streptavidin horseradish peroxidase hrp  (Thermo Fisher)


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    Structured Review

    Thermo Fisher streptavidin horseradish peroxidase hrp
    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 <t>streptavidin-HRP</t> 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
    Streptavidin Horseradish Peroxidase Hrp, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) 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

    2) 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

    3) 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

    4) 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

    5) 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

    6) 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

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    Blocking Assay:

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    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).

    Incubation:

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    Article Snippet: .. 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. ..

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

    Activity Assay:

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    Western Blot:

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    Translocation Assay:

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    Immunohistochemistry:

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    Article Title: Chronic doxorubicin administration impacts satellite cell and capillary abundance in a muscle‐specific manner. Chronic doxorubicin administration impacts satellite cell and capillary abundance in a muscle‐specific manner
    Article Snippet: Paragraph title: Immunohistochemistry ... The next day, slides were incubated for 70 min at room temperature in goat anti‐rabbit AF488 (#A11034; Invitrogen, laminin) and goat anti‐mouse biotinylated secondary antibody (no. 115‐065‐205; Jackson ImmunoResearch, West Grove, PA), and then reacted with streptavidin‐horseradish peroxidase (HRP) and AF555 tyramide included with the tyramide signal amplification (TSA) kit (#B40933; Invitrogen).

    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.

    Article Title: Chronic doxorubicin administration impacts satellite cell and capillary abundance in a muscle‐specific manner. Chronic doxorubicin administration impacts satellite cell and capillary abundance in a muscle‐specific manner
    Article Snippet: The next day, slides were incubated for 70 min at room temperature in goat anti‐rabbit AF488 (#A11034; Invitrogen, laminin) and goat anti‐mouse biotinylated secondary antibody (no. 115‐065‐205; Jackson ImmunoResearch, West Grove, PA), and then reacted with streptavidin‐horseradish peroxidase (HRP) and AF555 tyramide included with the tyramide signal amplification (TSA) kit (#B40933; Invitrogen). .. TSA‐AF555 was used to visualize Pax7 antibody binding.

    Immunofluorescence:

    Article Title: The cellular prion protein promotes olfactory sensory neuron survival and axon targeting during adult neurogenesis
    Article Snippet: Streptavidin-horseradish peroxidase (HRP) (Biosource International, Camarillo, CA) was used at 1:800 and incubated at room temperature for 20 min. BrdU was then visualized with localization of HRP activity with DAB+ chromogen (Dako, Carpinteria, CA). .. Dual immunofluorescence for BrdU was combined with that of either GAP43 or OMP.

    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. ..

    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 [ ]. ..

    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.

    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.

    IA:

    Article Title: Chronic doxorubicin administration impacts satellite cell and capillary abundance in a muscle‐specific manner. Chronic doxorubicin administration impacts satellite cell and capillary abundance in a muscle‐specific manner
    Article Snippet: Briefly, unfixed slides were incubated for 90 min at room temperature with antibodies directed against laminin (no. L9393; Sigma Aldrich, St. Louis, MO), myosin heavy chain (MHC) I [BA.D5; supernatant, Developmental Studies Hybridoma Bank (DSHB, Iowa City, IA)], MHC IIa (SC.71; supernatant, DSHB), and MHC IIb (BF.F3; supernatant, DSHB). .. The next day, slides were incubated for 70 min at room temperature in goat anti‐rabbit AF488 (#A11034; Invitrogen, laminin) and goat anti‐mouse biotinylated secondary antibody (no. 115‐065‐205; Jackson ImmunoResearch, West Grove, PA), and then reacted with streptavidin‐horseradish peroxidase (HRP) and AF555 tyramide included with the tyramide signal amplification (TSA) kit (#B40933; Invitrogen).

    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 [ ]. ..

    Plasmid Preparation:

    Article Title: The cellular prion protein promotes olfactory sensory neuron survival and axon targeting during adult neurogenesis
    Article Snippet: Streptavidin-horseradish peroxidase (HRP) (Biosource International, Camarillo, CA) was used at 1:800 and incubated at room temperature for 20 min. BrdU was then visualized with localization of HRP activity with DAB+ chromogen (Dako, Carpinteria, CA). .. Streptavidin-horseradish peroxidase (HRP) (Biosource International, Camarillo, CA) was used at 1:800 and incubated at room temperature for 20 min. BrdU was then visualized with localization of HRP activity with DAB+ chromogen (Dako, Carpinteria, CA).

