streptavidin horseradish peroxidase hrp  (Thermo Fisher)


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    Thermo Fisher streptavidin horseradish peroxidase hrp
    Deletion of Acaca in beta cells impairs glucose-driven lipogenesis in mice. ( a ) PCR analysis to confirm deletion of the floxed Acaca allele (indicated by arrow) in Ins2 cre- Acaca flox/flox (βACC1KO) but not in Acaca flox/flox (ACC1 flox) mice. A control PCR confirmed amplifiable DNA template in all samples (upper band). ( b ) ACC1 protein in islet lysates assessed by avidin pull-down and <t>streptavidin–HRP</t> detection. Pyruvate carboxylase (PC) was used as a loading control. n =3 batches of islets from independent mice. ( c – e ) A d -[U- 14 C]glucose tracer was used to measure glucose-driven metabolic flux in islets isolated from mice and incorporation into cellular lipid pools ( c ), aqueous metabolites ( d ) and glucose oxidation ( e ) were quantified. White bars, INS2cre mouse islets; grey bars, βACC1KO mouse islets. n =4 batches of islets from independent mice. Data are presented as mean ± SEM. * p
    Streptavidin Horseradish Peroxidase Hrp, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Disruption of beta cell acetyl-CoA carboxylase-1 in mice impairs insulin secretion and beta cell mass"

    Article Title: Disruption of beta cell acetyl-CoA carboxylase-1 in mice impairs insulin secretion and beta cell mass

    Journal: Diabetologia

    doi: 10.1007/s00125-018-4743-7

    Deletion of Acaca in beta cells impairs glucose-driven lipogenesis in mice. ( a ) PCR analysis to confirm deletion of the floxed Acaca allele (indicated by arrow) in Ins2 cre- Acaca flox/flox (βACC1KO) but not in Acaca flox/flox (ACC1 flox) mice. A control PCR confirmed amplifiable DNA template in all samples (upper band). ( b ) ACC1 protein in islet lysates assessed by avidin pull-down and streptavidin–HRP detection. Pyruvate carboxylase (PC) was used as a loading control. n =3 batches of islets from independent mice. ( c – e ) A d -[U- 14 C]glucose tracer was used to measure glucose-driven metabolic flux in islets isolated from mice and incorporation into cellular lipid pools ( c ), aqueous metabolites ( d ) and glucose oxidation ( e ) were quantified. White bars, INS2cre mouse islets; grey bars, βACC1KO mouse islets. n =4 batches of islets from independent mice. Data are presented as mean ± SEM. * p
    Figure Legend Snippet: Deletion of Acaca in beta cells impairs glucose-driven lipogenesis in mice. ( a ) PCR analysis to confirm deletion of the floxed Acaca allele (indicated by arrow) in Ins2 cre- Acaca flox/flox (βACC1KO) but not in Acaca flox/flox (ACC1 flox) mice. A control PCR confirmed amplifiable DNA template in all samples (upper band). ( b ) ACC1 protein in islet lysates assessed by avidin pull-down and streptavidin–HRP detection. Pyruvate carboxylase (PC) was used as a loading control. n =3 batches of islets from independent mice. ( c – e ) A d -[U- 14 C]glucose tracer was used to measure glucose-driven metabolic flux in islets isolated from mice and incorporation into cellular lipid pools ( c ), aqueous metabolites ( d ) and glucose oxidation ( e ) were quantified. White bars, INS2cre mouse islets; grey bars, βACC1KO mouse islets. n =4 batches of islets from independent mice. Data are presented as mean ± SEM. * p

    Techniques Used: Mouse Assay, Polymerase Chain Reaction, Avidin-Biotin Assay, Isolation

    2) Product Images from "Surface interactions between two of the main periodontal pathogens: Porphyromonas gingivalis and Tannerella forsythia"

    Article Title: Surface interactions between two of the main periodontal pathogens: Porphyromonas gingivalis and Tannerella forsythia

    Journal: Journal of Periodontal & Implant Science

    doi: 10.5051/jpis.2016.46.1.2

    Cell-surface labeling with biotin. The surface proteins of P. gingivalis and T. forsythia were labeled with Sulfo-NHS-LC-Biotin and mixed with T. forsythia and P. gingivalis cells, respectively. Subsequently, the mixtures were subjected to SDS-PAGE, and then transferred onto nitrocellulose membranes. Biotinylated P. gingivalis and T. forsythia surface proteins were detected with streptavidin–HRP and 4-CN. Lanes: MW, molecular weight marker; Tf, biotinylated T. forsythia surface proteins bound to P. gingivalis ; Pg, biotinylated P. gingivalis surface proteins bound to T. forsythia
    Figure Legend Snippet: Cell-surface labeling with biotin. The surface proteins of P. gingivalis and T. forsythia were labeled with Sulfo-NHS-LC-Biotin and mixed with T. forsythia and P. gingivalis cells, respectively. Subsequently, the mixtures were subjected to SDS-PAGE, and then transferred onto nitrocellulose membranes. Biotinylated P. gingivalis and T. forsythia surface proteins were detected with streptavidin–HRP and 4-CN. Lanes: MW, molecular weight marker; Tf, biotinylated T. forsythia surface proteins bound to P. gingivalis ; Pg, biotinylated P. gingivalis surface proteins bound to T. forsythia

    Techniques Used: Labeling, SDS Page, Molecular Weight, Marker

    3) Product Images from ""

    Article Title:

