streptavidin horse radish peroxidase hrp  (Thermo Fisher)


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    Structured Review

    Thermo Fisher streptavidin horse radish peroxidase hrp
    Analysis of p53 binding to head-to-tail response element in cyclin B promoter using electrophoretic mobility shift assays. A , MCF10A, MCF10A/OD, and MCF10A/Δp53 cell lines were incubated with 10 ng/ml SN38 for 24 hours (+SN) or were left untreated (–SN). Binding reactions were prepared by incubating nuclear extracts or recombinant p53 with a biotin-labeled probe corresponding to the head-to-tail response element in the cyclin B promoter, in the presence (+) or absence (−) of a 200-fold molar excess of specific DNA (unlabeled probe). All binding reactions were carried out in the presence of a 100-fold molar excess of unlabeled non-specific DNA. Complexes were separated on 4% native polyacrylamide gel electrophoresis, transferred to positively charged nylon membrane, and visualized using a <t>streptavidin-horse</t> radish peroxidase conjugate. B , A parallel gel was transferred to nitrocellulose membrane and immunoblotted with p53-specific antibodies.
    Streptavidin Horse Radish Peroxidase Hrp, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 88/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/streptavidin horse radish peroxidase hrp/product/Thermo Fisher
    Average 88 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    streptavidin horse radish peroxidase hrp - by Bioz Stars, 2020-07
    88/100 stars

    Images

    1) Product Images from "p53 Dimers Associate with a Head-to-Tail Response Element to Repress Cyclin B Transcription"

    Article Title: p53 Dimers Associate with a Head-to-Tail Response Element to Repress Cyclin B Transcription

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0042615

    Analysis of p53 binding to head-to-tail response element in cyclin B promoter using electrophoretic mobility shift assays. A , MCF10A, MCF10A/OD, and MCF10A/Δp53 cell lines were incubated with 10 ng/ml SN38 for 24 hours (+SN) or were left untreated (–SN). Binding reactions were prepared by incubating nuclear extracts or recombinant p53 with a biotin-labeled probe corresponding to the head-to-tail response element in the cyclin B promoter, in the presence (+) or absence (−) of a 200-fold molar excess of specific DNA (unlabeled probe). All binding reactions were carried out in the presence of a 100-fold molar excess of unlabeled non-specific DNA. Complexes were separated on 4% native polyacrylamide gel electrophoresis, transferred to positively charged nylon membrane, and visualized using a streptavidin-horse radish peroxidase conjugate. B , A parallel gel was transferred to nitrocellulose membrane and immunoblotted with p53-specific antibodies.
    Figure Legend Snippet: Analysis of p53 binding to head-to-tail response element in cyclin B promoter using electrophoretic mobility shift assays. A , MCF10A, MCF10A/OD, and MCF10A/Δp53 cell lines were incubated with 10 ng/ml SN38 for 24 hours (+SN) or were left untreated (–SN). Binding reactions were prepared by incubating nuclear extracts or recombinant p53 with a biotin-labeled probe corresponding to the head-to-tail response element in the cyclin B promoter, in the presence (+) or absence (−) of a 200-fold molar excess of specific DNA (unlabeled probe). All binding reactions were carried out in the presence of a 100-fold molar excess of unlabeled non-specific DNA. Complexes were separated on 4% native polyacrylamide gel electrophoresis, transferred to positively charged nylon membrane, and visualized using a streptavidin-horse radish peroxidase conjugate. B , A parallel gel was transferred to nitrocellulose membrane and immunoblotted with p53-specific antibodies.

    Techniques Used: Binding Assay, Electrophoretic Mobility Shift Assay, Incubation, Recombinant, Labeling, Polyacrylamide Gel Electrophoresis

    2) Product Images from "A New Sandwich ELISA for Quantification of Thymidine Kinase 1 Protein Levels in Sera from Dogs with Different Malignancies Can Aid in Disease Management"

    Article Title: A New Sandwich ELISA for Quantification of Thymidine Kinase 1 Protein Levels in Sera from Dogs with Different Malignancies Can Aid in Disease Management

