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  • 99
    Thermo Fisher streptavidin horseradish peroxidase conjugate
    AMMP and ELISA target-binding assays. (a) Schematic of the AMMP target-binding assay. An HA-tagged ligand binds to target (Bcl-x L ) immobilized on <t>streptavidin</t> magnetic beads. Anti-HA antibody, labeled with fluorescein, binds to the HA tag and to antifluorescein antibody on the sensor surface. (b) AMMP signal in the target-binding assay is a function of dilution factor and ligand affinity. At the same dilution, Pep1 generates higher signal levels than Pep2, whereas ScPep1 and Pep1ΔHA show background levels of signal. (c) AMMP target-binding assay adjusted for peptide concentration as measured using the HA tag competition assay, demonstrating true relative affinities. (d) Schematic of the ELISA target-binding assay. An HA-tagged ligand binds to biotinylated target (Bcl-x L ) and anti-HA antibody on the ELISA plate. Streptavidin-HRP binds to biotin, resulting in an ELISA signal. (e) Target-binding ELISA assay is much less sensitive than the AMMP assay [described in (b)], and the respective samples behave equivalently: Pep1 generates a higher signal level than Pep2 and ScPep1 and Pep1ΔHA generate no signal over the background. (f) ELISA target-binding assay adjusted for peptide concentration as measured using the HA tag competition assay.
    Streptavidin Horseradish Peroxidase Conjugate, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1012 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore streptavidin horseradish peroxidase conjugate
    Missorted surface proteins accumulate in the sortase mutant AR01. A. Wild type S . pyogenes D471, sortase mutant AR01, complemented AR01+pAR107, and a passaged AR01 variant, were diluted from overnight cultures 1:100 into fresh media (containing spectinomycin for AR01+pAR107), grown to log phase, fixed, attached to glass cover slides, and permeabilized with PlyC. The cells were blocked and incubated with pentaglycine-biotin (5G-biotin) in the presence or absence of purified S . aureus sortase A. The slides were washed, and pentaglycine-biotins molecules (attached to LPXTG motifs by sortase) were detected using <t>FITC-streptavidin.</t> DAPI was used to visualize DNA. The scale bar represents 1 μm. Note that expression of sortase from pAR107 is lower than the wild type, explaining the presence of intact LPXTG motifs. B. The cell wall fraction of log-phase D471 cells (solubilized with PlyC in PBS 30% raffinose) was separated by SDS-PAGE. Duplicate gels were stained with GelCode blue or processed for Western blot using the 10B6 monoclonal antibody. The most prominent bands on the stained gel correspond to M protein.
    Streptavidin Horseradish Peroxidase Conjugate, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 99 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Thermo Fisher streptavidin horseradish peroxidase
    Expression of protocadherins. GFP was electroporated alone or in combination with protocadherins into K562 cells. a Immunoblotting of cell lysates with anti-GFP shows bands compatible with the expected molecular weights for GFP (27 kDa) and mature PCDHB11-GFP (110 kDa); image representative of three transfections. b Immunoblotting of cell lysates with anti-HA shows bands compatible with the expected molecular weights for mature HA-PCDHB11-GFP (113 kDa) and HA-PCDHGA3 (99 kDa); image representative of two transfections. c Proportion of medium and large clusters was lower in HA-PCDHB11-GFP-transfected than in HA-PCDHGA3-transfected cells, but higher than in control cells ( n = 10-12 images per condition). d Proportion of medium to large cell clusters when normalized by HA-PCDHGA3. For visualization of surface protocadherins, live cells transfected with GFP alone (e) or in combination with HA-PCDHB11-GFP (f) or HA-PCDHGA3 (g) were stained with anti-HA-biotin and <t>streptavidin-Alexa555,</t> then fixed. Blue: DAPI. Green: GFP. Red: surface HA-tagged protocadherins. Scale bar: 10 μm
    Streptavidin Horseradish Peroxidase, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 1821 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Thermo Fisher streptavidin horseradish peroxidase complex
    Expression of protocadherins. GFP was electroporated alone or in combination with protocadherins into K562 cells. a Immunoblotting of cell lysates with anti-GFP shows bands compatible with the expected molecular weights for GFP (27 kDa) and mature PCDHB11-GFP (110 kDa); image representative of three transfections. b Immunoblotting of cell lysates with anti-HA shows bands compatible with the expected molecular weights for mature HA-PCDHB11-GFP (113 kDa) and HA-PCDHGA3 (99 kDa); image representative of two transfections. c Proportion of medium and large clusters was lower in HA-PCDHB11-GFP-transfected than in HA-PCDHGA3-transfected cells, but higher than in control cells ( n = 10-12 images per condition). d Proportion of medium to large cell clusters when normalized by HA-PCDHGA3. For visualization of surface protocadherins, live cells transfected with GFP alone (e) or in combination with HA-PCDHB11-GFP (f) or HA-PCDHGA3 (g) were stained with anti-HA-biotin and <t>streptavidin-Alexa555,</t> then fixed. Blue: DAPI. Green: GFP. Red: surface HA-tagged protocadherins. Scale bar: 10 μm
    Streptavidin Horseradish Peroxidase Complex, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 271 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Thermo Fisher streptavidin horseradish peroxidase hrp conjugate
    Expression of protocadherins. GFP was electroporated alone or in combination with protocadherins into K562 cells. a Immunoblotting of cell lysates with anti-GFP shows bands compatible with the expected molecular weights for GFP (27 kDa) and mature PCDHB11-GFP (110 kDa); image representative of three transfections. b Immunoblotting of cell lysates with anti-HA shows bands compatible with the expected molecular weights for mature HA-PCDHB11-GFP (113 kDa) and HA-PCDHGA3 (99 kDa); image representative of two transfections. c Proportion of medium and large clusters was lower in HA-PCDHB11-GFP-transfected than in HA-PCDHGA3-transfected cells, but higher than in control cells ( n = 10-12 images per condition). d Proportion of medium to large cell clusters when normalized by HA-PCDHGA3. For visualization of surface protocadherins, live cells transfected with GFP alone (e) or in combination with HA-PCDHB11-GFP (f) or HA-PCDHGA3 (g) were stained with anti-HA-biotin and <t>streptavidin-Alexa555,</t> then fixed. Blue: DAPI. Green: GFP. Red: surface HA-tagged protocadherins. Scale bar: 10 μm
    Streptavidin Horseradish Peroxidase Hrp Conjugate, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 91/100, based on 308 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    R&D Systems streptavidin horseradish peroxidase
    sCD127 binding to IL-7. A : sCD127 was immobilized on a high-binding polystyrene surface to detect binding of biotinylated IL-7 by colorimetric determination with <t>streptavidin-HRP</t> as shown schematically. B : IL-7 binding (optical density, y -axis) over an IL-7 concentration range from 0.125–2,048 ng/mL ( x -axis) to sCD127 (100 ng/mL; circles), sCD132 (1 ng/mL; diamonds), and sCD127 + sCD132 (100 ng/mL + 1 ng/mL; squares). Error bars represent mean ± SD from n = 3 experiments. AU, arbitrary units.
    Streptavidin Horseradish Peroxidase, supplied by R&D Systems, used in various techniques. Bioz Stars score: 92/100, based on 301 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Becton Dickinson streptavidin horseradish peroxidase
