hrp conjugate Search Results


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  • 95
    Qiagen ni nta hrp
    Internalization of functional <t>HRP</t> by Tat13-ST and R 9 -ST. (A) Analysis of enzymatic HRP activities upon internalization of His 6 - Strep -tag II complexed with <t>Ni-NTA-HRP</t> or biotin-HRP, by the indicated Transtactins. Cells treated with either ST alone, or Ni-NTA-HRP complexed with His 6 - Strep -tag II, or biotin-HRP, showed no HRP activities (data not shown). (B) Absorbance was recalculated to the amount of both internalized HRP and total protein. Uptake results are expressed as pmol of HPR per mg of total protein.
    Ni Nta Hrp, supplied by Qiagen, used in various techniques. Bioz Stars score: 95/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ni nta hrp/product/Qiagen
    Average 95 stars, based on 14 article reviews
    Price from $9.99 to $1999.99
    ni nta hrp - by Bioz Stars, 2020-02
    95/100 stars
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    92
    Millipore hpr conjugated antibody
    Internalization of functional <t>HRP</t> by Tat13-ST and R 9 -ST. (A) Analysis of enzymatic HRP activities upon internalization of His 6 - Strep -tag II complexed with <t>Ni-NTA-HRP</t> or biotin-HRP, by the indicated Transtactins. Cells treated with either ST alone, or Ni-NTA-HRP complexed with His 6 - Strep -tag II, or biotin-HRP, showed no HRP activities (data not shown). (B) Absorbance was recalculated to the amount of both internalized HRP and total protein. Uptake results are expressed as pmol of HPR per mg of total protein.
    Hpr Conjugated Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hpr conjugated antibody/product/Millipore
    Average 92 stars, based on 9 article reviews
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    hpr conjugated antibody - by Bioz Stars, 2020-02
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    82
    GE Healthcare streptavidin hpr conjugate
    Internalization of functional <t>HRP</t> by Tat13-ST and R 9 -ST. (A) Analysis of enzymatic HRP activities upon internalization of His 6 - Strep -tag II complexed with <t>Ni-NTA-HRP</t> or biotin-HRP, by the indicated Transtactins. Cells treated with either ST alone, or Ni-NTA-HRP complexed with His 6 - Strep -tag II, or biotin-HRP, showed no HRP activities (data not shown). (B) Absorbance was recalculated to the amount of both internalized HRP and total protein. Uptake results are expressed as pmol of HPR per mg of total protein.
    Streptavidin Hpr Conjugate, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 82/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/streptavidin hpr conjugate/product/GE Healthcare
    Average 82 stars, based on 9 article reviews
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    streptavidin hpr conjugate - by Bioz Stars, 2020-02
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    79
    Thermo Fisher protein a hpr conjugate
    Internalization of functional <t>HRP</t> by Tat13-ST and R 9 -ST. (A) Analysis of enzymatic HRP activities upon internalization of His 6 - Strep -tag II complexed with <t>Ni-NTA-HRP</t> or biotin-HRP, by the indicated Transtactins. Cells treated with either ST alone, or Ni-NTA-HRP complexed with His 6 - Strep -tag II, or biotin-HRP, showed no HRP activities (data not shown). (B) Absorbance was recalculated to the amount of both internalized HRP and total protein. Uptake results are expressed as pmol of HPR per mg of total protein.
    Protein A Hpr Conjugate, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 79/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/protein a hpr conjugate/product/Thermo Fisher
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    77
    Thermo Fisher hrp conjugated polyclonal secondary antibody
    Internalization of functional <t>HRP</t> by Tat13-ST and R 9 -ST. (A) Analysis of enzymatic HRP activities upon internalization of His 6 - Strep -tag II complexed with <t>Ni-NTA-HRP</t> or biotin-HRP, by the indicated Transtactins. Cells treated with either ST alone, or Ni-NTA-HRP complexed with His 6 - Strep -tag II, or biotin-HRP, showed no HRP activities (data not shown). (B) Absorbance was recalculated to the amount of both internalized HRP and total protein. Uptake results are expressed as pmol of HPR per mg of total protein.