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0137871

    ELISA procedure, effect of buffer during pre-incubation and standard curve. (A) Schematic presentation of the sandwich ELISA. The five steps are: (1) coating of microplate wells with polyclonal dog anti-TK1 antibody (C215-231), (2) binding of TK1 in serum to coated antibody, (3) attachment of the biotinylated MAB 528–2 to TK1 in serum, (4) detection of biotin by streptavidin-HRP, and finally (5) enzymatic activity monitored by addition of 3,3 _, 5,5 _-Tetramethylbenzidine (TMB) chromogenic substrate. (B) Absorbance values of healthy, lymphoma and mammary tumor sera on TK1-ELISA during different pre-incubation time points (0, 30 and 60 min). The error bars represents the SEM of the mean values. (C) Comparison of the absorbance values of the serum samples from 0 min and 60 min. The error bars represent SEM of the mean. ns = no significant difference, *** p
    Figure Legend Snippet: ELISA procedure, effect of buffer during pre-incubation and standard curve. (A) Schematic presentation of the sandwich ELISA. The five steps are: (1) coating of microplate wells with polyclonal dog anti-TK1 antibody (C215-231), (2) binding of TK1 in serum to coated antibody, (3) attachment of the biotinylated MAB 528–2 to TK1 in serum, (4) detection of biotin by streptavidin-HRP, and finally (5) enzymatic activity monitored by addition of 3,3 _, 5,5 _-Tetramethylbenzidine (TMB) chromogenic substrate. (B) Absorbance values of healthy, lymphoma and mammary tumor sera on TK1-ELISA during different pre-incubation time points (0, 30 and 60 min). The error bars represents the SEM of the mean values. (C) Comparison of the absorbance values of the serum samples from 0 min and 60 min. The error bars represent SEM of the mean. ns = no significant difference, *** p

    Techniques Used: Enzyme-linked Immunosorbent Assay, Incubation, Sandwich ELISA, Binding Assay, Activity Assay

    Related Articles

    Incubation:

    Article Title: A New Sandwich ELISA for Quantification of Thymidine Kinase 1 Protein Levels in Sera from Dogs with Different Malignancies Can Aid in Disease Management
    Article Snippet: .. The plates were washed as above and streptavidin-horse radish peroxidase (HRP) diluted 1: 32,000 in wash buffer was added, and incubated for 1 h. After the final wash, 3, 3 _, 5, 5 _-Tetramethylbenzidine (TMB) (Thermo Fisher Scientific) was added and allowed to develop colour for 15 min, and then quenched with 2N H2 SO4 . .. The O.D values in wells were read at 450 nM in an Infinite M200 Micro plate reader (Tecan, Mannedörf, Germany).

    Article Title: Characterization of a novel glycosylated glutathione transferase of Onchocerca ochengi, closest relative of the human river blindness parasite
    Article Snippet: .. Following further washes, membranes were then incubated in streptavidin-horse radish peroxidase (HRP) (ThermoFisher) at a 1: 100 000 dilution for 1 hour at room temperature (20–23 °C). .. Membranes were washed and then incubated with SuperSignal West Dura (Pierce, UK) peroxidase buffer and luminol:enhancer solution at a 1:1 ratio, and developed by chemiluminescence, which continued for up to 5 h.

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    Thermo Fisher horse radish peroxidase hrp
    Cell surface localization of ANT1 and ANT2. A – D , After cell surface biotinylation of live cerebellar neurons, biotinylated cell surface proteins were isolated using <t>streptavidin-coupled</t> beads ( A–C ), and ANT1 and ANT2 were immunoprecipitated using ANT1- and ANT2-specific antibodies ( D ). Cell lysates (input), isolated biotinylated proteins (surface) and the ANT1 and ANT2 immunoprecipitates (IP) were subjected to Western blot (WB) analysis using either ANT1-specific (ANT1; A ), ANT2-specific (ANT2; B ), or tubulin ( C ) antibodies or using <t>HRP-conjugated</t> streptavidin ( D ). The 60 kDa ANT protein seen after short time exposure (top) and the 32 kDa ANT protein seen after long time exposure (bottom) are indicated.
    Horse Radish Peroxidase Hrp, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 28 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/horse radish peroxidase hrp/product/Thermo Fisher
    Average 92 stars, based on 28 article reviews
    Price from $9.99 to $1999.99
    horse radish peroxidase hrp - by Bioz Stars, 2020-07
    92/100 stars
      Buy from Supplier