    Binding analysis of various sialylated PA–glycan conjugates to wild-type compared with siglec mutant B cells. Results are representative of three independent experiments. (A–E) B cells of the indicated genotypes were stained with biotinylated PA conjugated with the following glycans: (A) NeuAcα2-6Galβ1-4GlcNAc, (B) NeuGc, (C) bNeuGc, (D) NeuAcα2-3Galβ1-4GlcNAc, and (E), NeuGcα2-3Galβ1-4GlcNAc. Binding was revealed using fluorescent <t>streptavidin.</t> Background staining by streptavidin alone is shown in gray. (F) Chemical structures of the NeuGc-containing sialosides.
    Streptavidin Horseradish Peroxidase, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 92/100, based on 703 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    PerkinElmer streptavidin horseradish peroxidase
    Binding analysis of various sialylated PA–glycan conjugates to wild-type compared with siglec mutant B cells. Results are representative of three independent experiments. (A–E) B cells of the indicated genotypes were stained with biotinylated PA conjugated with the following glycans: (A) NeuAcα2-6Galβ1-4GlcNAc, (B) NeuGc, (C) bNeuGc, (D) NeuAcα2-3Galβ1-4GlcNAc, and (E), NeuGcα2-3Galβ1-4GlcNAc. Binding was revealed using fluorescent <t>streptavidin.</t> Background staining by streptavidin alone is shown in gray. (F) Chemical structures of the NeuGc-containing sialosides.
    Streptavidin Horseradish Peroxidase, supplied by PerkinElmer, used in various techniques. Bioz Stars score: 93/100, based on 339 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Agilent technologies streptavidin horseradish peroxidase
    Seropositivity to E4, E7, and VLPs-L1 in serum of healthy women and women with CC by Slot blot system. In vitro purified HPV antigens were immobilized in PROTRAN membranes using the Hybri-Slot system, and membranes were fixed and blocked as described in “Materials and Methods.” Strips containing the 3 HPV16 antigens (E4 10 ng, E7 10 ng, VLPs-L1 200 ng) and negative controls (buffer alone and GFP 200 ng) were incubated with dilutions (1:2,500) of sera from women with CC (A), sera from healthy women (B), and positive and negative female serum controls for anti-HPV antibodies (C). Biotinylated secondary antibody (dil 1:10,000) and <t>Streptavidin-horseradish</t> peroxidase (1:8,000) were used to develop the system, and the bands were finally visualized by chemiluminescence in the Odyssey Fc system. CC = cervical cancer, GFP = green fluorescent protein, HPV = human papillomavirus, VLPs-L1 = virus-like particles from L1 protein.
    Streptavidin Horseradish Peroxidase, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 94/100, based on 1533 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Biocare Medical streptavidin horseradish peroxidase
    Seropositivity to E4, E7, and VLPs-L1 in serum of healthy women and women with CC by Slot blot system. In vitro purified HPV antigens were immobilized in PROTRAN membranes using the Hybri-Slot system, and membranes were fixed and blocked as described in “Materials and Methods.” Strips containing the 3 HPV16 antigens (E4 10 ng, E7 10 ng, VLPs-L1 200 ng) and negative controls (buffer alone and GFP 200 ng) were incubated with dilutions (1:2,500) of sera from women with CC (A), sera from healthy women (B), and positive and negative female serum controls for anti-HPV antibodies (C). Biotinylated secondary antibody (dil 1:10,000) and <t>Streptavidin-horseradish</t> peroxidase (1:8,000) were used to develop the system, and the bands were finally visualized by chemiluminescence in the Odyssey Fc system. CC = cervical cancer, GFP = green fluorescent protein, HPV = human papillomavirus, VLPs-L1 = virus-like particles from L1 protein.
    Streptavidin Horseradish Peroxidase, supplied by Biocare Medical, used in various techniques. Bioz Stars score: 92/100, based on 71 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Boehringer Mannheim streptavidin horseradish peroxidase
    Seropositivity to E4, E7, and VLPs-L1 in serum of healthy women and women with CC by Slot blot system. In vitro purified HPV antigens were immobilized in PROTRAN membranes using the Hybri-Slot system, and membranes were fixed and blocked as described in “Materials and Methods.” Strips containing the 3 HPV16 antigens (E4 10 ng, E7 10 ng, VLPs-L1 200 ng) and negative controls (buffer alone and GFP 200 ng) were incubated with dilutions (1:2,500) of sera from women with CC (A), sera from healthy women (B), and positive and negative female serum controls for anti-HPV antibodies (C). Biotinylated secondary antibody (dil 1:10,000) and <t>Streptavidin-horseradish</t> peroxidase (1:8,000) were used to develop the system, and the bands were finally visualized by chemiluminescence in the Odyssey Fc system. CC = cervical cancer, GFP = green fluorescent protein, HPV = human papillomavirus, VLPs-L1 = virus-like particles from L1 protein.
    Streptavidin Horseradish Peroxidase, supplied by Boehringer Mannheim, used in various techniques. Bioz Stars score: 92/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Roche streptavidin horseradish peroxidase
    Seropositivity to E4, E7, and VLPs-L1 in serum of healthy women and women with CC by Slot blot system. In vitro purified HPV antigens were immobilized in PROTRAN membranes using the Hybri-Slot system, and membranes were fixed and blocked as described in “Materials and Methods.” Strips containing the 3 HPV16 antigens (E4 10 ng, E7 10 ng, VLPs-L1 200 ng) and negative controls (buffer alone and GFP 200 ng) were incubated with dilutions (1:2,500) of sera from women with CC (A), sera from healthy women (B), and positive and negative female serum controls for anti-HPV antibodies (C). Biotinylated secondary antibody (dil 1:10,000) and <t>Streptavidin-horseradish</t> peroxidase (1:8,000) were used to develop the system, and the bands were finally visualized by chemiluminescence in the Odyssey Fc system. CC = cervical cancer, GFP = green fluorescent protein, HPV = human papillomavirus, VLPs-L1 = virus-like particles from L1 protein.
    Streptavidin Horseradish Peroxidase, supplied by Roche, used in various techniques. Bioz Stars score: 92/100, based on 33 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Genzyme streptavidin horseradish peroxidase
    Seropositivity to E4, E7, and VLPs-L1 in serum of healthy women and women with CC by Slot blot system. In vitro purified HPV antigens were immobilized in PROTRAN membranes using the Hybri-Slot system, and membranes were fixed and blocked as described in “Materials and Methods.” Strips containing the 3 HPV16 antigens (E4 10 ng, E7 10 ng, VLPs-L1 200 ng) and negative controls (buffer alone and GFP 200 ng) were incubated with dilutions (1:2,500) of sera from women with CC (A), sera from healthy women (B), and positive and negative female serum controls for anti-HPV antibodies (C). Biotinylated secondary antibody (dil 1:10,000) and <t>Streptavidin-horseradish</t> peroxidase (1:8,000) were used to develop the system, and the bands were finally visualized by chemiluminescence in the Odyssey Fc system. CC = cervical cancer, GFP = green fluorescent protein, HPV = human papillomavirus, VLPs-L1 = virus-like particles from L1 protein.
    Streptavidin Horseradish Peroxidase, supplied by Genzyme, used in various techniques. Bioz Stars score: 92/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    GE Healthcare streptavidin horseradish peroxidase