    Hrp Conjugated Polyclonal Secondary Antibody, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 77/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    77
    GE Healthcare anti gst hpr conjugate
    Internalization of functional <t>HRP</t> by Tat13-ST and R 9 -ST. (A) Analysis of enzymatic HRP activities upon internalization of His 6 - Strep -tag II complexed with <t>Ni-NTA-HRP</t> or biotin-HRP, by the indicated Transtactins. Cells treated with either ST alone, or Ni-NTA-HRP complexed with His 6 - Strep -tag II, or biotin-HRP, showed no HRP activities (data not shown). (B) Absorbance was recalculated to the amount of both internalized HRP and total protein. Uptake results are expressed as pmol of HPR per mg of total protein.
    Anti Gst Hpr Conjugate, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 77/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti gst hpr conjugate/product/GE Healthcare
    Average 77 stars, based on 4 article reviews
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    82
    GE Healthcare hrp conjugated secondary hpr conjugated ab
    Internalization of functional <t>HRP</t> by Tat13-ST and R 9 -ST. (A) Analysis of enzymatic HRP activities upon internalization of His 6 - Strep -tag II complexed with <t>Ni-NTA-HRP</t> or biotin-HRP, by the indicated Transtactins. Cells treated with either ST alone, or Ni-NTA-HRP complexed with His 6 - Strep -tag II, or biotin-HRP, showed no HRP activities (data not shown). (B) Absorbance was recalculated to the amount of both internalized HRP and total protein. Uptake results are expressed as pmol of HPR per mg of total protein.
    Hrp Conjugated Secondary Hpr Conjugated Ab, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 82/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 82 stars, based on 10 article reviews
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    90
    PerkinElmer antifluorescein hrp
    Internalization of functional <t>HRP</t> by Tat13-ST and R 9 -ST. (A) Analysis of enzymatic HRP activities upon internalization of His 6 - Strep -tag II complexed with <t>Ni-NTA-HRP</t> or biotin-HRP, by the indicated Transtactins. Cells treated with either ST alone, or Ni-NTA-HRP complexed with His 6 - Strep -tag II, or biotin-HRP, showed no HRP activities (data not shown). (B) Absorbance was recalculated to the amount of both internalized HRP and total protein. Uptake results are expressed as pmol of HPR per mg of total protein.
    Antifluorescein Hrp, supplied by PerkinElmer, used in various techniques. Bioz Stars score: 90/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/antifluorescein hrp/product/PerkinElmer
    Average 90 stars, based on 16 article reviews
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    90
    Thermo Fisher hisprobe horseradish peroxidase
    3I14 blocks trypsin-mediated HA maturation and pH-dependent conformational changes. ( a ) Trypsin Cleavage Inhibition Assay. 0.4 μg recombinant H3-histidine (H3-BR07) was incubated in the presence of 2.5 μg 3I14 or Fm-6 IgG1, or in the absence of antibody in Tris-HCl buffer at pH 8.0 containing 2 μg ml −1 Trypsin at 37 °C. Trypsin digestion was stopped at several time-points by boiling the sample in a 100 °C water bath. Samples were run on 10% reduced SDS–PAGE and blotted using a <t>HisProbe-HRP</t> Abs. Data represent a representative experiment from three independent experiments. ( b ) 3I14 IgG1 prevented by low-pH triggered conformational rearrangements on the surface-expressed H3-A2/68 and H3-BR07. Upper panels show four various conformations of HA: uncleaved precursor (HA0, left); trypsin in neutral pH cleaved (mature HA, left middle); fusion pH cleaved (mature HA, right middle) and trimeric HA2 (HA2, right). The conformation rearrangements of surface-expressed H3 were detected by FACS staining of 3I14 (solid bars) and the head binding control mAb E730 (open bars). Binding is expressed as the percentage of binding to untreated HA (HA0). For this antibody inhibition assay, H3 was pretreated without mAb, with 3I14, or with control Ab, Fm-6 IgG1 before exposure of the cleaved HAs to pH 4.9. Data represent mean+s.d. of three independent experiments. SDS–PAGE, SDS–polyacrylamide electrophoresis.