    Journal: Molecular Pharmacology

    doi: 10.1124/mol.112.083428

    Molecular mechanism of fursultiamine as a hepcidin antagonist. (A) Fursultiamine tightly associates with Fpn. Cells were induced to express Fpn-GFP and were pretreated with solvent (bars 1 and 2) or 10 µ M fursultiamine (bars 3–6) for 1 hour. Cells were then either not washed (cotreatment [Co-T]; black bar) or were washed with PBS 3 times (pretreatment [Pre-T]; gray bar), and 1 µ g/ml hepcidin was added for an additional 1 or 2 hours. The amount of Fpn-GFP was quantified using flow cytometry. Each bar represents at least 3 replicates, and error bars represent the standard deviation. Results were expressed as normalized amount of Fpn-GFP where hepcidin-untreated sample = 100% and hepcidin-treated (1 or 2 hours) sample = 0%. (B) Hepcidin binding to Fpn is attenuated in the presence of fursultiamine. Cells were induced to express Fpn-GFP and were pretreated with 0 or 10 µ M fursultiamine (Furs) for 30 minutes. A range of biotinylated hepcidin (B-hep) concentrations (0, 2.5, 5, and 10 µ g/ml) was added to the cells for another 30 minutes. Protein lysates were immunoprecipitated with anti-GFP Ab (ab290), and biotinylated hepcidin bound to Fpn-GFP was detected with streptavidin-HRP. The amount of immunoprecipitated Fpn-GFP was confirmed with anti-Fpn Ab. (C) Fursultiamine blocks Fpn residue C326. Cells expressing Fpn-GFP were treated with either hepcidin (0.5 and 1 µ g/ml) or fursultiamine (1, 3, 10, and 30 µ M) for 30 minutes. Cell surface Fpn-GFP was labeled with maleimide-biotinylation reagent for 30 minutes in 4C. Total protein lysates were immunoprecipitated with anti-GFP Ab (ab290), and samples were analyzed by Western blotting using strepavidin-HRP (top panel) or anti-GFP antibody (bottom panel).
    Figure Legend Snippet: Molecular mechanism of fursultiamine as a hepcidin antagonist. (A) Fursultiamine tightly associates with Fpn. Cells were induced to express Fpn-GFP and were pretreated with solvent (bars 1 and 2) or 10 µ M fursultiamine (bars 3–6) for 1 hour. Cells were then either not washed (cotreatment [Co-T]; black bar) or were washed with PBS 3 times (pretreatment [Pre-T]; gray bar), and 1 µ g/ml hepcidin was added for an additional 1 or 2 hours. The amount of Fpn-GFP was quantified using flow cytometry. Each bar represents at least 3 replicates, and error bars represent the standard deviation. Results were expressed as normalized amount of Fpn-GFP where hepcidin-untreated sample = 100% and hepcidin-treated (1 or 2 hours) sample = 0%. (B) Hepcidin binding to Fpn is attenuated in the presence of fursultiamine. Cells were induced to express Fpn-GFP and were pretreated with 0 or 10 µ M fursultiamine (Furs) for 30 minutes. A range of biotinylated hepcidin (B-hep) concentrations (0, 2.5, 5, and 10 µ g/ml) was added to the cells for another 30 minutes. Protein lysates were immunoprecipitated with anti-GFP Ab (ab290), and biotinylated hepcidin bound to Fpn-GFP was detected with streptavidin-HRP. The amount of immunoprecipitated Fpn-GFP was confirmed with anti-Fpn Ab. (C) Fursultiamine blocks Fpn residue C326. Cells expressing Fpn-GFP were treated with either hepcidin (0.5 and 1 µ g/ml) or fursultiamine (1, 3, 10, and 30 µ M) for 30 minutes. Cell surface Fpn-GFP was labeled with maleimide-biotinylation reagent for 30 minutes in 4C. Total protein lysates were immunoprecipitated with anti-GFP Ab (ab290), and samples were analyzed by Western blotting using strepavidin-HRP (top panel) or anti-GFP antibody (bottom panel).

    Techniques Used: Flow Cytometry, Cytometry, Standard Deviation, Binding Assay, Immunoprecipitation, Expressing, Labeling, Western Blot

    4) Product Images from "The EphA8 Receptor Regulates Integrin Activity through p110? Phosphatidylinositol-3 Kinase in a Tyrosine Kinase Activity-Independent Manner"

    Article Title: The EphA8 Receptor Regulates Integrin Activity through p110? Phosphatidylinositol-3 Kinase in a Tyrosine Kinase Activity-Independent Manner

    Journal: Molecular and Cellular Biology

    doi: 10.1128/MCB.21.14.4579-4597.2001

    (A) Effects of anti-α 5 β 1 and anti-β 3 integrin blocking antibodies (Ab) on NIH 3T3 cell adhesion to fibronectin. NIH 3T3 fibroblasts stably expressing wild-type or kinase-inactive EphA8 were detached and incubated for 5 min with either anti-α 5 β 1 or anti-β 3 integrin blocking antibody (5 μg/ml). The cells were then replated on fibronectin-coated coverslips and allowed to adhere for 15 min. Data from three independent experiments are presented as means ± SE. (B) Induction of wild-type EphA8 protein expression in NIH 3T3 fibroblasts. Cells were incubated with 2 μg of doxycycline (Dox) per ml for the indicated periods of time and then lysed, and proteins from the lysates were immunoprecipitated with anti-EphA8 antibody. Immunoprecipitates were separated by 7.5% SDS-PAGE and immunoblotted with anti-EphA8 antibody (top); the same blot was stripped of antibodies and reprobed with antiphosphotyrosine antibody (bottom). (C) Effects of anti-α 5 β 1 and anti-β 3 integrin blocking antibodies on NIH 3T3 cell attachment stimulated by the induced expression of EphA8. Cells were treated with doxycycline for the indicated periods of time, and cell attachment assays were performed after incubation with either anti-α 5 β 1 or anti-β 3 blocking antibodies as described above. (D) Analysis of α 5 β 1 and β 3 integrins expressed in NIH 3T3 cells, concomitant with the induced expression of EphA8. EphA8 expression was induced for the indicated times, then the cells were harvested and cell surface proteins were biotinylated; integrins were immunoprecipitated with anti-α 5 polyclonal antibody, and biotinylated integrins were detected using streptavidin-HRP (top). Cells were lysed in PLC lysis buffer, and protein concentrations were equalized (bottom). Cell lysates were fractionated by SDS-PAGE and then analyzed by immunobloting using anti-β 3 antibody as a probe.
    Figure Legend Snippet: (A) Effects of anti-α 5 β 1 and anti-β 3 integrin blocking antibodies (Ab) on NIH 3T3 cell adhesion to fibronectin. NIH 3T3 fibroblasts stably expressing wild-type or kinase-inactive EphA8 were detached and incubated for 5 min with either anti-α 5 β 1 or anti-β 3 integrin blocking antibody (5 μg/ml). The cells were then replated on fibronectin-coated coverslips and allowed to adhere for 15 min. Data from three independent experiments are presented as means ± SE. (B) Induction of wild-type EphA8 protein expression in NIH 3T3 fibroblasts. Cells were incubated with 2 μg of doxycycline (Dox) per ml for the indicated periods of time and then lysed, and proteins from the lysates were immunoprecipitated with anti-EphA8 antibody. Immunoprecipitates were separated by 7.5% SDS-PAGE and immunoblotted with anti-EphA8 antibody (top); the same blot was stripped of antibodies and reprobed with antiphosphotyrosine antibody (bottom). (C) Effects of anti-α 5 β 1 and anti-β 3 integrin blocking antibodies on NIH 3T3 cell attachment stimulated by the induced expression of EphA8. Cells were treated with doxycycline for the indicated periods of time, and cell attachment assays were performed after incubation with either anti-α 5 β 1 or anti-β 3 blocking antibodies as described above. (D) Analysis of α 5 β 1 and β 3 integrins expressed in NIH 3T3 cells, concomitant with the induced expression of EphA8. EphA8 expression was induced for the indicated times, then the cells were harvested and cell surface proteins were biotinylated; integrins were immunoprecipitated with anti-α 5 polyclonal antibody, and biotinylated integrins were detected using streptavidin-HRP (top). Cells were lysed in PLC lysis buffer, and protein concentrations were equalized (bottom). Cell lysates were fractionated by SDS-PAGE and then analyzed by immunobloting using anti-β 3 antibody as a probe.