    Coimmunoprecipitation of HA-SH3p4 and Flag-β1-adrenergic receptor from HEK293 cells. pcDNA3 Flag-β1-AR ( Left ) or pcDNA3 Flag-β2-AR ( Right ) were transiently transfected into HEK293 cells in the absence or presence of pcDNA3 HA-SH3p4 or pcDNA3 HA-SH3p4 ΔSH3. Nonstimulated cells and cells stimulated with 10 μM isoproterenol for various periods of time were lysed in digitonin buffer. Flag-β1-AR was immunoprecipitated with M2 anti-Flag affinity gel from samples containing equal amounts of protein. Immunoprecipitates were subjected to SDS/PAGE and Western blot analysis. The blot was initially probed with anti-HA rabbit polyclonal antibody to detect HA-SH3p4 and HA-SH3p4 ΔSH3. The blot was subsequently stripped and reprobed with biotinylated-M2 anti-Flag antibody and <t>streptavidin/horseradish</t> peroxidase conjugates to detect Flag-βAR. Overexpression of HA-SH3p4 or HA-SH3p4ΔSH3 in whole cell lysate also was monitored. The experiment was repeated at least three times with similar results. The diffuse doublet of both Flag-β1-AR and Flag-β2-AR in the middle panel likely represents differentially glycosylated forms of these receptors.
    Streptavidin Horseradish Peroxidase, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 93/100, based on 713 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    SouthernBiotech streptavidin horseradish peroxidase
    Deletion of the ER retention signal in CD3ɛ is sufficient to allow surface expression of the TCR complex in ζ-deficient T cells. (A) Surface expression of TCR complexes in ζ-expressing and ζ-deficient T cells. The parental murine T cell hybridoma 2B4 and its ζ-deficient MA5.8 mutant were stably transfected with either wild-type human CD3ɛ or with human ɛmut. Cells were double stained with the anti-murine TCRβ antibody H57-597 and the anti–human CD3 antibody Leu4 and analyzed by two-color flow cytometry (top). Representative clones for each condition are shown. The result of single staining with anti–human CD3ɛ antibody SK7 of intact or detergent-permeabilized cells is shown in the middle and bottom rows. (B) The ER retention mutant of CD3ɛ is expressed at the cell surface within a TCR complex. The human CD3ɛ-transfected clones were surface biotinylated and immunoprecipitated with Leu4 from Brij96 detergent lysates. The immunoprecipitates were resolved by two-dimensional nonreducing/reducing SDS-PAGE and immunoblotted with <t>streptavidin-peroxidase.</t> The positions of human and murine TCR and CD3 chains are indicated.
    Streptavidin Horseradish Peroxidase, supplied by SouthernBiotech, used in various techniques. Bioz Stars score: 92/100, based on 160 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    NEN Life Science streptavidin horseradish peroxidase
    Deletion of the ER retention signal in CD3ɛ is sufficient to allow surface expression of the TCR complex in ζ-deficient T cells. (A) Surface expression of TCR complexes in ζ-expressing and ζ-deficient T cells. The parental murine T cell hybridoma 2B4 and its ζ-deficient MA5.8 mutant were stably transfected with either wild-type human CD3ɛ or with human ɛmut. Cells were double stained with the anti-murine TCRβ antibody H57-597 and the anti–human CD3 antibody Leu4 and analyzed by two-color flow cytometry (top). Representative clones for each condition are shown. The result of single staining with anti–human CD3ɛ antibody SK7 of intact or detergent-permeabilized cells is shown in the middle and bottom rows. (B) The ER retention mutant of CD3ɛ is expressed at the cell surface within a TCR complex. The human CD3ɛ-transfected clones were surface biotinylated and immunoprecipitated with Leu4 from Brij96 detergent lysates. The immunoprecipitates were resolved by two-dimensional nonreducing/reducing SDS-PAGE and immunoblotted with <t>streptavidin-peroxidase.</t> The positions of human and murine TCR and CD3 chains are indicated.
    Streptavidin Horseradish Peroxidase, supplied by NEN Life Science, used in various techniques. Bioz Stars score: 92/100, based on 61 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Mab Technologies streptavidin horseradish peroxidase
    IL-1β-induced C/EBPδ binding to a κB site is inhibited by Aβ . A) Representative western blot of C/EBPδ after <t>streptavidin-agarose</t> pull-down using biotinylated κB oligonucleotides. Primary astro-microglial cells were exposed to oligomer- or fibril-enriched preparations of Aβ (10 μM, oAβ or fAβ) in combination with IL-1β (10 ng/ml) for 3 h. κB oligonucleotides without biotin were used as a control for unspecific binding. B) Relative levels of C/EBPδ binding to the κB site showing that IL-1β induces a significant increase that is inhibited after Aβ exposure. The data represent mean ± SEM for three independent experiments. *p
    Streptavidin Horseradish Peroxidase, supplied by Mab Technologies, used in various techniques. Bioz Stars score: 92/100, based on 124 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Pharmingen streptavidin horseradish peroxidase
    IL-1β-induced C/EBPδ binding to a κB site is inhibited by Aβ . A) Representative western blot of C/EBPδ after <t>streptavidin-agarose</t> pull-down using biotinylated κB oligonucleotides. Primary astro-microglial cells were exposed to oligomer- or fibril-enriched preparations of Aβ (10 μM, oAβ or fAβ) in combination with IL-1β (10 ng/ml) for 3 h. κB oligonucleotides without biotin were used as a control for unspecific binding. B) Relative levels of C/EBPδ binding to the κB site showing that IL-1β induces a significant increase that is inhibited after Aβ exposure. The data represent mean ± SEM for three independent experiments. *p
    Streptavidin Horseradish Peroxidase, supplied by Pharmingen, used in various techniques. Bioz Stars score: 92/100, based on 60 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Rockland Immunochemicals streptavidin horseradish peroxidase
    IL-1β-induced C/EBPδ binding to a κB site is inhibited by Aβ . A) Representative western blot of C/EBPδ after <t>streptavidin-agarose</t> pull-down using biotinylated κB oligonucleotides. Primary astro-microglial cells were exposed to oligomer- or fibril-enriched preparations of Aβ (10 μM, oAβ or fAβ) in combination with IL-1β (10 ng/ml) for 3 h. κB oligonucleotides without biotin were used as a control for unspecific binding. B) Relative levels of C/EBPδ binding to the κB site showing that IL-1β induces a significant increase that is inhibited after Aβ exposure. The data represent mean ± SEM for three independent experiments. *p
    Streptavidin Horseradish Peroxidase, supplied by Rockland Immunochemicals, used in various techniques. Bioz Stars score: 92/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Sanquin streptavidin horseradish peroxidase
    IL-1β-induced C/EBPδ binding to a κB site is inhibited by Aβ . A) Representative western blot of C/EBPδ after <t>streptavidin-agarose</t> pull-down using biotinylated κB oligonucleotides. Primary astro-microglial cells were exposed to oligomer- or fibril-enriched preparations of Aβ (10 μM, oAβ or fAβ) in combination with IL-1β (10 ng/ml) for 3 h. κB oligonucleotides without biotin were used as a control for unspecific binding. B) Relative levels of C/EBPδ binding to the κB site showing that IL-1β induces a significant increase that is inhibited after Aβ exposure. The data represent mean ± SEM for three independent experiments. *p
    Streptavidin Horseradish Peroxidase, supplied by Sanquin, used in various techniques. Bioz Stars score: 92/100, based on 28 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Bio-Rad streptavidin horseradish peroxidase
