pierce streptavidin hrp  (Thermo Fisher)


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    Structured Review

    Thermo Fisher pierce streptavidin hrp
    Pierce Streptavidin Hrp, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pierce streptavidin hrp/product/Thermo Fisher
    Average 98 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    pierce streptavidin hrp - by Bioz Stars, 2020-03
    98/100 stars

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    Article Title: A Gel-Based Dual Antibody Capture and Detection Method for Assaying of Extracellular Cytokine Secretion
    Article Snippet: Streptavidin-hydrazide (Pierce Chemical, Rockford, IL; cat. no. 21120).

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  • 99
    Thermo Fisher streptavidin hrp
    Characterization of the BRWD2/PHIP CryptoTudor domain. ( A ) Diagram depicting the recombinant BRWD2/PHIP CryptoTudor–bromodomain (BRWD2/PHIP–Crypt–bromo) construct used for binding studies. N-terminal 10X-Histidine (red box) and C-terminal 1XFlag (green box) tags were included for protein purification. ( B ) Coomassie stained SDS-PAGE gel of in vitro chromatin capture experiment using the BRWD2/PHIP–Crypt–bromo module. (Lane 1 ) Input MNase-digested chromatin. (Lane 2 ) Chromatin subjected to anti-Flag immunoprecipitation without BRWD2/PHIP–Crypt–bromo. (Lane 3 ) Chromatin incubated with recombinant BRWD2/PHIP–Crypt–bromo and subjected to anti-Flag immunoprecipitation. ( C ) Quantitative MS analysis of histones captured in B . Bars indicate the fraction of total histone represented by each modification state in the input (gray) or Flag immunoprecipitation material (red). (Un) Unmodified; (me1) monomethylated; (me2) dimethylated; (me3) trimethylated; (Ac) acetylated. ( D ) Coomassie-stained SDS-PAGE gel of histone peptide pull-downs performed with human ( top ) or Drosophila ( bottom ) Crypt–bromo constructs. Recombinant protein was incubated with <t>streptavidin</t> beads alone (SA-beads) or the biotinylated histone peptides indicated. Ten percent of input and 20% of each pull-down sample were loaded. ( Bottom ) Eluted proteins were subjected to dot blotting using <t>streptavidin-HRP</t> (SA-HRP). ( E ) ITC experiments with human BRWD2–Crypt–bromo titrated with H3 unmodified ( left ), H3K4me1 ( middle ), and H3K4me3 ( right ) peptides. ( F ) Coomassie-stained SDS-PAGE gel of pull-downs performed with human BRWD2/PHIP–Crypt–bromo and a panel of histone peptides. Ten percent of input and 20% of each pull-down sample were loaded. Streptavidin-HRP dot blot loading control is shown below the gel image. ( G ) Coomassie-stained SDS-PAGE gel of a panel of histone peptide pull-downs performed with human BRWD2–Crypt–bromo ( top ), the isolated CryptoTudor domain ( middle ), or the isolated tandem bromodomains ( bottom ). Ten percent of input and 20% of each pull-down sample were loaded. Dot blot loading control is shown below each gel image. ( H ) Coomassie-stained gels of histone peptide pull-downs performed with point mutations of the BRWD2 CryptoTudor domain. Dot blot loading controls are shown below the gels. ( I ). Positions of residues predicted to be involved in methyl-lysine binding are highlighted in red.
    Streptavidin Hrp, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 162 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/streptavidin hrp/product/Thermo Fisher
    Average 99 stars, based on 162 article reviews
    Price from $9.99 to $1999.99
    streptavidin hrp - by Bioz Stars, 2020-03
    99/100 stars
      Buy from Supplier