    Techniques Used: Blocking Assay, Stable Transfection, Expressing, Incubation, Immunoprecipitation, SDS Page, Cell Attachment Assay, Planar Chromatography, Lysis, Western Blot

    5) Product Images from "Regulation of Insulin-Stimulated Glucose Transporter GLUT4 Translocation and Akt Kinase Activity by Ceramide"

    Article Title: Regulation of Insulin-Stimulated Glucose Transporter GLUT4 Translocation and Akt Kinase Activity by Ceramide

    Journal: Molecular and Cellular Biology

    doi:

    C 2 -ceramide inhibits insulin-stimulated GLUT4 and IRAP translocation. Plasma membrane GLUT4 (A and B) and IRAP (C and D) levels were measured as described in Materials and Methods. In both assays, C 2 -ceramide (C2) (100 μM) or C 2 -dihydroceramide (C 2 H 2 ) (100 μM) was added 2 h prior to initiation of the assay. Insulin (20 nM) was present for the last 10 min. Immunofluorescence detection of GLUT4 on plasma membrane sheets was performed with polyclonal sheep anti-GLUT4 primary antibodies followed by rhodamine-conjugated anti-sheep secondary antibodies. Images were captured with a digital camera (A) and quantitated as described in Materials and Methods (B). Biotinylated IRAP was detected with streptavidin-HRP and visualized with enhanced chemifluorescence (C), and the results were quantitated on a phosphorimager (D). Each asterisk denotes that the difference from the value obtained in the presence of insulin alone was statistically significant at a P value of
    Figure Legend Snippet: C 2 -ceramide inhibits insulin-stimulated GLUT4 and IRAP translocation. Plasma membrane GLUT4 (A and B) and IRAP (C and D) levels were measured as described in Materials and Methods. In both assays, C 2 -ceramide (C2) (100 μM) or C 2 -dihydroceramide (C 2 H 2 ) (100 μM) was added 2 h prior to initiation of the assay. Insulin (20 nM) was present for the last 10 min. Immunofluorescence detection of GLUT4 on plasma membrane sheets was performed with polyclonal sheep anti-GLUT4 primary antibodies followed by rhodamine-conjugated anti-sheep secondary antibodies. Images were captured with a digital camera (A) and quantitated as described in Materials and Methods (B). Biotinylated IRAP was detected with streptavidin-HRP and visualized with enhanced chemifluorescence (C), and the results were quantitated on a phosphorimager (D). Each asterisk denotes that the difference from the value obtained in the presence of insulin alone was statistically significant at a P value of

    Techniques Used: Translocation Assay, Immunofluorescence

    6) Product Images from "Theaflavin-3, 3?-Digallate Induces Epidermal Growth Factor Receptor Down-Regulation"

    Article Title: Theaflavin-3, 3?-Digallate Induces Epidermal Growth Factor Receptor Down-Regulation

    Journal: Molecular carcinogenesis

    doi: 10.1002/mc.20174

    TF-3 induces internalization of the EGFR in A431 EGFR-overexpressing cells. (A) Confocal microscope images. After culturing in serum-free DMEM for 24 h, A431 cells were incubated with TF-3 (20 μM) for 1 h. Cells were fixed, permeabilized, and stained with an antibody against the N-terminus of the EGFR (528). This was followed by incubation with Alexa Fluor 568-conjugated anti-mouse IgG and analysis by confocal microscope. (B) A431 cells (3 × 10 4 cells) were seeded in 96-well plates. After culturing for 24 h, media were replaced with serum-free DMEM and cells were incubated for an additional 24 h. Cells were treated with different concentrations of TF-3 for 1 h. After washing with PBS, cells were incubated with acetic acid (pH 2.7)/NaCl at 4 °C. The relative number of ligand binding sites on the cell surface was determined by incubating cells with biotinylated EGF followed by incubation with streptavidin-HRP and HRP substrate. Absorbance at 415 nm was measured to quantify the biotinylated EGF level. Data are represented as mean ± S.D. (n = 3). The asterick (*) indicates a significant ( P
    Figure Legend Snippet: TF-3 induces internalization of the EGFR in A431 EGFR-overexpressing cells. (A) Confocal microscope images. After culturing in serum-free DMEM for 24 h, A431 cells were incubated with TF-3 (20 μM) for 1 h. Cells were fixed, permeabilized, and stained with an antibody against the N-terminus of the EGFR (528). This was followed by incubation with Alexa Fluor 568-conjugated anti-mouse IgG and analysis by confocal microscope. (B) A431 cells (3 × 10 4 cells) were seeded in 96-well plates. After culturing for 24 h, media were replaced with serum-free DMEM and cells were incubated for an additional 24 h. Cells were treated with different concentrations of TF-3 for 1 h. After washing with PBS, cells were incubated with acetic acid (pH 2.7)/NaCl at 4 °C. The relative number of ligand binding sites on the cell surface was determined by incubating cells with biotinylated EGF followed by incubation with streptavidin-HRP and HRP substrate. Absorbance at 415 nm was measured to quantify the biotinylated EGF level. Data are represented as mean ± S.D. (n = 3). The asterick (*) indicates a significant ( P

    Techniques Used: Microscopy, Incubation, Staining, Ligand Binding Assay

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    Amplification:

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    Blocking Assay:

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    Article Snippet: After blocking the wells with 5% skim milk in PBS, 100 μL of heat-inactivated sample diluted 1:1 in sample diluent (3% BSA in PBS containing 1% IGEPAL CA-630) was added and incubated for 1 h at 37°C. .. Wells were washed 3 times and incubated for 30 min at room temperature with 100 μL of 1:4000 diluted streptavidin-horseradish peroxidase (HRP) (Thermo Scientific, Rockford, IL).