    The HUL-1 E3 encoded by ICP0 exon 3 promotes its own ubiquitylation as well as that of cdc34 in vitro . ( A ) In vitro ubiquitylation reactions containing GST or the indicated GST fusion protein, the master mix, recombinant cdc34, ATP, and the ATP-regenerating system were separated by SDS/PAGE and probed with <t>streptavidin.</t> Dots to the right of bands indicate polyubiquitylated species that are specifically present or augmented in reactions containing GST-exon 3 or GST-680. ( B ) GST or GST-fusion proteins were precipitated from reaction mixtures with glutathione Sepharose beads. Precipitates were separated as above and probed with streptavidin. Dots to the right of bands indicate ubiquitylated GST-exon 3 or GST-680. ( C ) Purified GST-exon 3 (lane 9) or reaction mixtures containing GST or the indicated GST fusion protein (lanes 10–13) were electophoretically separated and probed with Ab against GST. Reactive bands were detected by ECL. ( D ) GST and GST-fusion proteins were precipitated from reactions as above. Precipitates (lanes 18–21) and total reaction mixtures (lanes 14–17) were separated as above and probed with Ab against cdc34. Cdc34 was visualized by ECL. ( E ) GST and GST-fusion proteins were precipitated as above. Precipitates (lanes 26–29) and total reaction mixtures (lanes 22–25) were separated and probed with Ab against GST. Bands reacting with the Ab were detected with BCIP/NBT.
    Streptavidin Horseradish Peroxidase, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 92/100, based on 56 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Biogenex streptavidin horseradish peroxidase
    The HUL-1 E3 encoded by ICP0 exon 3 promotes its own ubiquitylation as well as that of cdc34 in vitro . ( A ) In vitro ubiquitylation reactions containing GST or the indicated GST fusion protein, the master mix, recombinant cdc34, ATP, and the ATP-regenerating system were separated by SDS/PAGE and probed with <t>streptavidin.</t> Dots to the right of bands indicate polyubiquitylated species that are specifically present or augmented in reactions containing GST-exon 3 or GST-680. ( B ) GST or GST-fusion proteins were precipitated from reaction mixtures with glutathione Sepharose beads. Precipitates were separated as above and probed with streptavidin. Dots to the right of bands indicate ubiquitylated GST-exon 3 or GST-680. ( C ) Purified GST-exon 3 (lane 9) or reaction mixtures containing GST or the indicated GST fusion protein (lanes 10–13) were electophoretically separated and probed with Ab against GST. Reactive bands were detected by ECL. ( D ) GST and GST-fusion proteins were precipitated from reactions as above. Precipitates (lanes 18–21) and total reaction mixtures (lanes 14–17) were separated as above and probed with Ab against cdc34. Cdc34 was visualized by ECL. ( E ) GST and GST-fusion proteins were precipitated as above. Precipitates (lanes 26–29) and total reaction mixtures (lanes 22–25) were separated and probed with Ab against GST. Bands reacting with the Ab were detected with BCIP/NBT.
    Streptavidin Horseradish Peroxidase, supplied by Biogenex, used in various techniques. Bioz Stars score: 92/100, based on 63 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Bio-Synthesis Inc streptavidin horseradish peroxidase
    The HUL-1 E3 encoded by ICP0 exon 3 promotes its own ubiquitylation as well as that of cdc34 in vitro . ( A ) In vitro ubiquitylation reactions containing GST or the indicated GST fusion protein, the master mix, recombinant cdc34, ATP, and the ATP-regenerating system were separated by SDS/PAGE and probed with <t>streptavidin.</t> Dots to the right of bands indicate polyubiquitylated species that are specifically present or augmented in reactions containing GST-exon 3 or GST-680. ( B ) GST or GST-fusion proteins were precipitated from reaction mixtures with glutathione Sepharose beads. Precipitates were separated as above and probed with streptavidin. Dots to the right of bands indicate ubiquitylated GST-exon 3 or GST-680. ( C ) Purified GST-exon 3 (lane 9) or reaction mixtures containing GST or the indicated GST fusion protein (lanes 10–13) were electophoretically separated and probed with Ab against GST. Reactive bands were detected by ECL. ( D ) GST and GST-fusion proteins were precipitated from reactions as above. Precipitates (lanes 18–21) and total reaction mixtures (lanes 14–17) were separated as above and probed with Ab against cdc34. Cdc34 was visualized by ECL. ( E ) GST and GST-fusion proteins were precipitated as above. Precipitates (lanes 26–29) and total reaction mixtures (lanes 22–25) were separated and probed with Ab against GST. Bands reacting with the Ab were detected with BCIP/NBT.
    Streptavidin Horseradish Peroxidase, supplied by Bio-Synthesis Inc, used in various techniques. Bioz Stars score: 93/100, based on 30 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ScyTek streptavidin horseradish peroxidase
    The HUL-1 E3 encoded by ICP0 exon 3 promotes its own ubiquitylation as well as that of cdc34 in vitro . ( A ) In vitro ubiquitylation reactions containing GST or the indicated GST fusion protein, the master mix, recombinant cdc34, ATP, and the ATP-regenerating system were separated by SDS/PAGE and probed with <t>streptavidin.</t> Dots to the right of bands indicate polyubiquitylated species that are specifically present or augmented in reactions containing GST-exon 3 or GST-680. ( B ) GST or GST-fusion proteins were precipitated from reaction mixtures with glutathione Sepharose beads. Precipitates were separated as above and probed with streptavidin. Dots to the right of bands indicate ubiquitylated GST-exon 3 or GST-680. ( C ) Purified GST-exon 3 (lane 9) or reaction mixtures containing GST or the indicated GST fusion protein (lanes 10–13) were electophoretically separated and probed with Ab against GST. Reactive bands were detected by ECL. ( D ) GST and GST-fusion proteins were precipitated from reactions as above. Precipitates (lanes 18–21) and total reaction mixtures (lanes 14–17) were separated as above and probed with Ab against cdc34. Cdc34 was visualized by ECL. ( E ) GST and GST-fusion proteins were precipitated as above. Precipitates (lanes 26–29) and total reaction mixtures (lanes 22–25) were separated and probed with Ab against GST. Bands reacting with the Ab were detected with BCIP/NBT.
    Streptavidin Horseradish Peroxidase, supplied by ScyTek, used in various techniques. Bioz Stars score: 92/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    AMMP and ELISA target-binding assays. (a) Schematic of the AMMP target-binding assay. An HA-tagged ligand binds to target (Bcl-x L ) immobilized on streptavidin magnetic beads. Anti-HA antibody, labeled with fluorescein, binds to the HA tag and to antifluorescein antibody on the sensor surface. (b) AMMP signal in the target-binding assay is a function of dilution factor and ligand affinity. At the same dilution, Pep1 generates higher signal levels than Pep2, whereas ScPep1 and Pep1ΔHA show background levels of signal. (c) AMMP target-binding assay adjusted for peptide concentration as measured using the HA tag competition assay, demonstrating true relative affinities. (d) Schematic of the ELISA target-binding assay. An HA-tagged ligand binds to biotinylated target (Bcl-x L ) and anti-HA antibody on the ELISA plate. Streptavidin-HRP binds to biotin, resulting in an ELISA signal. (e) Target-binding ELISA assay is much less sensitive than the AMMP assay [described in (b)], and the respective samples behave equivalently: Pep1 generates a higher signal level than Pep2 and ScPep1 and Pep1ΔHA generate no signal over the background. (f) ELISA target-binding assay adjusted for peptide concentration as measured using the HA tag competition assay.

