endopeptidase gluc  (New England Biolabs)


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    New England Biolabs endopeptidase gluc
    A) Schematic representation of fully reduced, disulfide and sulfonyl forms of HMGB1 and their biological functions. B) DNA beads bind to disulfide HMGB1 in feces from colitis mice. The redox state of HMGB1 captured by DNA beads B1 or B2 from feces of colitis mice was assessed by trypsin digestion followed by LC/MS analysis. Cell lysate from colorectal epithelial (Caco 2) cells was used as control for intracellular HMGB1. Diagnostic peptides showed with the presence of molecular weights 1496 and 550 (Da) indicates reduced cysteines 23 and 45 respectively, whereas the appearance of molecular weights of 1564 and 618 (Da) indicates forming of an intramolecular disulfide linkage between cysteines 23 and 45 (arrows). Cys 106 (MW = 2002) is in reduced form in all samples presented here. Data are representative from two separate experiments. C) DNA beads bind to hyper-acetylated form of HMGB1 in feces from colitis mice. Representative spetra of the LC-MS traces of the above samples digested <t>with</t> <t>endopeptidase</t> <t>GluC.</t> The presence of peptides with molecular weights 1624 and 1132 Da (arrows) indicates the hypo-acetylation of lysine residues in NLS1 and NLS2 regions respectively; whereas the presence of peptides of 1749 and 1342 Da (arrows) indicates hyper-acetylation of lysines within NLS1 and NLS2 regions. Data are representative from two separate experiments. D) B2 beads bind to redox modified HMGB1 proteins. Increasing amounts of various HMGB1 proteins (100 or 250 ng) were added to B2 beads (20 µl) and the mixture (50 µl total volume) was incubated at room temperature for two hours. The mixture was then centrifuged and HMGB1 bound to beads were revealed by western blotting with anti-HMGB1 antibodies. N = 3 experiments. E) B2 beads do not bind to TNF. To examine the specificity of DNA beads and HMGB1 binding, human TNF (200 ng) was incubated with increasing amounts of B2 beads (as indicated) at room temperature for two hours. After incubation, TNF remaining in the supernatants and bound to the beads were analyzed by western blot probed with anti-human TNF antibodies. Data are representative from three separate experiments. F) B2 beads do not bind to human histone H3. B2, B1 or control beads (5 µl) in each tube were incubated with increasing amounts of human histone H3 (0, 0.01, 0.1, 0.2, 0.5, 1, 2, 3 µg) for two hours at room temperature. The amount of histone H3 bound to DNA beads was analyzed by western blot using anti-histone H3 antibodies. Histone H3 protein was used as a positive control in western blot. Data are representative of 3 repeats.
    Endopeptidase Gluc, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Sequestering HMGB1 via DNA-Conjugated Beads Ameliorates Murine Colitis"

    Article Title: Sequestering HMGB1 via DNA-Conjugated Beads Ameliorates Murine Colitis