    Electrophoresis:

    Article Title: The EphA8 Receptor Regulates Integrin Activity through p110? Phosphatidylinositol-3 Kinase in a Tyrosine Kinase Activity-Independent Manner
    Article Snippet: Bound material was eluted by boiling the beads in 5% sodium dodecyl sulfate (SDS) and resolved by electrophoresis on SDS–7.5 polyacrylamide gels (7.5% SDS-PAGE) under nonreducing conditions. .. Biotinylated integrins were detected by incubating blots with streptavidin-horseradish peroxidase (HRP) (Pierce).

    Sandwich ELISA:

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    Article Snippet: Secreted IL-32 protein in the supernatant was measured using an IL-32 sandwich enzyme-linked immunosorbent assay (ELISA) kit (SEL101; YbdY Biotech, South Korea) or a matched antibody pair (BioLegend, San Diego, CA). .. For detection we used streptavidin-horseradish peroxidase (HRP) (1:1,000; Pierce, Rockford, IL) and ABTS [2,2′-azinobis(3-ethylbenzthiazolinesulfonic acid)] HRP substrate mixture (Kirkegaard and Perry Laboratories, Inc., Gaithersburg, MD), and plates were read at 405 nm.

    Article Title: Hepatitis B Virus Surface Antigen Activates Myeloid Dendritic Cells via a Soluble CD14-Dependent Mechanism
    Article Snippet: CD14 concentration and sCD14-HBsAg complexes were analyzed by sandwich ELISA. .. Assay diluent, used for blocking and sample dilution, streptavidin-horseradish peroxidase (HRP), and TMB (3,3′,5,5′-tetramethylbenzidine) solution were all from eBioscience.

    Incubation:

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    Article Title: Surface interactions between two of the main periodontal pathogens: Porphyromonas gingivalis and Tannerella forsythia
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    Article Title: The EphA8 Receptor Regulates Integrin Activity through p110? Phosphatidylinositol-3 Kinase in a Tyrosine Kinase Activity-Independent Manner
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    Article Title: Disruption of beta cell acetyl-CoA carboxylase-1 in mice impairs insulin secretion and beta cell mass
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    Western Blot:

    Article Title: The EphA8 Receptor Regulates Integrin Activity through p110? Phosphatidylinositol-3 Kinase in a Tyrosine Kinase Activity-Independent Manner
    Article Snippet: Paragraph title: Immunoprecipitation, Western blotting, cell surface biotinylation, and pulse-chase experiments. ... Biotinylated integrins were detected by incubating blots with streptavidin-horseradish peroxidase (HRP) (Pierce).

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    Translocation Assay:

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    Immunohistochemistry:

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    Article Snippet: Paragraph title: Immunohistochemical staining ... The sections were washed as above and incubated with biotin-conjugated goat anti-rat IgG or goat anti-human IgG for 1 h at RT, followed by streptavidin–horseradish peroxidase (HRP) (Thermo Scientific, Waltham, MA, USA) for 20 min.

    RIA Assay:

    Article Title: Disruption of beta cell acetyl-CoA carboxylase-1 in mice impairs insulin secretion and beta cell mass
    Article Snippet: Western blotting Tissue and cells were lysed in radioimmunoassay precipitation (RIPA) buffer and western blotting performed as previously described [ ] using the primary antibodies indicated. .. ACC1 protein was identified by avidin–agarose bead pull-down, SDS-PAGE, transfer to polyvinylidene difluoride (PVDF), incubation with streptavidin–horseradish peroxidase (HRP) (ThermoFisher) and chemiluminescent detection: this method utilises the affinity of the endogenous ACC1-bound biotin for avidin/streptavidin and has been described previously [ ].

    Pulse Chase:

    Article Title: The EphA8 Receptor Regulates Integrin Activity through p110? Phosphatidylinositol-3 Kinase in a Tyrosine Kinase Activity-Independent Manner
    Article Snippet: Paragraph title: Immunoprecipitation, Western blotting, cell surface biotinylation, and pulse-chase experiments. ... Biotinylated integrins were detected by incubating blots with streptavidin-horseradish peroxidase (HRP) (Pierce).

    Immunoprecipitation:

    Article Title: The EphA8 Receptor Regulates Integrin Activity through p110? Phosphatidylinositol-3 Kinase in a Tyrosine Kinase Activity-Independent Manner
    Article Snippet: Paragraph title: Immunoprecipitation, Western blotting, cell surface biotinylation, and pulse-chase experiments. ... Biotinylated integrins were detected by incubating blots with streptavidin-horseradish peroxidase (HRP) (Pierce).

    Article Title:
    Article Snippet: .. The reagent was washed off with PBS, and total protein was isolated and immunoprecipitated with anti-GFP antibody (Abcam) and blotted using streptavidin–horseradish peroxidase (HRP) (Pierce) for the detection of biotinylated species. ..

    Article Title: Regulation of Insulin-Stimulated Glucose Transporter GLUT4 Translocation and Akt Kinase Activity by Ceramide
    Article Snippet: Samples were eluted in sodium dodecyl sulfate (SDS), and the eluate was divided into two parts; 80% was allocated for a gel to quantitate the amount of biotin, and 20% was allocated for a gel to quantitate the amount of IRAP immunoprecipitated. .. SDS gels intended for biotin quantitation were transferred to polyvinylidene difluoride membranes (Fisher), blocked in Tris-buffered saline containing 0.2% Tween with 6% bovine serum albumin, treated with 1 μg of streptavidin-horseradish peroxidase (HRP) (Pierce) per ml for 2 h, washed in Tris-buffered saline containing 0.2% Tween, and developed with an enhanced chemifluorescence kit (Amersham) on a STORM 860 scanner.