    Journal: Analytical Chemistry

    Article Title: Robust, Quantitative Analysis of Proteins using Peptide Immunoreagents, in Vitro Translation, and an Ultrasensitive Acoustic Resonant Sensor

    doi: 10.1021/ac500084d

    Figure Lengend Snippet: AMMP and ELISA target-binding assays. (a) Schematic of the AMMP target-binding assay. An HA-tagged ligand binds to target (Bcl-x L ) immobilized on streptavidin magnetic beads. Anti-HA antibody, labeled with fluorescein, binds to the HA tag and to antifluorescein antibody on the sensor surface. (b) AMMP signal in the target-binding assay is a function of dilution factor and ligand affinity. At the same dilution, Pep1 generates higher signal levels than Pep2, whereas ScPep1 and Pep1ΔHA show background levels of signal. (c) AMMP target-binding assay adjusted for peptide concentration as measured using the HA tag competition assay, demonstrating true relative affinities. (d) Schematic of the ELISA target-binding assay. An HA-tagged ligand binds to biotinylated target (Bcl-x L ) and anti-HA antibody on the ELISA plate. Streptavidin-HRP binds to biotin, resulting in an ELISA signal. (e) Target-binding ELISA assay is much less sensitive than the AMMP assay [described in (b)], and the respective samples behave equivalently: Pep1 generates a higher signal level than Pep2 and ScPep1 and Pep1ΔHA generate no signal over the background. (f) ELISA target-binding assay adjusted for peptide concentration as measured using the HA tag competition assay.

    Article Snippet: Plates were washed with wash buffer [1× PBS + 0.1% (v/v) Tween-20] and blocked with 1× PBS + 5% (w/v) BSA for 2 h. In each well, 100 μL of sample and 100 μL of 33 nM biotinylated Bcl-xL were added and incubated for 4 h. Plates were washed, incubated with streptavidin horseradish peroxidase conjugate (Strep-HRP, Thermo Scientific) for 1 h, washed, and incubated with TMB substrate (Thermo Scientific).

    Techniques: Enzyme-linked Immunosorbent Assay, Binding Assay, Magnetic Beads, Labeling, Concentration Assay, Competitive Binding Assay

    Missorted surface proteins accumulate in the sortase mutant AR01. A. Wild type S . pyogenes D471, sortase mutant AR01, complemented AR01+pAR107, and a passaged AR01 variant, were diluted from overnight cultures 1:100 into fresh media (containing spectinomycin for AR01+pAR107), grown to log phase, fixed, attached to glass cover slides, and permeabilized with PlyC. The cells were blocked and incubated with pentaglycine-biotin (5G-biotin) in the presence or absence of purified S . aureus sortase A. The slides were washed, and pentaglycine-biotins molecules (attached to LPXTG motifs by sortase) were detected using FITC-streptavidin. DAPI was used to visualize DNA. The scale bar represents 1 μm. Note that expression of sortase from pAR107 is lower than the wild type, explaining the presence of intact LPXTG motifs. B. The cell wall fraction of log-phase D471 cells (solubilized with PlyC in PBS 30% raffinose) was separated by SDS-PAGE. Duplicate gels were stained with GelCode blue or processed for Western blot using the 10B6 monoclonal antibody. The most prominent bands on the stained gel correspond to M protein.

    Journal: PLoS ONE

    Article Title: Streptococcus pyogenes Sortase Mutants Are Highly Susceptible to Killing by Host Factors Due to Aberrant Envelope Physiology

    doi: 10.1371/journal.pone.0140784

    Figure Lengend Snippet: Missorted surface proteins accumulate in the sortase mutant AR01. A. Wild type S . pyogenes D471, sortase mutant AR01, complemented AR01+pAR107, and a passaged AR01 variant, were diluted from overnight cultures 1:100 into fresh media (containing spectinomycin for AR01+pAR107), grown to log phase, fixed, attached to glass cover slides, and permeabilized with PlyC. The cells were blocked and incubated with pentaglycine-biotin (5G-biotin) in the presence or absence of purified S . aureus sortase A. The slides were washed, and pentaglycine-biotins molecules (attached to LPXTG motifs by sortase) were detected using FITC-streptavidin. DAPI was used to visualize DNA. The scale bar represents 1 μm. Note that expression of sortase from pAR107 is lower than the wild type, explaining the presence of intact LPXTG motifs. B. The cell wall fraction of log-phase D471 cells (solubilized with PlyC in PBS 30% raffinose) was separated by SDS-PAGE. Duplicate gels were stained with GelCode blue or processed for Western blot using the 10B6 monoclonal antibody. The most prominent bands on the stained gel correspond to M protein.

    Article Snippet: Biotinylated goat anti-rabbit antibody (Sigma) was used at a 1:5000 dilution, and streptavidin horseradish peroxidase conjugate (Sigma) was used at a 1:5000 dilution.

    Techniques: Mutagenesis, Variant Assay, Incubation, Purification, Expressing, SDS Page, Staining, Western Blot

    Expression of protocadherins. GFP was electroporated alone or in combination with protocadherins into K562 cells. a Immunoblotting of cell lysates with anti-GFP shows bands compatible with the expected molecular weights for GFP (27 kDa) and mature PCDHB11-GFP (110 kDa); image representative of three transfections. b Immunoblotting of cell lysates with anti-HA shows bands compatible with the expected molecular weights for mature HA-PCDHB11-GFP (113 kDa) and HA-PCDHGA3 (99 kDa); image representative of two transfections. c Proportion of medium and large clusters was lower in HA-PCDHB11-GFP-transfected than in HA-PCDHGA3-transfected cells, but higher than in control cells ( n = 10-12 images per condition). d Proportion of medium to large cell clusters when normalized by HA-PCDHGA3. For visualization of surface protocadherins, live cells transfected with GFP alone (e) or in combination with HA-PCDHB11-GFP (f) or HA-PCDHGA3 (g) were stained with anti-HA-biotin and streptavidin-Alexa555, then fixed. Blue: DAPI. Green: GFP. Red: surface HA-tagged protocadherins. Scale bar: 10 μm