    99
    Thermo Fisher peroxidase conjugated streptavidin
    Assay principle. Interferon beta (IFN-β) 1a is non-specifically bound to the surface allowing the presentation of multiple epitopes. A “bridge” is formed by the subsequent addition of a positive serum sample or rabbit antihuman IFN-β and biotin-labeled IFN-β 1a. The latter is detected by HRP-conjugated <t>streptavidin.</t>
    Peroxidase Conjugated Streptavidin, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 142 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/peroxidase conjugated streptavidin/product/Thermo Fisher
    Average 99 stars, based on 142 article reviews
    Price from $9.99 to $1999.99
    peroxidase conjugated streptavidin - by Bioz Stars, 2020-03
    99/100 stars
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    99
    Thermo Fisher streptavidin peroxidase
    The protein ELK-1 was ubiquitinated in the protoarrays by SCF1(FBXO25). A , experimental scheme of the ubiquitination in vitro reaction using the protoarray and SCF1 complexes. The ubiquitin mix (E1+E2 or E2DN+ATP+biotin-ubiquitin+ubiquitin) was added with the SCF1 complexes wild type or mutant in the ubiquitination reaction. Furthermore, the slides were incubated with <t>streptavidin-Alexa</t> Fluor 647 and scanned for visualization of the ubiquitinated proteins. B , protoarray slides ubiquitinated by SCF1(FBXO25) or SCF1(FBXO25-ΔF-box) highlighting a block with proteins differentially ubiquitinated by the wild type SCF1 complex. The protein ELK1, a member of ETS oncogene family, was differentially ubiquitinated by SCF1(FBXO25) ( n = 2). The other revealed spots were loading controls or ubiquitin-binding proteins spotted in the slides.
    Streptavidin Peroxidase, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/streptavidin peroxidase/product/Thermo Fisher
    Average 99 stars, based on 16 article reviews
    Price from $9.99 to $1999.99
    streptavidin peroxidase - by Bioz Stars, 2020-03
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    Image Search Results


    Characterization of the BRWD2/PHIP CryptoTudor domain. ( A ) Diagram depicting the recombinant BRWD2/PHIP CryptoTudor–bromodomain (BRWD2/PHIP–Crypt–bromo) construct used for binding studies. N-terminal 10X-Histidine (red box) and C-terminal 1XFlag (green box) tags were included for protein purification. ( B ) Coomassie stained SDS-PAGE gel of in vitro chromatin capture experiment using the BRWD2/PHIP–Crypt–bromo module. (Lane 1 ) Input MNase-digested chromatin. (Lane 2 ) Chromatin subjected to anti-Flag immunoprecipitation without BRWD2/PHIP–Crypt–bromo. (Lane 3 ) Chromatin incubated with recombinant BRWD2/PHIP–Crypt–bromo and subjected to anti-Flag immunoprecipitation. ( C ) Quantitative MS analysis of histones captured in B . Bars indicate the fraction of total histone represented by each modification state in the input (gray) or Flag immunoprecipitation material (red). (Un) Unmodified; (me1) monomethylated; (me2) dimethylated; (me3) trimethylated; (Ac) acetylated. ( D ) Coomassie-stained SDS-PAGE gel of histone peptide pull-downs performed with human ( top ) or Drosophila ( bottom ) Crypt–bromo constructs. Recombinant protein was incubated with streptavidin beads alone (SA-beads) or the biotinylated histone peptides indicated. Ten percent of input and 20% of each pull-down sample were loaded. ( Bottom ) Eluted proteins were subjected to dot blotting using streptavidin-HRP (SA-HRP). ( E ) ITC experiments with human BRWD2–Crypt–bromo titrated with H3 unmodified ( left ), H3K4me1 ( middle ), and H3K4me3 ( right ) peptides. ( F ) Coomassie-stained SDS-PAGE gel of pull-downs performed with human BRWD2/PHIP–Crypt–bromo and a panel of histone peptides. Ten percent of input and 20% of each pull-down sample were loaded. Streptavidin-HRP dot blot loading control is shown below the gel image. ( G ) Coomassie-stained SDS-PAGE gel of a panel of histone peptide pull-downs performed with human BRWD2–Crypt–bromo ( top ), the isolated CryptoTudor domain ( middle ), or the isolated tandem bromodomains ( bottom ). Ten percent of input and 20% of each pull-down sample were loaded. Dot blot loading control is shown below each gel image. ( H ) Coomassie-stained gels of histone peptide pull-downs performed with point mutations of the BRWD2 CryptoTudor domain. Dot blot loading controls are shown below the gels. ( I ). Positions of residues predicted to be involved in methyl-lysine binding are highlighted in red.

    Journal: Genes & Development

    Article Title: A cryptic Tudor domain links BRWD2/PHIP to COMPASS-mediated histone H3K4 methylation