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0103992

    A) Schematic representation of fully reduced, disulfide and sulfonyl forms of HMGB1 and their biological functions. B) DNA beads bind to disulfide HMGB1 in feces from colitis mice. The redox state of HMGB1 captured by DNA beads B1 or B2 from feces of colitis mice was assessed by trypsin digestion followed by LC/MS analysis. Cell lysate from colorectal epithelial (Caco 2) cells was used as control for intracellular HMGB1. Diagnostic peptides showed with the presence of molecular weights 1496 and 550 (Da) indicates reduced cysteines 23 and 45 respectively, whereas the appearance of molecular weights of 1564 and 618 (Da) indicates forming of an intramolecular disulfide linkage between cysteines 23 and 45 (arrows). Cys 106 (MW = 2002) is in reduced form in all samples presented here. Data are representative from two separate experiments. C) DNA beads bind to hyper-acetylated form of HMGB1 in feces from colitis mice. Representative spetra of the LC-MS traces of the above samples digested with endopeptidase GluC. The presence of peptides with molecular weights 1624 and 1132 Da (arrows) indicates the hypo-acetylation of lysine residues in NLS1 and NLS2 regions respectively; whereas the presence of peptides of 1749 and 1342 Da (arrows) indicates hyper-acetylation of lysines within NLS1 and NLS2 regions. Data are representative from two separate experiments. D) B2 beads bind to redox modified HMGB1 proteins. Increasing amounts of various HMGB1 proteins (100 or 250 ng) were added to B2 beads (20 µl) and the mixture (50 µl total volume) was incubated at room temperature for two hours. The mixture was then centrifuged and HMGB1 bound to beads were revealed by western blotting with anti-HMGB1 antibodies. N = 3 experiments. E) B2 beads do not bind to TNF. To examine the specificity of DNA beads and HMGB1 binding, human TNF (200 ng) was incubated with increasing amounts of B2 beads (as indicated) at room temperature for two hours. After incubation, TNF remaining in the supernatants and bound to the beads were analyzed by western blot probed with anti-human TNF antibodies. Data are representative from three separate experiments. F) B2 beads do not bind to human histone H3. B2, B1 or control beads (5 µl) in each tube were incubated with increasing amounts of human histone H3 (0, 0.01, 0.1, 0.2, 0.5, 1, 2, 3 µg) for two hours at room temperature. The amount of histone H3 bound to DNA beads was analyzed by western blot using anti-histone H3 antibodies. Histone H3 protein was used as a positive control in western blot. Data are representative of 3 repeats.
    Figure Legend Snippet: A) Schematic representation of fully reduced, disulfide and sulfonyl forms of HMGB1 and their biological functions. B) DNA beads bind to disulfide HMGB1 in feces from colitis mice. The redox state of HMGB1 captured by DNA beads B1 or B2 from feces of colitis mice was assessed by trypsin digestion followed by LC/MS analysis. Cell lysate from colorectal epithelial (Caco 2) cells was used as control for intracellular HMGB1. Diagnostic peptides showed with the presence of molecular weights 1496 and 550 (Da) indicates reduced cysteines 23 and 45 respectively, whereas the appearance of molecular weights of 1564 and 618 (Da) indicates forming of an intramolecular disulfide linkage between cysteines 23 and 45 (arrows). Cys 106 (MW = 2002) is in reduced form in all samples presented here. Data are representative from two separate experiments. C) DNA beads bind to hyper-acetylated form of HMGB1 in feces from colitis mice. Representative spetra of the LC-MS traces of the above samples digested with endopeptidase GluC. The presence of peptides with molecular weights 1624 and 1132 Da (arrows) indicates the hypo-acetylation of lysine residues in NLS1 and NLS2 regions respectively; whereas the presence of peptides of 1749 and 1342 Da (arrows) indicates hyper-acetylation of lysines within NLS1 and NLS2 regions. Data are representative from two separate experiments. D) B2 beads bind to redox modified HMGB1 proteins. Increasing amounts of various HMGB1 proteins (100 or 250 ng) were added to B2 beads (20 µl) and the mixture (50 µl total volume) was incubated at room temperature for two hours. The mixture was then centrifuged and HMGB1 bound to beads were revealed by western blotting with anti-HMGB1 antibodies. N = 3 experiments. E) B2 beads do not bind to TNF. To examine the specificity of DNA beads and HMGB1 binding, human TNF (200 ng) was incubated with increasing amounts of B2 beads (as indicated) at room temperature for two hours. After incubation, TNF remaining in the supernatants and bound to the beads were analyzed by western blot probed with anti-human TNF antibodies. Data are representative from three separate experiments. F) B2 beads do not bind to human histone H3. B2, B1 or control beads (5 µl) in each tube were incubated with increasing amounts of human histone H3 (0, 0.01, 0.1, 0.2, 0.5, 1, 2, 3 µg) for two hours at room temperature. The amount of histone H3 bound to DNA beads was analyzed by western blot using anti-histone H3 antibodies. Histone H3 protein was used as a positive control in western blot. Data are representative of 3 repeats.