    Article Title: Chronic doxorubicin administration impacts satellite cell and capillary abundance in a muscle‐specific manner. Chronic doxorubicin administration impacts satellite cell and capillary abundance in a muscle‐specific manner
    Article Snippet: The next day, slides were incubated for 70 min at room temperature in goat anti‐rabbit AF488 (#A11034; Invitrogen, laminin) and goat anti‐mouse biotinylated secondary antibody (no. 115‐065‐205; Jackson ImmunoResearch, West Grove, PA), and then reacted with streptavidin‐horseradish peroxidase (HRP) and AF555 tyramide included with the tyramide signal amplification (TSA) kit (#B40933; Invitrogen). .. The next day, slides were incubated for 70 min at room temperature in goat anti‐rabbit AF488 (#A11034; Invitrogen, laminin) and goat anti‐mouse biotinylated secondary antibody (no. 115‐065‐205; Jackson ImmunoResearch, West Grove, PA), and then reacted with streptavidin‐horseradish peroxidase (HRP) and AF555 tyramide included with the tyramide signal amplification (TSA) kit (#B40933; Invitrogen).

    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: 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.

    Recombinant:

    Article Title: Unlike for Human Monocytes after LPS Activation, Release of TNF-? by THP-1 Cells Is Produced by a TACE Catalytically Different from Constitutive TACE
    Article Snippet: Monoclonal anti-human extracellular TNF-α-Fluorescein, monoclonal anti-human TACE-Phycoerythrin and Human recombinant TACE were obtained from R & D Systems Europe (Lille, France). .. Streptavidin-Horseradish peroxidase (HRP) was from Zymed (Clinisciences, Montrouge, France).

    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.

    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.

    Article Title: Chronic doxorubicin administration impacts satellite cell and capillary abundance in a muscle‐specific manner. Chronic doxorubicin administration impacts satellite cell and capillary abundance in a muscle‐specific manner
    Article Snippet: For Pax7/laminin/DAPI staining (visualization of myonuclei and satellite cells), immunohistochemical procedures were adapted from Finnerty et al. ( ). .. The next day, slides were incubated for 70 min at room temperature in goat anti‐rabbit AF488 (#A11034; Invitrogen, laminin) and goat anti‐mouse biotinylated secondary antibody (no. 115‐065‐205; Jackson ImmunoResearch, West Grove, PA), and then reacted with streptavidin‐horseradish peroxidase (HRP) and AF555 tyramide included with the tyramide signal amplification (TSA) kit (#B40933; Invitrogen).

    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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  • 99
    Thermo Fisher streptavidin hrp
    Schematic diagram showed non-radioactive metabolic incorporation followed by azide-biotin or azide-Alex555 labeling, and biotin signals of proteins were detected by <t>streptavidin-HRP</t> by western blot. HPG is incorporated into newly synthesized proteins by metabolism and protein synthesis and the triazole conjugation between newly alkyne proteins labeled HPG and azide labeled either biotin or Alex555 via CuSO4 catalysis (A) . (B-a) The detection of biotin signals from extracted total proteins labeled by labeling reaction. Normal culture medium was changed to replace DMEM free of L-methionine supplemented with HPG after pulse 4 hr, and proteins were extracted in each of group at various time points including 0, 4, 24 and 72 hr. (B-b) Biotin signals of total proteins were detected. 1: Normal culture condition group; 2: HPG plus anisomycin group; 3: HPG group. (B-c,d,e) Biotin signals of Bcl-2, MMP-9 and IgG were individually detected in the immunoprecipitate pulled down by primary antibodies via siRNA post-transfection followed by non-radioactive metabolic labeling. (B-f) Radioactive isotope 35 S-methonine incorporated into synthesized IgG purified by immunoprecipitation was detected by autoradiography. 1: 35 S-methonine treated human choriocarcinoma cell line BeWo group and then antibody against human IgG immunoprecipitated human IgG in extracted total proteins; 2: cycloheximide plus 35 S-methonine treated BeWo group then antibody against human IgG immunoprecipitated human IgG in extracted total proteins; 3: 35 S-methonine treated skin fibroblast and then antibody against human IgG immunoprecipitated human IgG in extracted total proteins.
    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, 2020-04
    99/100 stars
      Buy from Supplier