    Journal: BMC Evolutionary Biology

    Article Title: Functional test of PCDHB11, the most human-specific neuronal surface protein

    doi: 10.1186/s12862-016-0652-x

    Figure Lengend Snippet: Expression of protocadherins. GFP was electroporated alone or in combination with protocadherins into K562 cells. a Immunoblotting of cell lysates with anti-GFP shows bands compatible with the expected molecular weights for GFP (27 kDa) and mature PCDHB11-GFP (110 kDa); image representative of three transfections. b Immunoblotting of cell lysates with anti-HA shows bands compatible with the expected molecular weights for mature HA-PCDHB11-GFP (113 kDa) and HA-PCDHGA3 (99 kDa); image representative of two transfections. c Proportion of medium and large clusters was lower in HA-PCDHB11-GFP-transfected than in HA-PCDHGA3-transfected cells, but higher than in control cells ( n = 10-12 images per condition). d Proportion of medium to large cell clusters when normalized by HA-PCDHGA3. For visualization of surface protocadherins, live cells transfected with GFP alone (e) or in combination with HA-PCDHB11-GFP (f) or HA-PCDHGA3 (g) were stained with anti-HA-biotin and streptavidin-Alexa555, then fixed. Blue: DAPI. Green: GFP. Red: surface HA-tagged protocadherins. Scale bar: 10 μm

    Article Snippet: For GFP detection, membranes were incubated with a rabbit polyclonal antibody (Life Technologies, A-11122) diluted 1:2000 in 50 mM Tris, 100 mM NaCl, 0.1 % Tween 20, pH 7.4, with 3 % bovine serum albumine (Sigma, St. Louis, MO) and a horse-radish peroxidase-conjugated anti-rabbit secondary antibody (Invitrogen, Waltham, MA), while for HA revelation, they were incubated with biotinylated 3 F10 rat monoclonal antibody (Roche Life Science, Indianapolis, IN) diluted 1:500 in the same buffer, and streptavidin-horseradish peroxidase (Invitrogen, Waltham, MA).

    Techniques: Expressing, Transfection, Staining

    sCD127 binding to IL-7. A : sCD127 was immobilized on a high-binding polystyrene surface to detect binding of biotinylated IL-7 by colorimetric determination with streptavidin-HRP as shown schematically. B : IL-7 binding (optical density, y -axis) over an IL-7 concentration range from 0.125–2,048 ng/mL ( x -axis) to sCD127 (100 ng/mL; circles), sCD132 (1 ng/mL; diamonds), and sCD127 + sCD132 (100 ng/mL + 1 ng/mL; squares). Error bars represent mean ± SD from n = 3 experiments. AU, arbitrary units.

    Journal: Diabetes

    Article Title: Concentration and Activity of the Soluble Form of the Interleukin-7 Receptor ? in Type 1 Diabetes Identifies an Interplay Between Hyperglycemia and Immune Function

    doi: 10.2337/db12-1726

    Figure Lengend Snippet: sCD127 binding to IL-7. A : sCD127 was immobilized on a high-binding polystyrene surface to detect binding of biotinylated IL-7 by colorimetric determination with streptavidin-HRP as shown schematically. B : IL-7 binding (optical density, y -axis) over an IL-7 concentration range from 0.125–2,048 ng/mL ( x -axis) to sCD127 (100 ng/mL; circles), sCD132 (1 ng/mL; diamonds), and sCD127 + sCD132 (100 ng/mL + 1 ng/mL; squares). Error bars represent mean ± SD from n = 3 experiments. AU, arbitrary units.

    Article Snippet: High-binding polystyrene 96-well plates were coated overnight with sCD127 (100 ng/mL; R & D Systems) and/or sCD132 (1 ng/mL; R & D Systems) in PBS, washed, blocked with PBS-2% BSA, and incubated with increasing concentrations (0.125–2,048 pg/mL) of biotinylated IL-7 (R & D Systems) for 2 h. Detection of bound IL-7 was performed by incubation of plates with streptavidin-horseradish peroxidase (HRP; R & D Systems) followed by addition of tetramethylbenzidine substrate solution (R & D Systems) and colorimetric determination of sCD127-bound IL-7.

    Techniques: Binding Assay, Concentration Assay

    Binding analysis of various sialylated PA–glycan conjugates to wild-type compared with siglec mutant B cells. Results are representative of three independent experiments. (A–E) B cells of the indicated genotypes were stained with biotinylated PA conjugated with the following glycans: (A) NeuAcα2-6Galβ1-4GlcNAc, (B) NeuGc, (C) bNeuGc, (D) NeuAcα2-3Galβ1-4GlcNAc, and (E), NeuGcα2-3Galβ1-4GlcNAc. Binding was revealed using fluorescent streptavidin. Background staining by streptavidin alone is shown in gray. (F) Chemical structures of the NeuGc-containing sialosides.

    Journal: The Journal of Experimental Medicine

    Article Title: Decoration of T-independent antigen with ligands for CD22 and Siglec-G can suppress immunity and induce B cell tolerance in vivo

    doi: 10.1084/jem.20091873

    Figure Lengend Snippet: Binding analysis of various sialylated PA–glycan conjugates to wild-type compared with siglec mutant B cells. Results are representative of three independent experiments. (A–E) B cells of the indicated genotypes were stained with biotinylated PA conjugated with the following glycans: (A) NeuAcα2-6Galβ1-4GlcNAc, (B) NeuGc, (C) bNeuGc, (D) NeuAcα2-3Galβ1-4GlcNAc, and (E), NeuGcα2-3Galβ1-4GlcNAc. Binding was revealed using fluorescent streptavidin. Background staining by streptavidin alone is shown in gray. (F) Chemical structures of the NeuGc-containing sialosides.

    Article Snippet: For detection, biotinylated rat anti–mouse IgM (clone M41) and IgG3 (BD) antibodies were used at 0.25 µg/ml, followed by streptavidin–horseradish peroxidase (HRP; BD), diluted in ELISA buffer.

    Techniques: Binding Assay, Mutagenesis, Staining

    Seropositivity to E4, E7, and VLPs-L1 in serum of healthy women and women with CC by Slot blot system. In vitro purified HPV antigens were immobilized in PROTRAN membranes using the Hybri-Slot system, and membranes were fixed and blocked as described in “Materials and Methods.” Strips containing the 3 HPV16 antigens (E4 10 ng, E7 10 ng, VLPs-L1 200 ng) and negative controls (buffer alone and GFP 200 ng) were incubated with dilutions (1:2,500) of sera from women with CC (A), sera from healthy women (B), and positive and negative female serum controls for anti-HPV antibodies (C). Biotinylated secondary antibody (dil 1:10,000) and Streptavidin-horseradish peroxidase (1:8,000) were used to develop the system, and the bands were finally visualized by chemiluminescence in the Odyssey Fc system. CC = cervical cancer, GFP = green fluorescent protein, HPV = human papillomavirus, VLPs-L1 = virus-like particles from L1 protein.

    Journal: Medicine

    Article Title: Validation of Serological Antibody Profiles Against Human Papillomavirus Type 16 Antigens as Markers for Early Detection of Cervical Cancer

    doi: 10.1097/MD.0000000000002769

    Figure Lengend Snippet: Seropositivity to E4, E7, and VLPs-L1 in serum of healthy women and women with CC by Slot blot system. In vitro purified HPV antigens were immobilized in PROTRAN membranes using the Hybri-Slot system, and membranes were fixed and blocked as described in “Materials and Methods.” Strips containing the 3 HPV16 antigens (E4 10 ng, E7 10 ng, VLPs-L1 200 ng) and negative controls (buffer alone and GFP 200 ng) were incubated with dilutions (1:2,500) of sera from women with CC (A), sera from healthy women (B), and positive and negative female serum controls for anti-HPV antibodies (C). Biotinylated secondary antibody (dil 1:10,000) and Streptavidin-horseradish peroxidase (1:8,000) were used to develop the system, and the bands were finally visualized by chemiluminescence in the Odyssey Fc system. CC = cervical cancer, GFP = green fluorescent protein, HPV = human papillomavirus, VLPs-L1 = virus-like particles from L1 protein.