    Techniques Used: Liquid Chromatography with Mass Spectroscopy, Diagnostic Assay, Modification, Incubation, Western Blot, Binding Assay, Positive Control

    endopeptidase gluc  (New England Biolabs)


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    New England Biolabs endopeptidase gluc
    A) Schematic representation of fully reduced, disulfide and sulfonyl forms of HMGB1 and their biological functions. B) DNA beads bind to disulfide HMGB1 in feces from colitis mice. The redox state of HMGB1 captured by DNA beads B1 or B2 from feces of colitis mice was assessed by trypsin digestion followed by LC/MS analysis. Cell lysate from colorectal epithelial (Caco 2) cells was used as control for intracellular HMGB1. Diagnostic peptides showed with the presence of molecular weights 1496 and 550 (Da) indicates reduced cysteines 23 and 45 respectively, whereas the appearance of molecular weights of 1564 and 618 (Da) indicates forming of an intramolecular disulfide linkage between cysteines 23 and 45 (arrows). Cys 106 (MW = 2002) is in reduced form in all samples presented here. Data are representative from two separate experiments. C) DNA beads bind to hyper-acetylated form of HMGB1 in feces from colitis mice. Representative spetra of the LC-MS traces of the above samples digested <t>with</t> <t>endopeptidase</t> <t>GluC.</t> The presence of peptides with molecular weights 1624 and 1132 Da (arrows) indicates the hypo-acetylation of lysine residues in NLS1 and NLS2 regions respectively; whereas the presence of peptides of 1749 and 1342 Da (arrows) indicates hyper-acetylation of lysines within NLS1 and NLS2 regions. Data are representative from two separate experiments. D) B2 beads bind to redox modified HMGB1 proteins. Increasing amounts of various HMGB1 proteins (100 or 250 ng) were added to B2 beads (20 µl) and the mixture (50 µl total volume) was incubated at room temperature for two hours. The mixture was then centrifuged and HMGB1 bound to beads were revealed by western blotting with anti-HMGB1 antibodies. N = 3 experiments. E) B2 beads do not bind to TNF. To examine the specificity of DNA beads and HMGB1 binding, human TNF (200 ng) was incubated with increasing amounts of B2 beads (as indicated) at room temperature for two hours. After incubation, TNF remaining in the supernatants and bound to the beads were analyzed by western blot probed with anti-human TNF antibodies. Data are representative from three separate experiments. F) B2 beads do not bind to human histone H3. B2, B1 or control beads (5 µl) in each tube were incubated with increasing amounts of human histone H3 (0, 0.01, 0.1, 0.2, 0.5, 1, 2, 3 µg) for two hours at room temperature. The amount of histone H3 bound to DNA beads was analyzed by western blot using anti-histone H3 antibodies. Histone H3 protein was used as a positive control in western blot. Data are representative of 3 repeats.
    Endopeptidase Gluc, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Sequestering HMGB1 via DNA-Conjugated Beads Ameliorates Murine Colitis"

    Article Title: Sequestering HMGB1 via DNA-Conjugated Beads Ameliorates Murine Colitis