    88
    Thermo Fisher streptavidin horse radish peroxidase hrp
    Analysis of p53 binding to head-to-tail response element in cyclin B promoter using electrophoretic mobility shift assays. A , MCF10A, MCF10A/OD, and MCF10A/Δp53 cell lines were incubated with 10 ng/ml SN38 for 24 hours (+SN) or were left untreated (–SN). Binding reactions were prepared by incubating nuclear extracts or recombinant p53 with a biotin-labeled probe corresponding to the head-to-tail response element in the cyclin B promoter, in the presence (+) or absence (−) of a 200-fold molar excess of specific DNA (unlabeled probe). All binding reactions were carried out in the presence of a 100-fold molar excess of unlabeled non-specific DNA. Complexes were separated on 4% native polyacrylamide gel electrophoresis, transferred to positively charged nylon membrane, and visualized using a <t>streptavidin-horse</t> radish peroxidase conjugate. B , A parallel gel was transferred to nitrocellulose membrane and immunoblotted with p53-specific antibodies.
    Streptavidin Horse Radish Peroxidase Hrp, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 88/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/streptavidin horse radish peroxidase hrp/product/Thermo Fisher
    Average 88 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    streptavidin horse radish peroxidase hrp - by Bioz Stars, 2020-07
    88/100 stars
      Buy from Supplier

    91
    Thermo Fisher streptavidin horse radish peroxidase
    FKBP25 associates with ribosome biogenesis factors and other proteins in an RNA-dependent manner. ( A ) Schematic of BioID-based identification of cellular proteins proximal to FKBP25. ( B ) <t>Streptavidin-HRP</t> western blot of whole cell extracts and streptavidin capture from U2OS cells stably expressing an FKBP25 biotin ligase fusion or biotin ligase control, incubated for 24 hours in media containing 50 μM biotin. ( C ) Mass spectrometry identification of biotinylated proteins enriched in FKBP25-BirA streptavidin purifications relative to BirA control. The number of significant peptides identified relative to fold change is shown. ( D ) Enriched gene ontologies by molecular function. ( E ) FKBP25 3xFLAG-tagged co-immunoprecipitated material with and without pre-treatment with RNaseA analyzed by SDS-PAGE and visualized by silver stain. Empty vector cell lines are shown as a control. ( F ) Mass spectrometry analysis of proteins enriched in the FKBP25-FLAG sample relative to control, for samples either untreated or pre-treated with RNaseA. ( G ) Summarized gene ontology analysis by biological process. ( H ) Overlap in identified proteins between the BioID and FLAG co-immunoprecipitation experiments.
    Streptavidin Horse Radish Peroxidase, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 91/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/streptavidin horse radish peroxidase/product/Thermo Fisher
    Average 91 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    streptavidin horse radish peroxidase - by Bioz Stars, 2020-07
    91/100 stars
      Buy from Supplier

    Image Search Results


    Cell surface localization of ANT1 and ANT2. A – D , After cell surface biotinylation of live cerebellar neurons, biotinylated cell surface proteins were isolated using streptavidin-coupled beads ( A–C ), and ANT1 and ANT2 were immunoprecipitated using ANT1- and ANT2-specific antibodies ( D ). Cell lysates (input), isolated biotinylated proteins (surface) and the ANT1 and ANT2 immunoprecipitates (IP) were subjected to Western blot (WB) analysis using either ANT1-specific (ANT1; A ), ANT2-specific (ANT2; B ), or tubulin ( C ) antibodies or using HRP-conjugated streptavidin ( D ). The 60 kDa ANT protein seen after short time exposure (top) and the 32 kDa ANT protein seen after long time exposure (bottom) are indicated.

    Journal: The Journal of Neuroscience

    Article Title: The Interaction between Cell Adhesion Molecule L1, Matrix Metalloproteinase 14, and Adenine Nucleotide Translocator at the Plasma Membrane Regulates L1-Mediated Neurite Outgrowth of Murine Cerebellar Neurons

    doi: 10.1523/JNEUROSCI.6165-11.2012

    Figure Lengend Snippet: Cell surface localization of ANT1 and ANT2. A – D , After cell surface biotinylation of live cerebellar neurons, biotinylated cell surface proteins were isolated using streptavidin-coupled beads ( A–C ), and ANT1 and ANT2 were immunoprecipitated using ANT1- and ANT2-specific antibodies ( D ). Cell lysates (input), isolated biotinylated proteins (surface) and the ANT1 and ANT2 immunoprecipitates (IP) were subjected to Western blot (WB) analysis using either ANT1-specific (ANT1; A ), ANT2-specific (ANT2; B ), or tubulin ( C ) antibodies or using HRP-conjugated streptavidin ( D ). The 60 kDa ANT protein seen after short time exposure (top) and the 32 kDa ANT protein seen after long time exposure (bottom) are indicated.