    Ligand Binding Assay:

    Article Title: Theaflavin-3, 3?-Digallate Induces Epidermal Growth Factor Receptor Down-Regulation
    Article Snippet: The number of ligand binding sites on the cell surface was determined by incubating cells with biotinylated EGF [ ]. .. To quantify the amount of biotinylated EGF, cells were incubated with streptavidin-horseradish peroxidase (HRP) (Zymed Laboratories, Carlsbad, CA) followed by HRP substrate (Bio-Rad) to develop color.

    Generated:

    Article Title: Association between gene polymorphisms and obesity and physical fitness in Korean children
    Article Snippet: The single-stranded PCR template generated by exonuclease digestion was overlaid on a 384-well plate precoated covalently with primer extension primers (SNP-IT primers), which were designed to hybridize immediately adjacent to polymorphic sites. .. The identities of the incorporated nucleotide were determined using serial colorimetric reactions using anti-FITC-AP (Roche, Basel, Switzerland) and streptavidin-horseradish peroxidase (HRP) (Pierce, Rockford, IL, USA).

    Polymerase Chain Reaction:

    Article Title: Association between gene polymorphisms and obesity and physical fitness in Korean children
    Article Snippet: The single-stranded PCR template generated by exonuclease digestion was overlaid on a 384-well plate precoated covalently with primer extension primers (SNP-IT primers), which were designed to hybridize immediately adjacent to polymorphic sites. .. The identities of the incorporated nucleotide were determined using serial colorimetric reactions using anti-FITC-AP (Roche, Basel, Switzerland) and streptavidin-horseradish peroxidase (HRP) (Pierce, Rockford, IL, USA).

    Binding Assay:

    Article Title: Attenuated Infectious Hematopoietic Necrosis Virus with Rearranged Gene Order as Potential Vaccine
    Article Snippet: To block nonspecific binding to the membrane, plates were then incubated with 2% bovine serum albumin (BSA)–PBS for 2 h at room temperature. .. Following additional washing steps (5 times in PBS), the plates were developed using streptavidin-horseradish peroxidase (HRP) (Thermo Scientific) for 1 h at room temperature, washed again with PBS, and incubated with 3-amino 9-ethylcarbazole (Sigma-Aldrich) for 30 min at room temperature in the dark.

    Radioactivity:

    Article Title: The EphA8 Receptor Regulates Integrin Activity through p110? Phosphatidylinositol-3 Kinase in a Tyrosine Kinase Activity-Independent Manner
    Article Snippet: Biotinylated integrins were detected by incubating blots with streptavidin-horseradish peroxidase (HRP) (Pierce). .. The cells were then pulse-labeled for 15 min with 200 μCi of [35 S]methionine and [35 S]cysteine (NEN), per ml, washed once to remove unincorporated radioactivity, and chased for 30 min in unlabeled normal medium with or without preclustered EphA5-Fc.

    Fluorescence:

    Article Title: B7x/B7-H4 modulates the adaptive immune response and ameliorates renal injury in antibody-mediated nephritis
    Article Snippet: The sections were washed as above and incubated with biotin-conjugated goat anti-rat IgG or goat anti-human IgG for 1 h at RT, followed by streptavidin–horseradish peroxidase (HRP) (Thermo Scientific, Waltham, MA, USA) for 20 min. .. The sections were washed as above and incubated with biotin-conjugated goat anti-rat IgG or goat anti-human IgG for 1 h at RT, followed by streptavidin–horseradish peroxidase (HRP) (Thermo Scientific, Waltham, MA, USA) for 20 min.

    Isolation:

    Article Title:
    Article Snippet: .. The reagent was washed off with PBS, and total protein was isolated and immunoprecipitated with anti-GFP antibody (Abcam) and blotted using streptavidin–horseradish peroxidase (HRP) (Pierce) for the detection of biotinylated species. ..

    Transfection:

    Article Title: The EphA8 Receptor Regulates Integrin Activity through p110? Phosphatidylinositol-3 Kinase in a Tyrosine Kinase Activity-Independent Manner
    Article Snippet: Biotinylated integrins were detected by incubating blots with streptavidin-horseradish peroxidase (HRP) (Pierce). .. For pulse-chase experiments, cells were transiently transfected with FLAG-tagged p110γ and then treated with doxycycline to induce the wild-type EphA8 protein.

    Article Title: West Nile Virus Genome with Glycosylated Envelope Protein and Deletion of Alpha Helices 1, 2, and 4 in the Capsid Protein Is Noninfectious and Efficiently Secretes Subviral Particles
    Article Snippet: The relative amount of secreted E protein (i.e., SVPs) in the culture fluid of transfected HEK-293 cells at 2 dpt (determined as the optimal time in pilot experiments) was analyzed quantitatively using capture enzyme-linked immunosorbent assay (ELISA). .. Plates were subsequently washed with PBST and incubated for 30 min at RT with streptavidin-horseradish peroxidase (HRP) (Life Technologies, Frederick, MD).

    Microscopy:

    Article Title: B7x/B7-H4 modulates the adaptive immune response and ameliorates renal injury in antibody-mediated nephritis
    Article Snippet: The sections were washed as above and incubated with biotin-conjugated goat anti-rat IgG or goat anti-human IgG for 1 h at RT, followed by streptavidin–horseradish peroxidase (HRP) (Thermo Scientific, Waltham, MA, USA) for 20 min. .. The sections were washed as above and incubated with biotin-conjugated goat anti-rat IgG or goat anti-human IgG for 1 h at RT, followed by streptavidin–horseradish peroxidase (HRP) (Thermo Scientific, Waltham, MA, USA) for 20 min.

    Avidin-Biotin Assay:

    Article Title: Disruption of beta cell acetyl-CoA carboxylase-1 in mice impairs insulin secretion and beta cell mass
    Article Snippet: .. ACC1 protein was identified by avidin–agarose bead pull-down, SDS-PAGE, transfer to polyvinylidene difluoride (PVDF), incubation with streptavidin–horseradish peroxidase (HRP) (ThermoFisher) and chemiluminescent detection: this method utilises the affinity of the endogenous ACC1-bound biotin for avidin/streptavidin and has been described previously [ ]. ..