    Article Snippet: To develop the system, Streptavidin-horseradish peroxidase (DAKO, Germany) diluted in PBS-0.05% Tween 20 was incubated at 4o C for 1.5 hours, and it was visualized by chemiluminescence in the Odyssey Fc system.

    Techniques: Dot Blot, In Vitro, Purification, Incubation

    Coimmunoprecipitation of HA-SH3p4 and Flag-β1-adrenergic receptor from HEK293 cells. pcDNA3 Flag-β1-AR ( Left ) or pcDNA3 Flag-β2-AR ( Right ) were transiently transfected into HEK293 cells in the absence or presence of pcDNA3 HA-SH3p4 or pcDNA3 HA-SH3p4 ΔSH3. Nonstimulated cells and cells stimulated with 10 μM isoproterenol for various periods of time were lysed in digitonin buffer. Flag-β1-AR was immunoprecipitated with M2 anti-Flag affinity gel from samples containing equal amounts of protein. Immunoprecipitates were subjected to SDS/PAGE and Western blot analysis. The blot was initially probed with anti-HA rabbit polyclonal antibody to detect HA-SH3p4 and HA-SH3p4 ΔSH3. The blot was subsequently stripped and reprobed with biotinylated-M2 anti-Flag antibody and streptavidin/horseradish peroxidase conjugates to detect Flag-βAR. Overexpression of HA-SH3p4 or HA-SH3p4ΔSH3 in whole cell lysate also was monitored. The experiment was repeated at least three times with similar results. The diffuse doublet of both Flag-β1-AR and Flag-β2-AR in the middle panel likely represents differentially glycosylated forms of these receptors.

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

    Article Title: Identification of the endophilins (SH3p4/p8/p13) as novel binding partners for the ?1-adrenergic receptor

    doi:

    Figure Lengend Snippet: Coimmunoprecipitation of HA-SH3p4 and Flag-β1-adrenergic receptor from HEK293 cells. pcDNA3 Flag-β1-AR ( Left ) or pcDNA3 Flag-β2-AR ( Right ) were transiently transfected into HEK293 cells in the absence or presence of pcDNA3 HA-SH3p4 or pcDNA3 HA-SH3p4 ΔSH3. Nonstimulated cells and cells stimulated with 10 μM isoproterenol for various periods of time were lysed in digitonin buffer. Flag-β1-AR was immunoprecipitated with M2 anti-Flag affinity gel from samples containing equal amounts of protein. Immunoprecipitates were subjected to SDS/PAGE and Western blot analysis. The blot was initially probed with anti-HA rabbit polyclonal antibody to detect HA-SH3p4 and HA-SH3p4 ΔSH3. The blot was subsequently stripped and reprobed with biotinylated-M2 anti-Flag antibody and streptavidin/horseradish peroxidase conjugates to detect Flag-βAR. Overexpression of HA-SH3p4 or HA-SH3p4ΔSH3 in whole cell lysate also was monitored. The experiment was repeated at least three times with similar results. The diffuse doublet of both Flag-β1-AR and Flag-β2-AR in the middle panel likely represents differentially glycosylated forms of these receptors.

    Article Snippet: Streptavidin horseradish peroxidase, anti-mouse horseradish peroxidase, and anti-rabbit horseradish peroxidase were obtained from Amersham Pharmacia.

    Techniques: Transfection, Immunoprecipitation, SDS Page, Western Blot, Over Expression

    Deletion of the ER retention signal in CD3ɛ is sufficient to allow surface expression of the TCR complex in ζ-deficient T cells. (A) Surface expression of TCR complexes in ζ-expressing and ζ-deficient T cells. The parental murine T cell hybridoma 2B4 and its ζ-deficient MA5.8 mutant were stably transfected with either wild-type human CD3ɛ or with human ɛmut. Cells were double stained with the anti-murine TCRβ antibody H57-597 and the anti–human CD3 antibody Leu4 and analyzed by two-color flow cytometry (top). Representative clones for each condition are shown. The result of single staining with anti–human CD3ɛ antibody SK7 of intact or detergent-permeabilized cells is shown in the middle and bottom rows. (B) The ER retention mutant of CD3ɛ is expressed at the cell surface within a TCR complex. The human CD3ɛ-transfected clones were surface biotinylated and immunoprecipitated with Leu4 from Brij96 detergent lysates. The immunoprecipitates were resolved by two-dimensional nonreducing/reducing SDS-PAGE and immunoblotted with streptavidin-peroxidase. The positions of human and murine TCR and CD3 chains are indicated.

    Journal: The Journal of Experimental Medicine

    Article Title: An orderly inactivation of intracellular retention signals controls surface expression of the T cell antigen receptor

    doi: 10.1084/jem.20041133

    Figure Lengend Snippet: Deletion of the ER retention signal in CD3ɛ is sufficient to allow surface expression of the TCR complex in ζ-deficient T cells. (A) Surface expression of TCR complexes in ζ-expressing and ζ-deficient T cells. The parental murine T cell hybridoma 2B4 and its ζ-deficient MA5.8 mutant were stably transfected with either wild-type human CD3ɛ or with human ɛmut. Cells were double stained with the anti-murine TCRβ antibody H57-597 and the anti–human CD3 antibody Leu4 and analyzed by two-color flow cytometry (top). Representative clones for each condition are shown. The result of single staining with anti–human CD3ɛ antibody SK7 of intact or detergent-permeabilized cells is shown in the middle and bottom rows. (B) The ER retention mutant of CD3ɛ is expressed at the cell surface within a TCR complex. The human CD3ɛ-transfected clones were surface biotinylated and immunoprecipitated with Leu4 from Brij96 detergent lysates. The immunoprecipitates were resolved by two-dimensional nonreducing/reducing SDS-PAGE and immunoblotted with streptavidin-peroxidase. The positions of human and murine TCR and CD3 chains are indicated.

    Article Snippet: Protein G was added and immunoprecipitates were subjected to two-dimensional SDS-PAGE (first dimension under nonreducing and second dimension under reducing conditions), immunotransferred to a nitrocellulose membrane, hybridized with streptavidin horseradish peroxidase (Southern Biotechnology Associates, Inc.), and developed by ECL (Bio-Rad Laboratories).