    doi: 10.1101/gad.305201.117

    Figure Lengend Snippet: Characterization of the BRWD2/PHIP CryptoTudor domain. ( A ) Diagram depicting the recombinant BRWD2/PHIP CryptoTudor–bromodomain (BRWD2/PHIP–Crypt–bromo) construct used for binding studies. N-terminal 10X-Histidine (red box) and C-terminal 1XFlag (green box) tags were included for protein purification. ( B ) Coomassie stained SDS-PAGE gel of in vitro chromatin capture experiment using the BRWD2/PHIP–Crypt–bromo module. (Lane 1 ) Input MNase-digested chromatin. (Lane 2 ) Chromatin subjected to anti-Flag immunoprecipitation without BRWD2/PHIP–Crypt–bromo. (Lane 3 ) Chromatin incubated with recombinant BRWD2/PHIP–Crypt–bromo and subjected to anti-Flag immunoprecipitation. ( C ) Quantitative MS analysis of histones captured in B . Bars indicate the fraction of total histone represented by each modification state in the input (gray) or Flag immunoprecipitation material (red). (Un) Unmodified; (me1) monomethylated; (me2) dimethylated; (me3) trimethylated; (Ac) acetylated. ( D ) Coomassie-stained SDS-PAGE gel of histone peptide pull-downs performed with human ( top ) or Drosophila ( bottom ) Crypt–bromo constructs. Recombinant protein was incubated with streptavidin beads alone (SA-beads) or the biotinylated histone peptides indicated. Ten percent of input and 20% of each pull-down sample were loaded. ( Bottom ) Eluted proteins were subjected to dot blotting using streptavidin-HRP (SA-HRP). ( E ) ITC experiments with human BRWD2–Crypt–bromo titrated with H3 unmodified ( left ), H3K4me1 ( middle ), and H3K4me3 ( right ) peptides. ( F ) Coomassie-stained SDS-PAGE gel of pull-downs performed with human BRWD2/PHIP–Crypt–bromo and a panel of histone peptides. Ten percent of input and 20% of each pull-down sample were loaded. Streptavidin-HRP dot blot loading control is shown below the gel image. ( G ) Coomassie-stained SDS-PAGE gel of a panel of histone peptide pull-downs performed with human BRWD2–Crypt–bromo ( top ), the isolated CryptoTudor domain ( middle ), or the isolated tandem bromodomains ( bottom ). Ten percent of input and 20% of each pull-down sample were loaded. Dot blot loading control is shown below each gel image. ( H ) Coomassie-stained gels of histone peptide pull-downs performed with point mutations of the BRWD2 CryptoTudor domain. Dot blot loading controls are shown below the gels. ( I ). Positions of residues predicted to be involved in methyl-lysine binding are highlighted in red.

    Article Snippet: As a loading control, 0.25 µL of the eluted proteins was spotted onto a nitrocellulose membrane and detected using streptavidin-HRP (Thermo Scientific, no. 21130).

    Techniques: Recombinant, Construct, Binding Assay, Protein Purification, Staining, SDS Page, In Vitro, Immunoprecipitation, Incubation, Mass Spectrometry, Modification, Dot Blot, Isolation

    Assay principle. Interferon beta (IFN-β) 1a is non-specifically bound to the surface allowing the presentation of multiple epitopes. A “bridge” is formed by the subsequent addition of a positive serum sample or rabbit antihuman IFN-β and biotin-labeled IFN-β 1a. The latter is detected by HRP-conjugated streptavidin.

    Journal: Frontiers in Neurology

    Article Title: Development and Validation of an Enzyme-Linked Immunosorbent Assay for the Detection of Binding Anti-Drug Antibodies against Interferon Beta

    doi: 10.3389/fneur.2017.00305

    Figure Lengend Snippet: Assay principle. Interferon beta (IFN-β) 1a is non-specifically bound to the surface allowing the presentation of multiple epitopes. A “bridge” is formed by the subsequent addition of a positive serum sample or rabbit antihuman IFN-β and biotin-labeled IFN-β 1a. The latter is detected by HRP-conjugated streptavidin.

    Article Snippet: After washing, 100 µL/well of horseradish peroxidase-conjugated streptavidin (Strep-HRP, 1 in 10,000, Thermo Fisher Scientific Pierce Technology, USA) is added.

    Techniques: Labeling

    The protein ELK-1 was ubiquitinated in the protoarrays by SCF1(FBXO25). A , experimental scheme of the ubiquitination in vitro reaction using the protoarray and SCF1 complexes. The ubiquitin mix (E1+E2 or E2DN+ATP+biotin-ubiquitin+ubiquitin) was added with the SCF1 complexes wild type or mutant in the ubiquitination reaction. Furthermore, the slides were incubated with streptavidin-Alexa Fluor 647 and scanned for visualization of the ubiquitinated proteins. B , protoarray slides ubiquitinated by SCF1(FBXO25) or SCF1(FBXO25-ΔF-box) highlighting a block with proteins differentially ubiquitinated by the wild type SCF1 complex. The protein ELK1, a member of ETS oncogene family, was differentially ubiquitinated by SCF1(FBXO25) ( n = 2). The other revealed spots were loading controls or ubiquitin-binding proteins spotted in the slides.