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0103992

    A) Schematic representation of fully reduced, disulfide and sulfonyl forms of HMGB1 and their biological functions. B) DNA beads bind to disulfide HMGB1 in feces from colitis mice. The redox state of HMGB1 captured by DNA beads B1 or B2 from feces of colitis mice was assessed by trypsin digestion followed by LC/MS analysis. Cell lysate from colorectal epithelial (Caco 2) cells was used as control for intracellular HMGB1. Diagnostic peptides showed with the presence of molecular weights 1496 and 550 (Da) indicates reduced cysteines 23 and 45 respectively, whereas the appearance of molecular weights of 1564 and 618 (Da) indicates forming of an intramolecular disulfide linkage between cysteines 23 and 45 (arrows). Cys 106 (MW = 2002) is in reduced form in all samples presented here. Data are representative from two separate experiments. C) DNA beads bind to hyper-acetylated form of HMGB1 in feces from colitis mice. Representative spetra of the LC-MS traces of the above samples digested with endopeptidase GluC. The presence of peptides with molecular weights 1624 and 1132 Da (arrows) indicates the hypo-acetylation of lysine residues in NLS1 and NLS2 regions respectively; whereas the presence of peptides of 1749 and 1342 Da (arrows) indicates hyper-acetylation of lysines within NLS1 and NLS2 regions. Data are representative from two separate experiments. D) B2 beads bind to redox modified HMGB1 proteins. Increasing amounts of various HMGB1 proteins (100 or 250 ng) were added to B2 beads (20 µl) and the mixture (50 µl total volume) was incubated at room temperature for two hours. The mixture was then centrifuged and HMGB1 bound to beads were revealed by western blotting with anti-HMGB1 antibodies. N = 3 experiments. E) B2 beads do not bind to TNF. To examine the specificity of DNA beads and HMGB1 binding, human TNF (200 ng) was incubated with increasing amounts of B2 beads (as indicated) at room temperature for two hours. After incubation, TNF remaining in the supernatants and bound to the beads were analyzed by western blot probed with anti-human TNF antibodies. Data are representative from three separate experiments. F) B2 beads do not bind to human histone H3. B2, B1 or control beads (5 µl) in each tube were incubated with increasing amounts of human histone H3 (0, 0.01, 0.1, 0.2, 0.5, 1, 2, 3 µg) for two hours at room temperature. The amount of histone H3 bound to DNA beads was analyzed by western blot using anti-histone H3 antibodies. Histone H3 protein was used as a positive control in western blot. Data are representative of 3 repeats.
    Figure Legend Snippet: A) Schematic representation of fully reduced, disulfide and sulfonyl forms of HMGB1 and their biological functions. B) DNA beads bind to disulfide HMGB1 in feces from colitis mice. The redox state of HMGB1 captured by DNA beads B1 or B2 from feces of colitis mice was assessed by trypsin digestion followed by LC/MS analysis. Cell lysate from colorectal epithelial (Caco 2) cells was used as control for intracellular HMGB1. Diagnostic peptides showed with the presence of molecular weights 1496 and 550 (Da) indicates reduced cysteines 23 and 45 respectively, whereas the appearance of molecular weights of 1564 and 618 (Da) indicates forming of an intramolecular disulfide linkage between cysteines 23 and 45 (arrows). Cys 106 (MW = 2002) is in reduced form in all samples presented here. Data are representative from two separate experiments. C) DNA beads bind to hyper-acetylated form of HMGB1 in feces from colitis mice. Representative spetra of the LC-MS traces of the above samples digested with endopeptidase GluC. The presence of peptides with molecular weights 1624 and 1132 Da (arrows) indicates the hypo-acetylation of lysine residues in NLS1 and NLS2 regions respectively; whereas the presence of peptides of 1749 and 1342 Da (arrows) indicates hyper-acetylation of lysines within NLS1 and NLS2 regions. Data are representative from two separate experiments. D) B2 beads bind to redox modified HMGB1 proteins. Increasing amounts of various HMGB1 proteins (100 or 250 ng) were added to B2 beads (20 µl) and the mixture (50 µl total volume) was incubated at room temperature for two hours. The mixture was then centrifuged and HMGB1 bound to beads were revealed by western blotting with anti-HMGB1 antibodies. N = 3 experiments. E) B2 beads do not bind to TNF. To examine the specificity of DNA beads and HMGB1 binding, human TNF (200 ng) was incubated with increasing amounts of B2 beads (as indicated) at room temperature for two hours. After incubation, TNF remaining in the supernatants and bound to the beads were analyzed by western blot probed with anti-human TNF antibodies. Data are representative from three separate experiments. F) B2 beads do not bind to human histone H3. B2, B1 or control beads (5 µl) in each tube were incubated with increasing amounts of human histone H3 (0, 0.01, 0.1, 0.2, 0.5, 1, 2, 3 µg) for two hours at room temperature. The amount of histone H3 bound to DNA beads was analyzed by western blot using anti-histone H3 antibodies. Histone H3 protein was used as a positive control in western blot. Data are representative of 3 repeats.

    Techniques Used: Liquid Chromatography with Mass Spectroscopy, Diagnostic Assay, Modification, Incubation, Western Blot, Binding Assay, Positive Control

    endoproteinase gluc digest  (New England Biolabs)


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    New England Biolabs endoproteinase gluc digest
    LC/MS/MS analysis of PAP-copurified proteins from bitter melon cotyledons.
    Endoproteinase Gluc Digest, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Characterization of a Soluble Phosphatidic Acid Phosphatase in Bitter Melon ( Momordica charantia )"

    Article Title: Characterization of a Soluble Phosphatidic Acid Phosphatase in Bitter Melon ( Momordica charantia )

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0106403

    LC/MS/MS analysis of PAP-copurified proteins from bitter melon cotyledons.
    Figure Legend Snippet: LC/MS/MS analysis of PAP-copurified proteins from bitter melon cotyledons.