    Labeling:

    Article Title: Surface interactions between two of the main periodontal pathogens: Porphyromonas gingivalis and Tannerella forsythia
    Article Snippet: The resulting P. gingivalis cells labeled with biotinylated T. forsythia surface proteins were then separated by SDS-PAGE and were transferred to a nitrocellulose membrane, as described elsewhere. .. Subsequently, biotinylated T. forsythia surface proteins were detected with the use of streptavidin–horseradish peroxidase (HRP) (Thermo Fisher Scientific) and 4-chloro-1-naphthol (4-CN) (Thermo Fisher Scientific), according to the manufacturer’s instructions.

    SDS Page:

    Article Title: Surface interactions between two of the main periodontal pathogens: Porphyromonas gingivalis and Tannerella forsythia
    Article Snippet: The resulting P. gingivalis cells labeled with biotinylated T. forsythia surface proteins were then separated by SDS-PAGE and were transferred to a nitrocellulose membrane, as described elsewhere. .. Subsequently, biotinylated T. forsythia surface proteins were detected with the use of streptavidin–horseradish peroxidase (HRP) (Thermo Fisher Scientific) and 4-chloro-1-naphthol (4-CN) (Thermo Fisher Scientific), according to the manufacturer’s instructions.

    Article Title: The EphA8 Receptor Regulates Integrin Activity through p110? Phosphatidylinositol-3 Kinase in a Tyrosine Kinase Activity-Independent Manner
    Article Snippet: Bound material was eluted by boiling the beads in 5% sodium dodecyl sulfate (SDS) and resolved by electrophoresis on SDS–7.5 polyacrylamide gels (7.5% SDS-PAGE) under nonreducing conditions. .. Biotinylated integrins were detected by incubating blots with streptavidin-horseradish peroxidase (HRP) (Pierce).

    Article Title: Disruption of beta cell acetyl-CoA carboxylase-1 in mice impairs insulin secretion and beta cell mass
    Article Snippet: .. ACC1 protein was identified by avidin–agarose bead pull-down, SDS-PAGE, transfer to polyvinylidene difluoride (PVDF), incubation with streptavidin–horseradish peroxidase (HRP) (ThermoFisher) and chemiluminescent detection: this method utilises the affinity of the endogenous ACC1-bound biotin for avidin/streptavidin and has been described previously [ ]. ..

    Software:

    Article Title: Association between gene polymorphisms and obesity and physical fitness in Korean children
    Article Snippet: The identities of the incorporated nucleotide were determined using serial colorimetric reactions using anti-FITC-AP (Roche, Basel, Switzerland) and streptavidin-horseradish peroxidase (HRP) (Pierce, Rockford, IL, USA). .. Development of yellow or blue colour was analysed using an ELISA reader and final genotyping calls were made using QCReview software.

    Enzyme-linked Immunosorbent Assay:

    Article Title: Human NOD2 Recognizes Structurally Unique Muramyl Dipeptides from Mycobacterium leprae
    Article Snippet: Secreted IL-32 protein in the supernatant was measured using an IL-32 sandwich enzyme-linked immunosorbent assay (ELISA) kit (SEL101; YbdY Biotech, South Korea) or a matched antibody pair (BioLegend, San Diego, CA). .. For detection we used streptavidin-horseradish peroxidase (HRP) (1:1,000; Pierce, Rockford, IL) and ABTS [2,2′-azinobis(3-ethylbenzthiazolinesulfonic acid)] HRP substrate mixture (Kirkegaard and Perry Laboratories, Inc., Gaithersburg, MD), and plates were read at 405 nm.

    Article Title: Hepatitis B Virus Surface Antigen Activates Myeloid Dendritic Cells via a Soluble CD14-Dependent Mechanism
    Article Snippet: Paragraph title: Analysis of sCD14 concentration and sCD14-HBsAg complexes by ELISA. ... Assay diluent, used for blocking and sample dilution, streptavidin-horseradish peroxidase (HRP), and TMB (3,3′,5,5′-tetramethylbenzidine) solution were all from eBioscience.

    Article Title: Detection of Influenza a Virus in Swine Nasal Swab Samples With a Wash-Free Magnetic Bioassay and a Handheld Giant Magnetoresistance Sensing System
    Article Snippet: Paragraph title: Enzyme Linked Immunosorbent Assay (ELISA) ... Wells were washed 3 times and incubated for 30 min at room temperature with 100 μL of 1:4000 diluted streptavidin-horseradish peroxidase (HRP) (Thermo Scientific, Rockford, IL).

    Article Title: West Nile Virus Genome with Glycosylated Envelope Protein and Deletion of Alpha Helices 1, 2, and 4 in the Capsid Protein Is Noninfectious and Efficiently Secretes Subviral Particles
    Article Snippet: The relative amount of secreted E protein (i.e., SVPs) in the culture fluid of transfected HEK-293 cells at 2 dpt (determined as the optimal time in pilot experiments) was analyzed quantitatively using capture enzyme-linked immunosorbent assay (ELISA). .. Plates were subsequently washed with PBST and incubated for 30 min at RT with streptavidin-horseradish peroxidase (HRP) (Life Technologies, Frederick, MD).

    Quantitation Assay:

    Article Title: Regulation of Insulin-Stimulated Glucose Transporter GLUT4 Translocation and Akt Kinase Activity by Ceramide
    Article Snippet: .. SDS gels intended for biotin quantitation were transferred to polyvinylidene difluoride membranes (Fisher), blocked in Tris-buffered saline containing 0.2% Tween with 6% bovine serum albumin, treated with 1 μg of streptavidin-horseradish peroxidase (HRP) (Pierce) per ml for 2 h, washed in Tris-buffered saline containing 0.2% Tween, and developed with an enhanced chemifluorescence kit (Amersham) on a STORM 860 scanner. .. SDS gels used for IRAP quantitation were treated identically to those for biotin quantitation except for the use of nonfat dry milk and application of anti-IRAP serum (1:2,000) and goat anti-rabbit HRP-conjugated antibody (1:5,000).