    93
    Thermo Fisher streptavidin conjugated hrp
    Photoaffinity labeling of various PrP species. <t>Streptavidin-HRP-probed</t> blots of samples photoaffinity labeled with PA-PBD peptide. (A) Samples containing PrP Int1 or PrP C were incubated with or without PA-PBD and exposed to UV light for varying time periods, as indicated. (B) Samples containing α -helical PrP or PrP Int1 were incubated with PA-PBD and exposed to UV light for 5 min. (C) Samples of PrP Int1 were incubated with varying concentrations of PA-PBD, as indicated, and exposed to UV light for 0 or 5 min, as indicated. (D) Sample containing 7 μ g of PrP Int1 photoaffinity labeled with PA-PBD (PA-PrP Int1 ) is compared to a standard curve of biotinylated AviTag PrP for reference.
    Streptavidin Conjugated Hrp, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/streptavidin conjugated hrp/product/Thermo Fisher
    Average 93 stars, based on 7 article reviews
    Price from $9.99 to $1999.99
    streptavidin conjugated hrp - by Bioz Stars, 2020-04
    93/100 stars
      Buy from Supplier

    Image Search Results


    Schematic diagram showed non-radioactive metabolic incorporation followed by azide-biotin or azide-Alex555 labeling, and biotin signals of proteins were detected by streptavidin-HRP by western blot. HPG is incorporated into newly synthesized proteins by metabolism and protein synthesis and the triazole conjugation between newly alkyne proteins labeled HPG and azide labeled either biotin or Alex555 via CuSO4 catalysis (A) . (B-a) The detection of biotin signals from extracted total proteins labeled by labeling reaction. Normal culture medium was changed to replace DMEM free of L-methionine supplemented with HPG after pulse 4 hr, and proteins were extracted in each of group at various time points including 0, 4, 24 and 72 hr. (B-b) Biotin signals of total proteins were detected. 1: Normal culture condition group; 2: HPG plus anisomycin group; 3: HPG group. (B-c,d,e) Biotin signals of Bcl-2, MMP-9 and IgG were individually detected in the immunoprecipitate pulled down by primary antibodies via siRNA post-transfection followed by non-radioactive metabolic labeling. (B-f) Radioactive isotope 35 S-methonine incorporated into synthesized IgG purified by immunoprecipitation was detected by autoradiography. 1: 35 S-methonine treated human choriocarcinoma cell line BeWo group and then antibody against human IgG immunoprecipitated human IgG in extracted total proteins; 2: cycloheximide plus 35 S-methonine treated BeWo group then antibody against human IgG immunoprecipitated human IgG in extracted total proteins; 3: 35 S-methonine treated skin fibroblast and then antibody against human IgG immunoprecipitated human IgG in extracted total proteins.

    Journal: BMC Cell Biology

    Article Title: A morphologic and semi-quantitative technique to analyze synthesis and release of specific proteins in cells

    doi: 10.1186/s12860-014-0045-1

    Figure Lengend Snippet: Schematic diagram showed non-radioactive metabolic incorporation followed by azide-biotin or azide-Alex555 labeling, and biotin signals of proteins were detected by streptavidin-HRP by western blot. HPG is incorporated into newly synthesized proteins by metabolism and protein synthesis and the triazole conjugation between newly alkyne proteins labeled HPG and azide labeled either biotin or Alex555 via CuSO4 catalysis (A) . (B-a) The detection of biotin signals from extracted total proteins labeled by labeling reaction. Normal culture medium was changed to replace DMEM free of L-methionine supplemented with HPG after pulse 4 hr, and proteins were extracted in each of group at various time points including 0, 4, 24 and 72 hr. (B-b) Biotin signals of total proteins were detected. 1: Normal culture condition group; 2: HPG plus anisomycin group; 3: HPG group. (B-c,d,e) Biotin signals of Bcl-2, MMP-9 and IgG were individually detected in the immunoprecipitate pulled down by primary antibodies via siRNA post-transfection followed by non-radioactive metabolic labeling. (B-f) Radioactive isotope 35 S-methonine incorporated into synthesized IgG purified by immunoprecipitation was detected by autoradiography. 1: 35 S-methonine treated human choriocarcinoma cell line BeWo group and then antibody against human IgG immunoprecipitated human IgG in extracted total proteins; 2: cycloheximide plus 35 S-methonine treated BeWo group then antibody against human IgG immunoprecipitated human IgG in extracted total proteins; 3: 35 S-methonine treated skin fibroblast and then antibody against human IgG immunoprecipitated human IgG in extracted total proteins.