    Techniques Used:

    endopeptidase gluc  (New England Biolabs)


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    New England Biolabs endopeptidase gluc
    Endopeptidase Gluc, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    endoproteinase gluc  (New England Biolabs)


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    New England Biolabs endoproteinase gluc
    Endoproteinase Gluc, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    endopeptidase gluc  (New England Biolabs)


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    New England Biolabs endopeptidase gluc
    ( A) Structure of the putative natural product kamptornamide ( 11 ) of the ksp cluster. The key structural features installed by posttranslational modifications are highlighted in colors that correspond to the respective genes in Fig. 2 A . ( B ) MS 2 fragmentation of the LahT fragment 11 . ( C ) EICs (left) and mass spectra (right) of the fully 13 C-labeled <t>GluC</t> fragments 3 and 9 from kspANRM coexpression using 13 C-Isogro broth. The mass shift between fully 13 C-labeled GluC fragments 3 and 9 is 194.20 Da. ( D ) EIC (left) and mass spectrum (right) of the released MeLan ring from triple digest of the fully <t>matured</t> <t>precursor</t> peptide KspANRM using the endopeptidase GluC and the exopeptidases aminopeptidase M and carboxypeptidase Y. The masses of 471.7642 Da ( m / z = 2) and 942.5188 Da ( m / z = 1) correspond to a nine-membered MeLan ring formed between Thr11 and Cys19 with an Asn20 extension. ( E ) Structure of the final natural product phaeornamide ( 12 ) of the pha cluster. The key structural features installed by posttranslational modifications are highlighted in colors that correspond to the respective genes in Fig. 2 D . ( F ) MS 2 fragmentation of the LahT fragment 12 . ( G ) EICs (left) and mass spectra (right) of the fully 13 C-labeled GluC fragments 8 and 10 from phaANRIM coexpression using 13 C-Isogro broth. The mass shift between fully 13 C-labeled GluC fragments 8 and 10 is 180.16 Da. ( H ) EIC (left) and mass spectrum (right) of the released MeLan ring from triple digest of the fully matured precursor peptide PhaANRIM using the endopeptidase GluC and the exopeptidases aminopeptidase M and carboxypeptidase Y. The mass of 518.2629 Da ( m / z = 1) corresponds to a four-membered MeLan ring formed between Cys4 and Thr7 with an Ile8 extension.
    Endopeptidase Gluc, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Ribosomally derived lipopeptides containing distinct fatty acyl moieties"

    Article Title: Ribosomally derived lipopeptides containing distinct fatty acyl moieties

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    doi: 10.1073/pnas.2113120119