    Techniques: Expressing, Mutagenesis, Stable Transfection, Transfection, Staining, Flow Cytometry, Cytometry, Clone Assay, Immunoprecipitation, SDS Page

    IL-1β-induced C/EBPδ binding to a κB site is inhibited by Aβ . A) Representative western blot of C/EBPδ after streptavidin-agarose pull-down using biotinylated κB oligonucleotides. Primary astro-microglial cells were exposed to oligomer- or fibril-enriched preparations of Aβ (10 μM, oAβ or fAβ) in combination with IL-1β (10 ng/ml) for 3 h. κB oligonucleotides without biotin were used as a control for unspecific binding. B) Relative levels of C/EBPδ binding to the κB site showing that IL-1β induces a significant increase that is inhibited after Aβ exposure. The data represent mean ± SEM for three independent experiments. *p

    Journal: Journal of Neuroinflammation

    Article Title: The CCAAT/enhancer binding protein (C/EBP) ? is differently regulated by fibrillar and oligomeric forms of the Alzheimer amyloid-? peptide

    doi: 10.1186/1742-2094-8-34

    Figure Lengend Snippet: IL-1β-induced C/EBPδ binding to a κB site is inhibited by Aβ . A) Representative western blot of C/EBPδ after streptavidin-agarose pull-down using biotinylated κB oligonucleotides. Primary astro-microglial cells were exposed to oligomer- or fibril-enriched preparations of Aβ (10 μM, oAβ or fAβ) in combination with IL-1β (10 ng/ml) for 3 h. κB oligonucleotides without biotin were used as a control for unspecific binding. B) Relative levels of C/EBPδ binding to the κB site showing that IL-1β induces a significant increase that is inhibited after Aβ exposure. The data represent mean ± SEM for three independent experiments. *p

    Article Snippet: The biotinylated detection antibody as well as streptavidin-horseradish peroxidase (SA-HRP; diluted 1:2000; Mabtech, Nacka, Sweden) was allowed to incubate for 1 h in successive steps.

    Techniques: Binding Assay, Western Blot

    The HUL-1 E3 encoded by ICP0 exon 3 promotes its own ubiquitylation as well as that of cdc34 in vitro . ( A ) In vitro ubiquitylation reactions containing GST or the indicated GST fusion protein, the master mix, recombinant cdc34, ATP, and the ATP-regenerating system were separated by SDS/PAGE and probed with streptavidin. Dots to the right of bands indicate polyubiquitylated species that are specifically present or augmented in reactions containing GST-exon 3 or GST-680. ( B ) GST or GST-fusion proteins were precipitated from reaction mixtures with glutathione Sepharose beads. Precipitates were separated as above and probed with streptavidin. Dots to the right of bands indicate ubiquitylated GST-exon 3 or GST-680. ( C ) Purified GST-exon 3 (lane 9) or reaction mixtures containing GST or the indicated GST fusion protein (lanes 10–13) were electophoretically separated and probed with Ab against GST. Reactive bands were detected by ECL. ( D ) GST and GST-fusion proteins were precipitated from reactions as above. Precipitates (lanes 18–21) and total reaction mixtures (lanes 14–17) were separated as above and probed with Ab against cdc34. Cdc34 was visualized by ECL. ( E ) GST and GST-fusion proteins were precipitated as above. Precipitates (lanes 26–29) and total reaction mixtures (lanes 22–25) were separated and probed with Ab against GST. Bands reacting with the Ab were detected with BCIP/NBT.

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

    Article Title: Characterization of the novel E3 ubiquitin ligase encoded in exon 3 of herpes simplex virus-1-infected cell protein 0

    doi: 10.1073/pnas.122246999

    Figure Lengend Snippet: The HUL-1 E3 encoded by ICP0 exon 3 promotes its own ubiquitylation as well as that of cdc34 in vitro . ( A ) In vitro ubiquitylation reactions containing GST or the indicated GST fusion protein, the master mix, recombinant cdc34, ATP, and the ATP-regenerating system were separated by SDS/PAGE and probed with streptavidin. Dots to the right of bands indicate polyubiquitylated species that are specifically present or augmented in reactions containing GST-exon 3 or GST-680. ( B ) GST or GST-fusion proteins were precipitated from reaction mixtures with glutathione Sepharose beads. Precipitates were separated as above and probed with streptavidin. Dots to the right of bands indicate ubiquitylated GST-exon 3 or GST-680. ( C ) Purified GST-exon 3 (lane 9) or reaction mixtures containing GST or the indicated GST fusion protein (lanes 10–13) were electophoretically separated and probed with Ab against GST. Reactive bands were detected by ECL. ( D ) GST and GST-fusion proteins were precipitated from reactions as above. Precipitates (lanes 18–21) and total reaction mixtures (lanes 14–17) were separated as above and probed with Ab against cdc34. Cdc34 was visualized by ECL. ( E ) GST and GST-fusion proteins were precipitated as above. Precipitates (lanes 26–29) and total reaction mixtures (lanes 22–25) were separated and probed with Ab against GST. Bands reacting with the Ab were detected with BCIP/NBT.

    Article Snippet: Biotinylated Ub was detected with streptavidin-horseradish peroxidase (Bio-Rad) at a dilution of 1:1,000.

    Techniques: In Vitro, Recombinant, SDS Page, Purification

    Analysis of HUL-1 E3 ligase function. ( A ) GST (lanes 1 and 2), GST-exon 3 (lanes 3, 4, and 7), GST-680. (lane 5), GST-615 (lane 6), or no additional protein were added to the in vitro ubiquitylation reaction master mix (MM) containing recombinant E1, biotinylated Ub, and ubiquitylation buffer in the presence and absence of recombinant cdc34 and ATP and the ATP-regenerating system as indicated. Reaction mixtures were electrophoretically separated in a denaturing polyacrylamide gel and probed with streptavidin. Dots to the right of bands indicate polyubiquitylated species that are specifically present or augmented in reactions containing GST-exon 3 or GST-680. ( B ) Electrophoretically separated reaction mixtures containing GST (lanes 9 and 10), the indicated ICP0 chimeric protein (lanes 11–15) in addition to the master mix, or the master mix alone (lane 16) along with the indicated reaction components were probed with an Ab against GST. Reactive bands were detected with BCIP/NBT. All procedures in this and other figure legends were as described in Materials and Methods .

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

    Article Title: Characterization of the novel E3 ubiquitin ligase encoded in exon 3 of herpes simplex virus-1-infected cell protein 0

    doi: 10.1073/pnas.122246999

    Figure Lengend Snippet: Analysis of HUL-1 E3 ligase function. ( A ) GST (lanes 1 and 2), GST-exon 3 (lanes 3, 4, and 7), GST-680. (lane 5), GST-615 (lane 6), or no additional protein were added to the in vitro ubiquitylation reaction master mix (MM) containing recombinant E1, biotinylated Ub, and ubiquitylation buffer in the presence and absence of recombinant cdc34 and ATP and the ATP-regenerating system as indicated. Reaction mixtures were electrophoretically separated in a denaturing polyacrylamide gel and probed with streptavidin. Dots to the right of bands indicate polyubiquitylated species that are specifically present or augmented in reactions containing GST-exon 3 or GST-680. ( B ) Electrophoretically separated reaction mixtures containing GST (lanes 9 and 10), the indicated ICP0 chimeric protein (lanes 11–15) in addition to the master mix, or the master mix alone (lane 16) along with the indicated reaction components were probed with an Ab against GST. Reactive bands were detected with BCIP/NBT. All procedures in this and other figure legends were as described in Materials and Methods .

    Article Snippet: Biotinylated Ub was detected with streptavidin-horseradish peroxidase (Bio-Rad) at a dilution of 1:1,000.

    Techniques: In Vitro, Recombinant