    Article Snippet: Each diluted standard was incubated with primary antibody coated on the well and streptavidin-HRP and OD value for each sample was detected by ELISA.

    Techniques: Labeling, Western Blot, Synthesized, Conjugation Assay, Transfection, Purification, Immunoprecipitation, Autoradiography

    Electron microscopy of PA1b-bound V-ATPase. A , representative classes of PA1b-streptavidin-HRP-bound V-ATPase in the absence of ATP. B , as A but in the presence of 2 m m Mg·ATP. The PA1b-streptavidin-HRP density is indicated by an arrow in the far left panel 1 of A. Scale bars in both A and B represent 15 nm. C–E , three-dimensional reconstructions of the V-ATPase viewed perpendicular to the long axis of the complex ( upper image ) and from the extracellular end ( lower image ) bound to PA1b ( C ), bound to PA1b after the addition of Mg·ATP ( D ) and a control with no PA1b ( E ). All models were generated using EMAN, and the picture was produced using Chimera rendered at the same sigma level. In C ( lower ), the decameric c ring (Protein Data Bank ID code 2DB4 ( 53 ) r ainbow colors ) and a subunit model ( red ) have been fitted to the PA1b-streptavidin-HRP V-ATPase reconstruction in the absence of ATP using Chimera. If catalytically active, the c ring would rotate counterclockwise with respect to subunit a when observed from this perspective.

    Journal: The Journal of Biological Chemistry

    Article Title: PA1b Inhibitor Binding to Subunits c and e of the Vacuolar ATPase Reveals Its Insecticidal Mechanism *

    doi: 10.1074/jbc.M113.541250

    Figure Lengend Snippet: Electron microscopy of PA1b-bound V-ATPase. A , representative classes of PA1b-streptavidin-HRP-bound V-ATPase in the absence of ATP. B , as A but in the presence of 2 m m Mg·ATP. The PA1b-streptavidin-HRP density is indicated by an arrow in the far left panel 1 of A. Scale bars in both A and B represent 15 nm. C–E , three-dimensional reconstructions of the V-ATPase viewed perpendicular to the long axis of the complex ( upper image ) and from the extracellular end ( lower image ) bound to PA1b ( C ), bound to PA1b after the addition of Mg·ATP ( D ) and a control with no PA1b ( E ). All models were generated using EMAN, and the picture was produced using Chimera rendered at the same sigma level. In C ( lower ), the decameric c ring (Protein Data Bank ID code 2DB4 ( 53 ) r ainbow colors ) and a subunit model ( red ) have been fitted to the PA1b-streptavidin-HRP V-ATPase reconstruction in the absence of ATP using Chimera. If catalytically active, the c ring would rotate counterclockwise with respect to subunit a when observed from this perspective.

    Article Snippet: For the second experiment, 4 μl of V-ATPase (4 μg) was mixed with 3 μl of biotin-PA1b (3 μg) and 3 μl of streptavidin-HRP (15 μg), made up to 60 μl using V-ATPase buffer and incubated for 30 min. Mg·ATP was from a stock solution of 100 mm at pH 7.5 to a final concentration of 5 mm , and the mixture was incubated at room temperature for 5 min to allow for complete turnover.

    Techniques: Electron Microscopy, Generated, Produced

    Expression of recombinant porcine CCL2. (A) CHO cell line stably expressing the porcine CCL2 fused to GFP. The expression of GFP fusion protein was directly analysed by flow cytometry. Non transfected CHO cells were used as negative control (grey histogram). 5 000 cells were acquired. (B) Western blot of CCL2-GFP produced by transfected CHO cells. Different dilutions of supernatant were resolved by 15% SDS-PAGE under reducing conditions and revealed with biotinylated anti-GFP and streptavidin-HRP. Numbers on the left indicate the position of MW markers. (C) Chemotactic activity of CCL2-GFP on porcine blood monocytes. Chemotaxis was assessed with the Transwell cell migration system and subsequent flow cytometry counting of migrated cells by a 45 s acquisition. (1) FSC versus SSC dot plot of migrated cells in response to supernatants from CHO cells expressing CCL2-GFP or the inverted sequence of pCCL2 fused to GFP (InvCCL2-GFP, negative control). (2) Results expressed as migration index, calculated as the ratio of the number of cells migrating to the chemokine and the number of cells in the negative control. Results from one representative experiment out of three performed are shown. (A color version of this figure is available at www.vetres.org. )