    ( A) Structure of the putative natural product kamptornamide ( 11 ) of the ksp cluster. The key structural features installed by posttranslational modifications are highlighted in colors that correspond to the respective genes in Fig. 2 A . ( B ) MS 2 fragmentation of the LahT fragment 11 . ( C ) EICs (left) and mass spectra (right) of the fully 13 C-labeled GluC fragments 3 and 9 from kspANRM coexpression using 13 C-Isogro broth. The mass shift between fully 13 C-labeled GluC fragments 3 and 9 is 194.20 Da. ( D ) EIC (left) and mass spectrum (right) of the released MeLan ring from triple digest of the fully matured precursor peptide KspANRM using the endopeptidase GluC and the exopeptidases aminopeptidase M and carboxypeptidase Y. The masses of 471.7642 Da ( m / z = 2) and 942.5188 Da ( m / z = 1) correspond to a nine-membered MeLan ring formed between Thr11 and Cys19 with an Asn20 extension. ( E ) Structure of the final natural product phaeornamide ( 12 ) of the pha cluster. The key structural features installed by posttranslational modifications are highlighted in colors that correspond to the respective genes in Fig. 2 D . ( F ) MS 2 fragmentation of the LahT fragment 12 . ( G ) EICs (left) and mass spectra (right) of the fully 13 C-labeled GluC fragments 8 and 10 from phaANRIM coexpression using 13 C-Isogro broth. The mass shift between fully 13 C-labeled GluC fragments 8 and 10 is 180.16 Da. ( H ) EIC (left) and mass spectrum (right) of the released MeLan ring from triple digest of the fully matured precursor peptide PhaANRIM using the endopeptidase GluC and the exopeptidases aminopeptidase M and carboxypeptidase Y. The mass of 518.2629 Da ( m / z = 1) corresponds to a four-membered MeLan ring formed between Cys4 and Thr7 with an Ile8 extension.
    Figure Legend Snippet: ( A) Structure of the putative natural product kamptornamide ( 11 ) of the ksp cluster. The key structural features installed by posttranslational modifications are highlighted in colors that correspond to the respective genes in Fig. 2 A . ( B ) MS 2 fragmentation of the LahT fragment 11 . ( C ) EICs (left) and mass spectra (right) of the fully 13 C-labeled GluC fragments 3 and 9 from kspANRM coexpression using 13 C-Isogro broth. The mass shift between fully 13 C-labeled GluC fragments 3 and 9 is 194.20 Da. ( D ) EIC (left) and mass spectrum (right) of the released MeLan ring from triple digest of the fully matured precursor peptide KspANRM using the endopeptidase GluC and the exopeptidases aminopeptidase M and carboxypeptidase Y. The masses of 471.7642 Da ( m / z = 2) and 942.5188 Da ( m / z = 1) correspond to a nine-membered MeLan ring formed between Thr11 and Cys19 with an Asn20 extension. ( E ) Structure of the final natural product phaeornamide ( 12 ) of the pha cluster. The key structural features installed by posttranslational modifications are highlighted in colors that correspond to the respective genes in Fig. 2 D . ( F ) MS 2 fragmentation of the LahT fragment 12 . ( G ) EICs (left) and mass spectra (right) of the fully 13 C-labeled GluC fragments 8 and 10 from phaANRIM coexpression using 13 C-Isogro broth. The mass shift between fully 13 C-labeled GluC fragments 8 and 10 is 180.16 Da. ( H ) EIC (left) and mass spectrum (right) of the released MeLan ring from triple digest of the fully matured precursor peptide PhaANRIM using the endopeptidase GluC and the exopeptidases aminopeptidase M and carboxypeptidase Y. The mass of 518.2629 Da ( m / z = 1) corresponds to a four-membered MeLan ring formed between Cys4 and Thr7 with an Ile8 extension.

    Techniques Used: Labeling

    endoproteinase gluc  (New England Biolabs)


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    New England Biolabs endoproteinase gluc
    Endoproteinase Gluc, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    endoproteinase gluc  (New England Biolabs)


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    New England Biolabs endoproteinase gluc
    Endoproteinase Gluc, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    endoproteinase gluc reaction  (New England Biolabs)


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    New England Biolabs endoproteinase gluc reaction
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    endoproteinase gluc  (New England Biolabs)


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    New England Biolabs endoproteinase gluc
    Endoproteinase Gluc, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    glu c endoproteinase  (New England Biolabs)