    Concentration Assay:

    Article Title: Surface interactions between two of the main periodontal pathogens: Porphyromonas gingivalis and Tannerella forsythia
    Article Snippet: Sulfo-NHS-LC-Biotin (Thermo Fisher Scientific) was added to the individual bacterial cells at a final concentration of 1 mg/mL, and the cells were incubated at RT for 30 minutes by rotation. .. Subsequently, biotinylated T. forsythia surface proteins were detected with the use of streptavidin–horseradish peroxidase (HRP) (Thermo Fisher Scientific) and 4-chloro-1-naphthol (4-CN) (Thermo Fisher Scientific), according to the manufacturer’s instructions.

    Article Title: Attenuated Infectious Hematopoietic Necrosis Virus with Rearranged Gene Order as Potential Vaccine
    Article Snippet: Head kidney leukocytes from individual fish were added to the wells in triplicate at a concentration of 1 × 105 per well. .. Following additional washing steps (5 times in PBS), the plates were developed using streptavidin-horseradish peroxidase (HRP) (Thermo Scientific) for 1 h at room temperature, washed again with PBS, and incubated with 3-amino 9-ethylcarbazole (Sigma-Aldrich) for 30 min at room temperature in the dark.

    Article Title: Hepatitis B Virus Surface Antigen Activates Myeloid Dendritic Cells via a Soluble CD14-Dependent Mechanism
    Article Snippet: Paragraph title: Analysis of sCD14 concentration and sCD14-HBsAg complexes by ELISA. ... Assay diluent, used for blocking and sample dilution, streptavidin-horseradish peroxidase (HRP), and TMB (3,3′,5,5′-tetramethylbenzidine) solution were all from eBioscience.

    Construct:

    Article Title: West Nile Virus Genome with Glycosylated Envelope Protein and Deletion of Alpha Helices 1, 2, and 4 in the Capsid Protein Is Noninfectious and Efficiently Secretes Subviral Particles
    Article Snippet: Paragraph title: Glycosylation of the E protein enhances SVP secretion from constructs with deletions in C. ... Plates were subsequently washed with PBST and incubated for 30 min at RT with streptavidin-horseradish peroxidase (HRP) (Life Technologies, Frederick, MD).

    Enzyme-linked Immunospot:

    Article Title: Attenuated Infectious Hematopoietic Necrosis Virus with Rearranged Gene Order as Potential Vaccine
    Article Snippet: Paragraph title: Quantification of antibody-secreting cells (ASCs) in the head kidney in response to N2G3 by ELISPOT assay. ... Following additional washing steps (5 times in PBS), the plates were developed using streptavidin-horseradish peroxidase (HRP) (Thermo Scientific) for 1 h at room temperature, washed again with PBS, and incubated with 3-amino 9-ethylcarbazole (Sigma-Aldrich) for 30 min at room temperature in the dark.

    Staining:

    Article Title: B7x/B7-H4 modulates the adaptive immune response and ameliorates renal injury in antibody-mediated nephritis
    Article Snippet: Paragraph title: Immunohistochemical staining ... The sections were washed as above and incubated with biotin-conjugated goat anti-rat IgG or goat anti-human IgG for 1 h at RT, followed by streptavidin–horseradish peroxidase (HRP) (Thermo Scientific, Waltham, MA, USA) for 20 min.

    Fluorescence In Situ Hybridization:

    Article Title: Attenuated Infectious Hematopoietic Necrosis Virus with Rearranged Gene Order as Potential Vaccine
    Article Snippet: Head kidney leukocytes from individual fish were added to the wells in triplicate at a concentration of 1 × 105 per well. .. Following additional washing steps (5 times in PBS), the plates were developed using streptavidin-horseradish peroxidase (HRP) (Thermo Scientific) for 1 h at room temperature, washed again with PBS, and incubated with 3-amino 9-ethylcarbazole (Sigma-Aldrich) for 30 min at room temperature in the dark.

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  • 90
    Thermo Fisher streptavidin hrp chemilluminescent detection system
    Streptavidin Hrp Chemilluminescent Detection System, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/streptavidin hrp chemilluminescent detection system/product/Thermo Fisher
    Average 90 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    streptavidin hrp chemilluminescent detection system - by Bioz Stars, 2020-01
    90/100 stars
      Buy from Supplier

    90
    Thermo Fisher streptavidin hrp conjugate
    Target-selective protein labelling with LDNASA chemistry. a Western blotting analysis of FKBP12 labelling in cell lysates. HeLa cell lysate was mixed with recombinant FKBP12 (1 µM) and incubated with reagent in 50 mM HEPES buffer, pH 7.2, 37 °C, 1 h. <t>SAv-HRP,</t> <t>streptavidin–horseradish</t> peroxidase conjugate; CBB, Coomassie brilliant blue staining. The high background (smear) signals of lane 6 and 7 may suggest unspecific labelling due to a high concentration of reagent (20 µM), whereas such background signals were less in lanes 1–5 (1–5 µM of reagent). b Western blotting analysis of endogenous FKBP12 labelling in live C2C12 cells. The cells were treated with 1 or 5 (1 µM) for 0–120 min at 37 °C in medium. c Time course plot of the endogenous FKBP12 labelling with 1 . d Molecular structures of LDNASA 9 and LDAI 10 for FR labelling. e In-gel fluorescence and western blotting analysis of endogenous FR labelling in KB cells. The cells were treated with 9 or 10 (1 µM) for 0–60 min at 37 °C in medium. FA, Folic acid (competitive inhibitor). f Time profile of the endogenous FR labelling with 9 . I and I 30 min are band intensities of Oregon Green-labelled FR at the indicated time point and at 30 min, respectively. Error bars represent s.d., n = 3
    Streptavidin Hrp Conjugate, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/streptavidin hrp conjugate/product/Thermo Fisher
    Average 90 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    streptavidin hrp conjugate - by Bioz Stars, 2020-01
    90/100 stars
      Buy from Supplier