    Hisprobe Horseradish Peroxidase, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hisprobe horseradish peroxidase/product/Thermo Fisher
    Average 90 stars, based on 15 article reviews
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    hisprobe horseradish peroxidase - by Bioz Stars, 2020-02
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    82
    Bangalore Genei hrp conjugates
    3I14 blocks trypsin-mediated HA maturation and pH-dependent conformational changes. ( a ) Trypsin Cleavage Inhibition Assay. 0.4 μg recombinant H3-histidine (H3-BR07) was incubated in the presence of 2.5 μg 3I14 or Fm-6 IgG1, or in the absence of antibody in Tris-HCl buffer at pH 8.0 containing 2 μg ml −1 Trypsin at 37 °C. Trypsin digestion was stopped at several time-points by boiling the sample in a 100 °C water bath. Samples were run on 10% reduced SDS–PAGE and blotted using a <t>HisProbe-HRP</t> Abs. Data represent a representative experiment from three independent experiments. ( b ) 3I14 IgG1 prevented by low-pH triggered conformational rearrangements on the surface-expressed H3-A2/68 and H3-BR07. Upper panels show four various conformations of HA: uncleaved precursor (HA0, left); trypsin in neutral pH cleaved (mature HA, left middle); fusion pH cleaved (mature HA, right middle) and trimeric HA2 (HA2, right). The conformation rearrangements of surface-expressed H3 were detected by FACS staining of 3I14 (solid bars) and the head binding control mAb E730 (open bars). Binding is expressed as the percentage of binding to untreated HA (HA0). For this antibody inhibition assay, H3 was pretreated without mAb, with 3I14, or with control Ab, Fm-6 IgG1 before exposure of the cleaved HAs to pH 4.9. Data represent mean+s.d. of three independent experiments. SDS–PAGE, SDS–polyacrylamide electrophoresis.
    Hrp Conjugates, supplied by Bangalore Genei, used in various techniques. Bioz Stars score: 82/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hrp conjugates/product/Bangalore Genei
    Average 82 stars, based on 1 article reviews
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    92
    Becton Dickinson hrp conjugate
    3I14 blocks trypsin-mediated HA maturation and pH-dependent conformational changes. ( a ) Trypsin Cleavage Inhibition Assay. 0.4 μg recombinant H3-histidine (H3-BR07) was incubated in the presence of 2.5 μg 3I14 or Fm-6 IgG1, or in the absence of antibody in Tris-HCl buffer at pH 8.0 containing 2 μg ml −1 Trypsin at 37 °C. Trypsin digestion was stopped at several time-points by boiling the sample in a 100 °C water bath. Samples were run on 10% reduced SDS–PAGE and blotted using a <t>HisProbe-HRP</t> Abs. Data represent a representative experiment from three independent experiments. ( b ) 3I14 IgG1 prevented by low-pH triggered conformational rearrangements on the surface-expressed H3-A2/68 and H3-BR07. Upper panels show four various conformations of HA: uncleaved precursor (HA0, left); trypsin in neutral pH cleaved (mature HA, left middle); fusion pH cleaved (mature HA, right middle) and trimeric HA2 (HA2, right). The conformation rearrangements of surface-expressed H3 were detected by FACS staining of 3I14 (solid bars) and the head binding control mAb E730 (open bars). Binding is expressed as the percentage of binding to untreated HA (HA0). For this antibody inhibition assay, H3 was pretreated without mAb, with 3I14, or with control Ab, Fm-6 IgG1 before exposure of the cleaved HAs to pH 4.9. Data represent mean+s.d. of three independent experiments. SDS–PAGE, SDS–polyacrylamide electrophoresis.