    Article Snippet: Streptavidin conjugated with horse radish peroxidase (HRP) and recombinant catalytically active MMP14 and MMP14 comprising the prodomain, the catalytic domain, and the hemopexin domain were from ThermoScientific.

    Techniques: Isolation, Immunoprecipitation, Western Blot

    Analysis of p53 binding to head-to-tail response element in cyclin B promoter using electrophoretic mobility shift assays. A , MCF10A, MCF10A/OD, and MCF10A/Δp53 cell lines were incubated with 10 ng/ml SN38 for 24 hours (+SN) or were left untreated (–SN). Binding reactions were prepared by incubating nuclear extracts or recombinant p53 with a biotin-labeled probe corresponding to the head-to-tail response element in the cyclin B promoter, in the presence (+) or absence (−) of a 200-fold molar excess of specific DNA (unlabeled probe). All binding reactions were carried out in the presence of a 100-fold molar excess of unlabeled non-specific DNA. Complexes were separated on 4% native polyacrylamide gel electrophoresis, transferred to positively charged nylon membrane, and visualized using a streptavidin-horse radish peroxidase conjugate. B , A parallel gel was transferred to nitrocellulose membrane and immunoblotted with p53-specific antibodies.

    Journal: PLoS ONE

    Article Title: p53 Dimers Associate with a Head-to-Tail Response Element to Repress Cyclin B Transcription

    doi: 10.1371/journal.pone.0042615

    Figure Lengend Snippet: Analysis of p53 binding to head-to-tail response element in cyclin B promoter using electrophoretic mobility shift assays. A , MCF10A, MCF10A/OD, and MCF10A/Δp53 cell lines were incubated with 10 ng/ml SN38 for 24 hours (+SN) or were left untreated (–SN). Binding reactions were prepared by incubating nuclear extracts or recombinant p53 with a biotin-labeled probe corresponding to the head-to-tail response element in the cyclin B promoter, in the presence (+) or absence (−) of a 200-fold molar excess of specific DNA (unlabeled probe). All binding reactions were carried out in the presence of a 100-fold molar excess of unlabeled non-specific DNA. Complexes were separated on 4% native polyacrylamide gel electrophoresis, transferred to positively charged nylon membrane, and visualized using a streptavidin-horse radish peroxidase conjugate. B , A parallel gel was transferred to nitrocellulose membrane and immunoblotted with p53-specific antibodies.

    Article Snippet: The electrophoretic mobility of the complexes was detected using streptavidin-horse radish peroxidase (HRP) and a chemiluminescent substrate (Thermo Scientific).

    Techniques: Binding Assay, Electrophoretic Mobility Shift Assay, Incubation, Recombinant, Labeling, Polyacrylamide Gel Electrophoresis

    ELISA procedure, effect of buffer during pre-incubation and standard curve. (A) Schematic presentation of the sandwich ELISA. The five steps are: (1) coating of microplate wells with polyclonal dog anti-TK1 antibody (C215-231), (2) binding of TK1 in serum to coated antibody, (3) attachment of the biotinylated MAB 528–2 to TK1 in serum, (4) detection of biotin by streptavidin-HRP, and finally (5) enzymatic activity monitored by addition of 3,3 _, 5,5 _-Tetramethylbenzidine (TMB) chromogenic substrate. (B) Absorbance values of healthy, lymphoma and mammary tumor sera on TK1-ELISA during different pre-incubation time points (0, 30 and 60 min). The error bars represents the SEM of the mean values. (C) Comparison of the absorbance values of the serum samples from 0 min and 60 min. The error bars represent SEM of the mean. ns = no significant difference, *** p