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    Structured Review

    New England Biolabs glu c endoproteinase
    Glu C Endoproteinase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    glu c endoproteinase - by Bioz Stars, 2023-01
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    New England Biolabs endopeptidase gluc
    A) Schematic representation of fully reduced, disulfide and sulfonyl forms of HMGB1 and their biological functions. B) DNA beads bind to disulfide HMGB1 in feces from colitis mice. The redox state of HMGB1 captured by DNA beads B1 or B2 from feces of colitis mice was assessed by trypsin digestion followed by LC/MS analysis. Cell lysate from colorectal epithelial (Caco 2) cells was used as control for intracellular HMGB1. Diagnostic peptides showed with the presence of molecular weights 1496 and 550 (Da) indicates reduced cysteines 23 and 45 respectively, whereas the appearance of molecular weights of 1564 and 618 (Da) indicates forming of an intramolecular disulfide linkage between cysteines 23 and 45 (arrows). Cys 106 (MW = 2002) is in reduced form in all samples presented here. Data are representative from two separate experiments. C) DNA beads bind to hyper-acetylated form of HMGB1 in feces from colitis mice. Representative spetra of the LC-MS traces of the above samples digested <t>with</t> <t>endopeptidase</t> <t>GluC.</t> The presence of peptides with molecular weights 1624 and 1132 Da (arrows) indicates the hypo-acetylation of lysine residues in NLS1 and NLS2 regions respectively; whereas the presence of peptides of 1749 and 1342 Da (arrows) indicates hyper-acetylation of lysines within NLS1 and NLS2 regions. Data are representative from two separate experiments. D) B2 beads bind to redox modified HMGB1 proteins. Increasing amounts of various HMGB1 proteins (100 or 250 ng) were added to B2 beads (20 µl) and the mixture (50 µl total volume) was incubated at room temperature for two hours. The mixture was then centrifuged and HMGB1 bound to beads were revealed by western blotting with anti-HMGB1 antibodies. N = 3 experiments. E) B2 beads do not bind to TNF. To examine the specificity of DNA beads and HMGB1 binding, human TNF (200 ng) was incubated with increasing amounts of B2 beads (as indicated) at room temperature for two hours. After incubation, TNF remaining in the supernatants and bound to the beads were analyzed by western blot probed with anti-human TNF antibodies. Data are representative from three separate experiments. F) B2 beads do not bind to human histone H3. B2, B1 or control beads (5 µl) in each tube were incubated with increasing amounts of human histone H3 (0, 0.01, 0.1, 0.2, 0.5, 1, 2, 3 µg) for two hours at room temperature. The amount of histone H3 bound to DNA beads was analyzed by western blot using anti-histone H3 antibodies. Histone H3 protein was used as a positive control in western blot. Data are representative of 3 repeats.
    Endopeptidase Gluc, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/endopeptidase gluc/product/New England Biolabs
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    endopeptidase gluc - by Bioz Stars, 2023-01
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    95
    New England Biolabs endoproteinase gluc digest
    LC/MS/MS analysis of PAP-copurified proteins from bitter melon cotyledons.
    Endoproteinase Gluc Digest, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/endoproteinase gluc digest/product/New England Biolabs
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
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    95
    New England Biolabs endoproteinase gluc
    LC/MS/MS analysis of PAP-copurified proteins from bitter melon cotyledons.
    Endoproteinase Gluc, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/endoproteinase gluc/product/New England Biolabs
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    endoproteinase gluc - by Bioz Stars, 2023-01
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    New England Biolabs endoproteinase gluc reaction
    LC/MS/MS analysis of PAP-copurified proteins from bitter melon cotyledons.
    Endoproteinase Gluc Reaction, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/endoproteinase gluc reaction/product/New England Biolabs
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    95
    New England Biolabs glu c endoproteinase
    LC/MS/MS analysis of PAP-copurified proteins from bitter melon cotyledons.
    Glu C Endoproteinase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/glu c endoproteinase/product/New England Biolabs
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    glu c endoproteinase - by Bioz Stars, 2023-01
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    A) Schematic representation of fully reduced, disulfide and sulfonyl forms of HMGB1 and their biological functions. B) DNA beads bind to disulfide HMGB1 in feces from colitis mice. The redox state of HMGB1 captured by DNA beads B1 or B2 from feces of colitis mice was assessed by trypsin digestion followed by LC/MS analysis. Cell lysate from colorectal epithelial (Caco 2) cells was used as control for intracellular HMGB1. Diagnostic peptides showed with the presence of molecular weights 1496 and 550 (Da) indicates reduced cysteines 23 and 45 respectively, whereas the appearance of molecular weights of 1564 and 618 (Da) indicates forming of an intramolecular disulfide linkage between cysteines 23 and 45 (arrows). Cys 106 (MW = 2002) is in reduced form in all samples presented here. Data are representative from two separate experiments. C) DNA beads bind to hyper-acetylated form of HMGB1 in feces from colitis mice. Representative spetra of the LC-MS traces of the above samples digested with endopeptidase GluC. The presence of peptides with molecular weights 1624 and 1132 Da (arrows) indicates the hypo-acetylation of lysine residues in NLS1 and NLS2 regions respectively; whereas the presence of peptides of 1749 and 1342 Da (arrows) indicates hyper-acetylation of lysines within NLS1 and NLS2 regions. Data are representative from two separate experiments. D) B2 beads bind to redox modified HMGB1 proteins. Increasing amounts of various HMGB1 proteins (100 or 250 ng) were added to B2 beads (20 µl) and the mixture (50 µl total volume) was incubated at room temperature for two hours. The mixture was then centrifuged and HMGB1 bound to beads were revealed by western blotting with anti-HMGB1 antibodies. N = 3 experiments. E) B2 beads do not bind to TNF. To examine the specificity of DNA beads and HMGB1 binding, human TNF (200 ng) was incubated with increasing amounts of B2 beads (as indicated) at room temperature for two hours. After incubation, TNF remaining in the supernatants and bound to the beads were analyzed by western blot probed with anti-human TNF antibodies. Data are representative from three separate experiments. F) B2 beads do not bind to human histone H3. B2, B1 or control beads (5 µl) in each tube were incubated with increasing amounts of human histone H3 (0, 0.01, 0.1, 0.2, 0.5, 1, 2, 3 µg) for two hours at room temperature. The amount of histone H3 bound to DNA beads was analyzed by western blot using anti-histone H3 antibodies. Histone H3 protein was used as a positive control in western blot. Data are representative of 3 repeats.