    Hrp Conjugate, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 92/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hrp conjugate/product/Becton Dickinson
    Average 92 stars, based on 11 article reviews
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    hrp conjugate - by Bioz Stars, 2020-02
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    84
    Jackson Immuno hrp conjugates
    3I14 blocks trypsin-mediated HA maturation and pH-dependent conformational changes. ( a ) Trypsin Cleavage Inhibition Assay. 0.4 μg recombinant H3-histidine (H3-BR07) was incubated in the presence of 2.5 μg 3I14 or Fm-6 IgG1, or in the absence of antibody in Tris-HCl buffer at pH 8.0 containing 2 μg ml −1 Trypsin at 37 °C. Trypsin digestion was stopped at several time-points by boiling the sample in a 100 °C water bath. Samples were run on 10% reduced SDS–PAGE and blotted using a <t>HisProbe-HRP</t> Abs. Data represent a representative experiment from three independent experiments. ( b ) 3I14 IgG1 prevented by low-pH triggered conformational rearrangements on the surface-expressed H3-A2/68 and H3-BR07. Upper panels show four various conformations of HA: uncleaved precursor (HA0, left); trypsin in neutral pH cleaved (mature HA, left middle); fusion pH cleaved (mature HA, right middle) and trimeric HA2 (HA2, right). The conformation rearrangements of surface-expressed H3 were detected by FACS staining of 3I14 (solid bars) and the head binding control mAb E730 (open bars). Binding is expressed as the percentage of binding to untreated HA (HA0). For this antibody inhibition assay, H3 was pretreated without mAb, with 3I14, or with control Ab, Fm-6 IgG1 before exposure of the cleaved HAs to pH 4.9. Data represent mean+s.d. of three independent experiments. SDS–PAGE, SDS–polyacrylamide electrophoresis.
    Hrp Conjugates, supplied by Jackson Immuno, used in various techniques. Bioz Stars score: 84/100, based on 47 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 84 stars, based on 47 article reviews
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    99
    Thermo Fisher hrp conjugate
    3I14 blocks trypsin-mediated HA maturation and pH-dependent conformational changes. ( a ) Trypsin Cleavage Inhibition Assay. 0.4 μg recombinant H3-histidine (H3-BR07) was incubated in the presence of 2.5 μg 3I14 or Fm-6 IgG1, or in the absence of antibody in Tris-HCl buffer at pH 8.0 containing 2 μg ml −1 Trypsin at 37 °C. Trypsin digestion was stopped at several time-points by boiling the sample in a 100 °C water bath. Samples were run on 10% reduced SDS–PAGE and blotted using a <t>HisProbe-HRP</t> Abs. Data represent a representative experiment from three independent experiments. ( b ) 3I14 IgG1 prevented by low-pH triggered conformational rearrangements on the surface-expressed H3-A2/68 and H3-BR07. Upper panels show four various conformations of HA: uncleaved precursor (HA0, left); trypsin in neutral pH cleaved (mature HA, left middle); fusion pH cleaved (mature HA, right middle) and trimeric HA2 (HA2, right). The conformation rearrangements of surface-expressed H3 were detected by FACS staining of 3I14 (solid bars) and the head binding control mAb E730 (open bars). Binding is expressed as the percentage of binding to untreated HA (HA0). For this antibody inhibition assay, H3 was pretreated without mAb, with 3I14, or with control Ab, Fm-6 IgG1 before exposure of the cleaved HAs to pH 4.9. Data represent mean+s.d. of three independent experiments. SDS–PAGE, SDS–polyacrylamide electrophoresis.
    Hrp Conjugate, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 278 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hrp conjugate/product/Thermo Fisher
    Average 99 stars, based on 278 article reviews
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    82
    Abcam hrp conjugates
    3I14 blocks trypsin-mediated HA maturation and pH-dependent conformational changes. ( a ) Trypsin Cleavage Inhibition Assay. 0.4 μg recombinant H3-histidine (H3-BR07) was incubated in the presence of 2.5 μg 3I14 or Fm-6 IgG1, or in the absence of antibody in Tris-HCl buffer at pH 8.0 containing 2 μg ml −1 Trypsin at 37 °C. Trypsin digestion was stopped at several time-points by boiling the sample in a 100 °C water bath. Samples were run on 10% reduced SDS–PAGE and blotted using a <t>HisProbe-HRP</t> Abs. Data represent a representative experiment from three independent experiments. ( b ) 3I14 IgG1 prevented by low-pH triggered conformational rearrangements on the surface-expressed H3-A2/68 and H3-BR07. Upper panels show four various conformations of HA: uncleaved precursor (HA0, left); trypsin in neutral pH cleaved (mature HA, left middle); fusion pH cleaved (mature HA, right middle) and trimeric HA2 (HA2, right). The conformation rearrangements of surface-expressed H3 were detected by FACS staining of 3I14 (solid bars) and the head binding control mAb E730 (open bars). Binding is expressed as the percentage of binding to untreated HA (HA0). For this antibody inhibition assay, H3 was pretreated without mAb, with 3I14, or with control Ab, Fm-6 IgG1 before exposure of the cleaved HAs to pH 4.9. Data represent mean+s.d. of three independent experiments. SDS–PAGE, SDS–polyacrylamide electrophoresis.