    Journal: PLoS ONE

    Article Title: A New Sandwich ELISA for Quantification of Thymidine Kinase 1 Protein Levels in Sera from Dogs with Different Malignancies Can Aid in Disease Management

    doi: 10.1371/journal.pone.0137871

    Figure Lengend Snippet: ELISA procedure, effect of buffer during pre-incubation and standard curve. (A) Schematic presentation of the sandwich ELISA. The five steps are: (1) coating of microplate wells with polyclonal dog anti-TK1 antibody (C215-231), (2) binding of TK1 in serum to coated antibody, (3) attachment of the biotinylated MAB 528–2 to TK1 in serum, (4) detection of biotin by streptavidin-HRP, and finally (5) enzymatic activity monitored by addition of 3,3 _, 5,5 _-Tetramethylbenzidine (TMB) chromogenic substrate. (B) Absorbance values of healthy, lymphoma and mammary tumor sera on TK1-ELISA during different pre-incubation time points (0, 30 and 60 min). The error bars represents the SEM of the mean values. (C) Comparison of the absorbance values of the serum samples from 0 min and 60 min. The error bars represent SEM of the mean. ns = no significant difference, *** p

    Article Snippet: The plates were washed as above and streptavidin-horse radish peroxidase (HRP) diluted 1: 32,000 in wash buffer was added, and incubated for 1 h. After the final wash, 3, 3 _, 5, 5 _-Tetramethylbenzidine (TMB) (Thermo Fisher Scientific) was added and allowed to develop colour for 15 min, and then quenched with 2N H2 SO4 .

    Techniques: Enzyme-linked Immunosorbent Assay, Incubation, Sandwich ELISA, Binding Assay, Activity Assay

    FKBP25 associates with ribosome biogenesis factors and other proteins in an RNA-dependent manner. ( A ) Schematic of BioID-based identification of cellular proteins proximal to FKBP25. ( B ) Streptavidin-HRP western blot of whole cell extracts and streptavidin capture from U2OS cells stably expressing an FKBP25 biotin ligase fusion or biotin ligase control, incubated for 24 hours in media containing 50 μM biotin. ( C ) Mass spectrometry identification of biotinylated proteins enriched in FKBP25-BirA streptavidin purifications relative to BirA control. The number of significant peptides identified relative to fold change is shown. ( D ) Enriched gene ontologies by molecular function. ( E ) FKBP25 3xFLAG-tagged co-immunoprecipitated material with and without pre-treatment with RNaseA analyzed by SDS-PAGE and visualized by silver stain. Empty vector cell lines are shown as a control. ( F ) Mass spectrometry analysis of proteins enriched in the FKBP25-FLAG sample relative to control, for samples either untreated or pre-treated with RNaseA. ( G ) Summarized gene ontology analysis by biological process. ( H ) Overlap in identified proteins between the BioID and FLAG co-immunoprecipitation experiments.

    Journal: Nucleic Acids Research

    Article Title: The basic tilted helix bundle domain of the prolyl isomerase FKBP25 is a novel double-stranded RNA binding module

    doi: 10.1093/nar/gkx852

    Figure Lengend Snippet: FKBP25 associates with ribosome biogenesis factors and other proteins in an RNA-dependent manner. ( A ) Schematic of BioID-based identification of cellular proteins proximal to FKBP25. ( B ) Streptavidin-HRP western blot of whole cell extracts and streptavidin capture from U2OS cells stably expressing an FKBP25 biotin ligase fusion or biotin ligase control, incubated for 24 hours in media containing 50 μM biotin. ( C ) Mass spectrometry identification of biotinylated proteins enriched in FKBP25-BirA streptavidin purifications relative to BirA control. The number of significant peptides identified relative to fold change is shown. ( D ) Enriched gene ontologies by molecular function. ( E ) FKBP25 3xFLAG-tagged co-immunoprecipitated material with and without pre-treatment with RNaseA analyzed by SDS-PAGE and visualized by silver stain. Empty vector cell lines are shown as a control. ( F ) Mass spectrometry analysis of proteins enriched in the FKBP25-FLAG sample relative to control, for samples either untreated or pre-treated with RNaseA. ( G ) Summarized gene ontology analysis by biological process. ( H ) Overlap in identified proteins between the BioID and FLAG co-immunoprecipitation experiments.

    Article Snippet: Clones were screened by western blotting with streptavidin–horse radish peroxidase (Thermo Fisher).

    Techniques: Western Blot, Stable Transfection, Expressing, Incubation, Mass Spectrometry, Immunoprecipitation, SDS Page, Silver Staining, Plasmid Preparation