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    Target-selective protein labelling with LDNASA chemistry. a Western blotting analysis of FKBP12 labelling in cell lysates. HeLa cell lysate was mixed with recombinant FKBP12 (1 µM) and incubated with reagent in 50 mM HEPES buffer, pH 7.2, 37 °C, 1 h. SAv-HRP, streptavidin–horseradish peroxidase conjugate; CBB, Coomassie brilliant blue staining. The high background (smear) signals of lane 6 and 7 may suggest unspecific labelling due to a high concentration of reagent (20 µM), whereas such background signals were less in lanes 1–5 (1–5 µM of reagent). b Western blotting analysis of endogenous FKBP12 labelling in live C2C12 cells. The cells were treated with 1 or 5 (1 µM) for 0–120 min at 37 °C in medium. c Time course plot of the endogenous FKBP12 labelling with 1 . d Molecular structures of LDNASA 9 and LDAI 10 for FR labelling. e In-gel fluorescence and western blotting analysis of endogenous FR labelling in KB cells. The cells were treated with 9 or 10 (1 µM) for 0–60 min at 37 °C in medium. FA, Folic acid (competitive inhibitor). f Time profile of the endogenous FR labelling with 9 . I and I 30 min are band intensities of Oregon Green-labelled FR at the indicated time point and at 30 min, respectively. Error bars represent s.d., n = 3

    Journal: Nature Communications

    Article Title: Rapid labelling and covalent inhibition of intracellular native proteins using ligand-directed N-acyl-N-alkyl sulfonamide

    doi: 10.1038/s41467-018-04343-0

    Figure Lengend Snippet: Target-selective protein labelling with LDNASA chemistry. a Western blotting analysis of FKBP12 labelling in cell lysates. HeLa cell lysate was mixed with recombinant FKBP12 (1 µM) and incubated with reagent in 50 mM HEPES buffer, pH 7.2, 37 °C, 1 h. SAv-HRP, streptavidin–horseradish peroxidase conjugate; CBB, Coomassie brilliant blue staining. The high background (smear) signals of lane 6 and 7 may suggest unspecific labelling due to a high concentration of reagent (20 µM), whereas such background signals were less in lanes 1–5 (1–5 µM of reagent). b Western blotting analysis of endogenous FKBP12 labelling in live C2C12 cells. The cells were treated with 1 or 5 (1 µM) for 0–120 min at 37 °C in medium. c Time course plot of the endogenous FKBP12 labelling with 1 . d Molecular structures of LDNASA 9 and LDAI 10 for FR labelling. e In-gel fluorescence and western blotting analysis of endogenous FR labelling in KB cells. The cells were treated with 9 or 10 (1 µM) for 0–60 min at 37 °C in medium. FA, Folic acid (competitive inhibitor). f Time profile of the endogenous FR labelling with 9 . I and I 30 min are band intensities of Oregon Green-labelled FR at the indicated time point and at 30 min, respectively. Error bars represent s.d., n = 3

    Article Snippet: The samples were analysed by western blotting using Streptavidin-HRP conjugate (SAv-HRP, Thermo, S911, 1:5000) and Coomassie Brilliant Blue (CBB) stain.

    Techniques: Western Blot, Recombinant, Incubation, Staining, Concentration Assay, Fluorescence

    Target-selective protein labelling with LDNASA chemistry. a Western blotting analysis of FKBP12 labelling in cell lysates. HeLa cell lysate was mixed with recombinant FKBP12 (1 µM) and incubated with reagent in 50 mM HEPES buffer, pH 7.2, 37 °C, 1 h. SAv-HRP, streptavidin–horseradish peroxidase conjugate; CBB, Coomassie brilliant blue staining. The high background (smear) signals of lane 6 and 7 may suggest unspecific labelling due to a high concentration of reagent (20 µM), whereas such background signals were less in lanes 1–5 (1–5 µM of reagent). b Western blotting analysis of endogenous FKBP12 labelling in live C2C12 cells. The cells were treated with 1 or 5 (1 µM) for 0–120 min at 37 °C in medium. c Time course plot of the endogenous FKBP12 labelling with 1 . d Molecular structures of LDNASA 9 and LDAI 10 for FR labelling. e In-gel fluorescence and western blotting analysis of endogenous FR labelling in KB cells. The cells were treated with 9 or 10 (1 µM) for 0–60 min at 37 °C in medium. FA, Folic acid (competitive inhibitor). f Time profile of the endogenous FR labelling with 9 . I and I 30 min are band intensities of Oregon Green-labelled FR at the indicated time point and at 30 min, respectively. Error bars represent s.d., n = 3

    Journal: Nature Communications

    Article Title: Rapid labelling and covalent inhibition of intracellular native proteins using ligand-directed N-acyl-N-alkyl sulfonamide

    doi: 10.1038/s41467-018-04343-0

    Figure Lengend Snippet: Target-selective protein labelling with LDNASA chemistry. a Western blotting analysis of FKBP12 labelling in cell lysates. HeLa cell lysate was mixed with recombinant FKBP12 (1 µM) and incubated with reagent in 50 mM HEPES buffer, pH 7.2, 37 °C, 1 h. SAv-HRP, streptavidin–horseradish peroxidase conjugate; CBB, Coomassie brilliant blue staining. The high background (smear) signals of lane 6 and 7 may suggest unspecific labelling due to a high concentration of reagent (20 µM), whereas such background signals were less in lanes 1–5 (1–5 µM of reagent). b Western blotting analysis of endogenous FKBP12 labelling in live C2C12 cells. The cells were treated with 1 or 5 (1 µM) for 0–120 min at 37 °C in medium. c Time course plot of the endogenous FKBP12 labelling with 1 . d Molecular structures of LDNASA 9 and LDAI 10 for FR labelling. e In-gel fluorescence and western blotting analysis of endogenous FR labelling in KB cells. The cells were treated with 9 or 10 (1 µM) for 0–60 min at 37 °C in medium. FA, Folic acid (competitive inhibitor). f Time profile of the endogenous FR labelling with 9 . I and I 30 min are band intensities of Oregon Green-labelled FR at the indicated time point and at 30 min, respectively. Error bars represent s.d., n = 3

    Article Snippet: The samples were analysed by western blotting using Streptavidin-HRP conjugate (SAv-HRP, Thermo, S911, 1:5000) and Coomassie Brilliant Blue (CBB) stain.

    Techniques: Western Blot, Recombinant, Incubation, Staining, Concentration Assay, Fluorescence