    Hrp Conjugates, supplied by Abcam, used in various techniques. Bioz Stars score: 82/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hrp conjugates/product/Abcam
    Average 82 stars, based on 1 article reviews
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    hrp conjugates - by Bioz Stars, 2020-02
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    86
    biomers.net hrp conjugates
    3I14 blocks trypsin-mediated HA maturation and pH-dependent conformational changes. ( a ) Trypsin Cleavage Inhibition Assay. 0.4 μg recombinant H3-histidine (H3-BR07) was incubated in the presence of 2.5 μg 3I14 or Fm-6 IgG1, or in the absence of antibody in Tris-HCl buffer at pH 8.0 containing 2 μg ml −1 Trypsin at 37 °C. Trypsin digestion was stopped at several time-points by boiling the sample in a 100 °C water bath. Samples were run on 10% reduced SDS–PAGE and blotted using a <t>HisProbe-HRP</t> Abs. Data represent a representative experiment from three independent experiments. ( b ) 3I14 IgG1 prevented by low-pH triggered conformational rearrangements on the surface-expressed H3-A2/68 and H3-BR07. Upper panels show four various conformations of HA: uncleaved precursor (HA0, left); trypsin in neutral pH cleaved (mature HA, left middle); fusion pH cleaved (mature HA, right middle) and trimeric HA2 (HA2, right). The conformation rearrangements of surface-expressed H3 were detected by FACS staining of 3I14 (solid bars) and the head binding control mAb E730 (open bars). Binding is expressed as the percentage of binding to untreated HA (HA0). For this antibody inhibition assay, H3 was pretreated without mAb, with 3I14, or with control Ab, Fm-6 IgG1 before exposure of the cleaved HAs to pH 4.9. Data represent mean+s.d. of three independent experiments. SDS–PAGE, SDS–polyacrylamide electrophoresis.
    Hrp Conjugates, supplied by biomers.net, used in various techniques. Bioz Stars score: 86/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 86 stars, based on 6 article reviews
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    94
    GE Healthcare hrp conjugate
    3I14 blocks trypsin-mediated HA maturation and pH-dependent conformational changes. ( a ) Trypsin Cleavage Inhibition Assay. 0.4 μg recombinant H3-histidine (H3-BR07) was incubated in the presence of 2.5 μg 3I14 or Fm-6 IgG1, or in the absence of antibody in Tris-HCl buffer at pH 8.0 containing 2 μg ml −1 Trypsin at 37 °C. Trypsin digestion was stopped at several time-points by boiling the sample in a 100 °C water bath. Samples were run on 10% reduced SDS–PAGE and blotted using a <t>HisProbe-HRP</t> Abs. Data represent a representative experiment from three independent experiments. ( b ) 3I14 IgG1 prevented by low-pH triggered conformational rearrangements on the surface-expressed H3-A2/68 and H3-BR07. Upper panels show four various conformations of HA: uncleaved precursor (HA0, left); trypsin in neutral pH cleaved (mature HA, left middle); fusion pH cleaved (mature HA, right middle) and trimeric HA2 (HA2, right). The conformation rearrangements of surface-expressed H3 were detected by FACS staining of 3I14 (solid bars) and the head binding control mAb E730 (open bars). Binding is expressed as the percentage of binding to untreated HA (HA0). For this antibody inhibition assay, H3 was pretreated without mAb, with 3I14, or with control Ab, Fm-6 IgG1 before exposure of the cleaved HAs to pH 4.9. Data represent mean+s.d. of three independent experiments. SDS–PAGE, SDS–polyacrylamide electrophoresis.