    Journal: The Journal of Biological Chemistry

    Article Title: The F-box Protein FBXO25 Promotes the Proteasome-dependent Degradation of ELK-1 Protein *

    doi: 10.1074/jbc.M113.504308

    Figure Lengend Snippet: The protein ELK-1 was ubiquitinated in the protoarrays by SCF1(FBXO25). A , experimental scheme of the ubiquitination in vitro reaction using the protoarray and SCF1 complexes. The ubiquitin mix (E1+E2 or E2DN+ATP+biotin-ubiquitin+ubiquitin) was added with the SCF1 complexes wild type or mutant in the ubiquitination reaction. Furthermore, the slides were incubated with streptavidin-Alexa Fluor 647 and scanned for visualization of the ubiquitinated proteins. B , protoarray slides ubiquitinated by SCF1(FBXO25) or SCF1(FBXO25-ΔF-box) highlighting a block with proteins differentially ubiquitinated by the wild type SCF1 complex. The protein ELK1, a member of ETS oncogene family, was differentially ubiquitinated by SCF1(FBXO25) ( n = 2). The other revealed spots were loading controls or ubiquitin-binding proteins spotted in the slides.

    Article Snippet: The proteins were loaded in SDS-PAGE, and the Western blots were probed with anti-polyubiquitin FK2 antibodies (Millipore) and with streptavidin-peroxidase (Thermo Pierce).

    Techniques: In Vitro, Mutagenesis, Incubation, Blocking Assay, Binding Assay

    In vitro and in cellulo ubiquitination of ELK-1 by SCF1(FBXO25). A , in vitro ubiquitination of ELK-1 by SCF1(FBXO25). Two different concentrations of affinity-purified SCF1(FBXO25) or SCF1(FBXO25-ΔF-box) complexes in combination with purified ELK-1-FLAG-His 6 from HEK293T cells, Ub-mix (E1, E2, ubiquitin), biotin-ubiquitin, and ATP, were used in ubiquitination in vitro reactions as indicated. Polyubiquitinated ELK-1 by SCF1(FBXO25) and not by SCF1(FBXO25-ΔF-box) was visualized by Western blotting with streptavidin-HRP and anti-ubiquitin antibodies. B , in cellulo ubiquitination of ELK-1 by FBXO25. HEK293T cells were transfected with the indicated plasmids for 48 h. Six hours before lysis the cells were treated with epoxomicin, and the lysates were boiled to remove any noncovalently bound proteins. The supernatants were used in immunoprecipitation ( IP ) with polyclonal anti-ELK-1, and polyubiquitinated ELK-1 was visualized by Western blotting ( IB ) with anti-ubiquitin FK2 antibodies.

    Journal: The Journal of Biological Chemistry

    Article Title: The F-box Protein FBXO25 Promotes the Proteasome-dependent Degradation of ELK-1 Protein *

    doi: 10.1074/jbc.M113.504308

    Figure Lengend Snippet: In vitro and in cellulo ubiquitination of ELK-1 by SCF1(FBXO25). A , in vitro ubiquitination of ELK-1 by SCF1(FBXO25). Two different concentrations of affinity-purified SCF1(FBXO25) or SCF1(FBXO25-ΔF-box) complexes in combination with purified ELK-1-FLAG-His 6 from HEK293T cells, Ub-mix (E1, E2, ubiquitin), biotin-ubiquitin, and ATP, were used in ubiquitination in vitro reactions as indicated. Polyubiquitinated ELK-1 by SCF1(FBXO25) and not by SCF1(FBXO25-ΔF-box) was visualized by Western blotting with streptavidin-HRP and anti-ubiquitin antibodies. B , in cellulo ubiquitination of ELK-1 by FBXO25. HEK293T cells were transfected with the indicated plasmids for 48 h. Six hours before lysis the cells were treated with epoxomicin, and the lysates were boiled to remove any noncovalently bound proteins. The supernatants were used in immunoprecipitation ( IP ) with polyclonal anti-ELK-1, and polyubiquitinated ELK-1 was visualized by Western blotting ( IB ) with anti-ubiquitin FK2 antibodies.

    Article Snippet: The proteins were loaded in SDS-PAGE, and the Western blots were probed with anti-polyubiquitin FK2 antibodies (Millipore) and with streptavidin-peroxidase (Thermo Pierce).

    Techniques: In Vitro, Affinity Purification, Purification, Western Blot, Transfection, Lysis, Immunoprecipitation