    Journal: PLoS ONE

    Article Title: Sequestering HMGB1 via DNA-Conjugated Beads Ameliorates Murine Colitis

    doi: 10.1371/journal.pone.0103992

    Figure Lengend Snippet: A) Schematic representation of fully reduced, disulfide and sulfonyl forms of HMGB1 and their biological functions. B) DNA beads bind to disulfide HMGB1 in feces from colitis mice. The redox state of HMGB1 captured by DNA beads B1 or B2 from feces of colitis mice was assessed by trypsin digestion followed by LC/MS analysis. Cell lysate from colorectal epithelial (Caco 2) cells was used as control for intracellular HMGB1. Diagnostic peptides showed with the presence of molecular weights 1496 and 550 (Da) indicates reduced cysteines 23 and 45 respectively, whereas the appearance of molecular weights of 1564 and 618 (Da) indicates forming of an intramolecular disulfide linkage between cysteines 23 and 45 (arrows). Cys 106 (MW = 2002) is in reduced form in all samples presented here. Data are representative from two separate experiments. C) DNA beads bind to hyper-acetylated form of HMGB1 in feces from colitis mice. Representative spetra of the LC-MS traces of the above samples digested with endopeptidase GluC. The presence of peptides with molecular weights 1624 and 1132 Da (arrows) indicates the hypo-acetylation of lysine residues in NLS1 and NLS2 regions respectively; whereas the presence of peptides of 1749 and 1342 Da (arrows) indicates hyper-acetylation of lysines within NLS1 and NLS2 regions. Data are representative from two separate experiments. D) B2 beads bind to redox modified HMGB1 proteins. Increasing amounts of various HMGB1 proteins (100 or 250 ng) were added to B2 beads (20 µl) and the mixture (50 µl total volume) was incubated at room temperature for two hours. The mixture was then centrifuged and HMGB1 bound to beads were revealed by western blotting with anti-HMGB1 antibodies. N = 3 experiments. E) B2 beads do not bind to TNF. To examine the specificity of DNA beads and HMGB1 binding, human TNF (200 ng) was incubated with increasing amounts of B2 beads (as indicated) at room temperature for two hours. After incubation, TNF remaining in the supernatants and bound to the beads were analyzed by western blot probed with anti-human TNF antibodies. Data are representative from three separate experiments. F) B2 beads do not bind to human histone H3. B2, B1 or control beads (5 µl) in each tube were incubated with increasing amounts of human histone H3 (0, 0.01, 0.1, 0.2, 0.5, 1, 2, 3 µg) for two hours at room temperature. The amount of histone H3 bound to DNA beads was analyzed by western blot using anti-histone H3 antibodies. Histone H3 protein was used as a positive control in western blot. Data are representative of 3 repeats.

    Article Snippet: Samples were subjected to digestion by trypsin (Promega, Madison, WI) or endopeptidase GluC (New England Bio Labs., Ipswich, MA) according to the manufacturer's instructions.

    Techniques: Liquid Chromatography with Mass Spectroscopy, Diagnostic Assay, Modification, Incubation, Western Blot, Binding Assay, Positive Control

    LC/MS/MS analysis of PAP-copurified proteins from bitter melon cotyledons.

    Journal: PLoS ONE

    Article Title: Characterization of a Soluble Phosphatidic Acid Phosphatase in Bitter Melon ( Momordica charantia )

    doi: 10.1371/journal.pone.0106403

    Figure Lengend Snippet: LC/MS/MS analysis of PAP-copurified proteins from bitter melon cotyledons.

    Article Snippet: The endoproteinase GluC digest was prepared following the manufacturer’s instructions (New England Biolabs, Boston, MA).

    Techniques: