAP1, a Rac- and Cdc42-binding Protein, Directly Binds and Cross-links Microfilaments

    doi:

    Figure Lengend Snippet: The 190-kD polypeptide is equivalent to IQGAP1. The 190-kD polypeptide was purified in denatured form by preparative SDS-PAGE, electroeluted from the gel, and digested in solution with endoproteinase lys C. Four peptides were purified by HPLC and sequenced. Comparison of the peptide sequences with the GenBank/EMBL/DDBJ data bank indicated high identity of the bovine adrenal protein with human IQGAP1, a 1,658–amino acid residue protein that contains four potential calmodulin-binding IQ domains, and a region homologous to catalytic domains of GAPs ( 40 ). Sequences corresponding to peptides 1 and 4 are also found in human IQGAP2, a protein which is 62% identical to IQGAP1, but is reportedly abundant only in liver ( 8 ). A 9-mer peptide corresponding to the highlighted residues within peptide 3 was used as an immunogen for the production of an anti-IQGAP1 antibody.

    Article Snippet: After digestion with endoproteinase lys C ( Boehringer Mannheim Biochemicals , Indianapolis, IN), four resulting peptides were purified by HPLC.

    Techniques: Purification, SDS Page, High Performance Liquid Chromatography, Binding Assay

    Limited proteolytic digestion of IFNAR1. ( A ) Coomassie-stained SDS-PAGE and Western blot of fragmented human IFNAR1. Recombinant soluble IFNAR1 was treated with endoproteinase Lys-C for 15 min or 1h. The resulting fragments were separated as 8 bands (with 15 min treatment) labeled by arrows on the SDS-PAGE gel. Anifrolumab retained binding to 3 protein bands (1, 4, and 5). Western blot band number 4 after 15 min digestion appears as a so-called “ghost band” likely due to sample or detection antibody overloading as previously described. 42 A ∼38 kDa band observed in the untreated IFNAR1 lane of the western blot was not detectable in the SDS-PAGE gel. This band is likely a minor degradation product that pre-existed in the initial protein preparation and was digested into smaller fragments upon endoproteinase treatment. ( B ) Schematic representation of the positions of digested IFNAR1 fragments as determined by N-terminal Edman sequencing. Apparent molecular weight (as estimated by SDS-PAGE) of all protein fragments are in parentheses. The positive fragments which were recognized by anifrolumab are shown in solid lines, and the negative bands are shown in dotted lines. The smallest ∼12 kDa fragment recognized by anifrolumab was approximately mapped to SD3-4 after the cleavage of K 240 .

    Journal: mAbs

    Article Title: Molecular basis for antagonistic activity of anifrolumab, an anti-interferon–α receptor 1 antibody

    doi: 10.1080/19420862.2015.1007810

    Figure Lengend Snippet: Limited proteolytic digestion of IFNAR1. ( A ) Coomassie-stained SDS-PAGE and Western blot of fragmented human IFNAR1. Recombinant soluble IFNAR1 was treated with endoproteinase Lys-C for 15 min or 1h. The resulting fragments were separated as 8 bands (with 15 min treatment) labeled by arrows on the SDS-PAGE gel. Anifrolumab retained binding to 3 protein bands (1, 4, and 5). Western blot band number 4 after 15 min digestion appears as a so-called “ghost band” likely due to sample or detection antibody overloading as previously described. 42 A ∼38 kDa band observed in the untreated IFNAR1 lane of the western blot was not detectable in the SDS-PAGE gel. This band is likely a minor degradation product that pre-existed in the initial protein preparation and was digested into smaller fragments upon endoproteinase treatment. ( B ) Schematic representation of the positions of digested IFNAR1 fragments as determined by N-terminal Edman sequencing. Apparent molecular weight (as estimated by SDS-PAGE) of all protein fragments are in parentheses. The positive fragments which were recognized by anifrolumab are shown in solid lines, and the negative bands are shown in dotted lines. The smallest ∼12 kDa fragment recognized by anifrolumab was approximately mapped to SD3-4 after the cleavage of K 240 .

    Article Snippet: Proteolytic fragmentation of IFNAR1 Proteolytic fragmentation of rhIFNAR1 was performed by incubating 15 μg rhIFNAR1 with 1 μg endoproteinase Lys C for 15 min, 1 h, and 26 h at room temperature.

    Techniques: Staining, SDS Page, Western Blot, Recombinant, Labeling, Binding Assay, Sequencing, Molecular Weight