    Journal: Veterinary Research

    Article Title: Porcine monocyte subsets differ in the expression of CCR2 and in their responsiveness to CCL2

    doi: 10.1051/vetres/2010048

    Figure Lengend Snippet: Expression of recombinant porcine CCL2. (A) CHO cell line stably expressing the porcine CCL2 fused to GFP. The expression of GFP fusion protein was directly analysed by flow cytometry. Non transfected CHO cells were used as negative control (grey histogram). 5 000 cells were acquired. (B) Western blot of CCL2-GFP produced by transfected CHO cells. Different dilutions of supernatant were resolved by 15% SDS-PAGE under reducing conditions and revealed with biotinylated anti-GFP and streptavidin-HRP. Numbers on the left indicate the position of MW markers. (C) Chemotactic activity of CCL2-GFP on porcine blood monocytes. Chemotaxis was assessed with the Transwell cell migration system and subsequent flow cytometry counting of migrated cells by a 45 s acquisition. (1) FSC versus SSC dot plot of migrated cells in response to supernatants from CHO cells expressing CCL2-GFP or the inverted sequence of pCCL2 fused to GFP (InvCCL2-GFP, negative control). (2) Results expressed as migration index, calculated as the ratio of the number of cells migrating to the chemokine and the number of cells in the negative control. Results from one representative experiment out of three performed are shown. (A color version of this figure is available at www.vetres.org. )

    Article Snippet: The expression of GFP-fused proteins in these clones was confirmed by Western blot using a biotin-conjugated goat anti-GFP polyclonal antibody and streptavidin-HRP.

    Techniques: Expressing, Recombinant, Stable Transfection, Flow Cytometry, Cytometry, Transfection, Negative Control, Western Blot, Produced, SDS Page, Activity Assay, Chemotaxis Assay, Migration, Sequencing

    Photoaffinity labeling of various PrP species. Streptavidin-HRP-probed blots of samples photoaffinity labeled with PA-PBD peptide. (A) Samples containing PrP Int1 or PrP C were incubated with or without PA-PBD and exposed to UV light for varying time periods, as indicated. (B) Samples containing α -helical PrP or PrP Int1 were incubated with PA-PBD and exposed to UV light for 5 min. (C) Samples of PrP Int1 were incubated with varying concentrations of PA-PBD, as indicated, and exposed to UV light for 0 or 5 min, as indicated. (D) Sample containing 7 μ g of PrP Int1 photoaffinity labeled with PA-PBD (PA-PrP Int1 ) is compared to a standard curve of biotinylated AviTag PrP for reference.

    Journal: Biochemistry

    Article Title: Prion Nucleation Site Unmasked by Transient Interaction with Phospholipid Cofactor

    doi: 10.1021/bi4014825

    Figure Lengend Snippet: Photoaffinity labeling of various PrP species. Streptavidin-HRP-probed blots of samples photoaffinity labeled with PA-PBD peptide. (A) Samples containing PrP Int1 or PrP C were incubated with or without PA-PBD and exposed to UV light for varying time periods, as indicated. (B) Samples containing α -helical PrP or PrP Int1 were incubated with PA-PBD and exposed to UV light for 5 min. (C) Samples of PrP Int1 were incubated with varying concentrations of PA-PBD, as indicated, and exposed to UV light for 0 or 5 min, as indicated. (D) Sample containing 7 μ g of PrP Int1 photoaffinity labeled with PA-PBD (PA-PrP Int1 ) is compared to a standard curve of biotinylated AviTag PrP for reference.

    Article Snippet: The resulting photoaffinity-labeled molecules were run on SDS-PAGE, transferred to PVDF, blocked with a 2.5% solution of bovine serum albumin (Fisher Scientific, Pittsburgh, PA), and incubated with streptavidin-conjugated HRP (ThermoFisher Scientific, Rockford, IL) at a 1:10 000 dilution before being washed with TBST and developed with SuperSignal West Femto maximum sensitivity substrate (ThermoFisher Scientific, Rockford, IL).

    Techniques: Labeling, Incubation