    Hrp Conjugate, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 94/100, based on 70 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 94 stars, based on 70 article reviews
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    92
    Medica Corporation hrp conjugate
    3I14 blocks trypsin-mediated HA maturation and pH-dependent conformational changes. ( a ) Trypsin Cleavage Inhibition Assay. 0.4 μg recombinant H3-histidine (H3-BR07) was incubated in the presence of 2.5 μg 3I14 or Fm-6 IgG1, or in the absence of antibody in Tris-HCl buffer at pH 8.0 containing 2 μg ml −1 Trypsin at 37 °C. Trypsin digestion was stopped at several time-points by boiling the sample in a 100 °C water bath. Samples were run on 10% reduced SDS–PAGE and blotted using a <t>HisProbe-HRP</t> Abs. Data represent a representative experiment from three independent experiments. ( b ) 3I14 IgG1 prevented by low-pH triggered conformational rearrangements on the surface-expressed H3-A2/68 and H3-BR07. Upper panels show four various conformations of HA: uncleaved precursor (HA0, left); trypsin in neutral pH cleaved (mature HA, left middle); fusion pH cleaved (mature HA, right middle) and trimeric HA2 (HA2, right). The conformation rearrangements of surface-expressed H3 were detected by FACS staining of 3I14 (solid bars) and the head binding control mAb E730 (open bars). Binding is expressed as the percentage of binding to untreated HA (HA0). For this antibody inhibition assay, H3 was pretreated without mAb, with 3I14, or with control Ab, Fm-6 IgG1 before exposure of the cleaved HAs to pH 4.9. Data represent mean+s.d. of three independent experiments. SDS–PAGE, SDS–polyacrylamide electrophoresis.
    Hrp Conjugate, supplied by Medica Corporation, used in various techniques. Bioz Stars score: 92/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hrp conjugate/product/Medica Corporation
    Average 92 stars, based on 5 article reviews
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    hrp conjugate - by Bioz Stars, 2020-02
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    94
    Promega hrp conjugate
    3I14 blocks trypsin-mediated HA maturation and pH-dependent conformational changes. ( a ) Trypsin Cleavage Inhibition Assay. 0.4 μg recombinant H3-histidine (H3-BR07) was incubated in the presence of 2.5 μg 3I14 or Fm-6 IgG1, or in the absence of antibody in Tris-HCl buffer at pH 8.0 containing 2 μg ml −1 Trypsin at 37 °C. Trypsin digestion was stopped at several time-points by boiling the sample in a 100 °C water bath. Samples were run on 10% reduced SDS–PAGE and blotted using a <t>HisProbe-HRP</t> Abs. Data represent a representative experiment from three independent experiments. ( b ) 3I14 IgG1 prevented by low-pH triggered conformational rearrangements on the surface-expressed H3-A2/68 and H3-BR07. Upper panels show four various conformations of HA: uncleaved precursor (HA0, left); trypsin in neutral pH cleaved (mature HA, left middle); fusion pH cleaved (mature HA, right middle) and trimeric HA2 (HA2, right). The conformation rearrangements of surface-expressed H3 were detected by FACS staining of 3I14 (solid bars) and the head binding control mAb E730 (open bars). Binding is expressed as the percentage of binding to untreated HA (HA0). For this antibody inhibition assay, H3 was pretreated without mAb, with 3I14, or with control Ab, Fm-6 IgG1 before exposure of the cleaved HAs to pH 4.9. Data represent mean+s.d. of three independent experiments. SDS–PAGE, SDS–polyacrylamide electrophoresis.
    Hrp Conjugate, supplied by Promega, used in various techniques. Bioz Stars score: 94/100, based on 80 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hrp conjugate/product/Promega
    Average 94 stars, based on 80 article reviews
    Price from $9.99 to $1999.99
    hrp conjugate - by Bioz Stars, 2020-02
    94/100 stars
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    93
    Boster Bio hrp conjugate
    3I14 blocks trypsin-mediated HA maturation and pH-dependent conformational changes. ( a ) Trypsin Cleavage Inhibition Assay. 0.4 μg recombinant H3-histidine (H3-BR07) was incubated in the presence of 2.5 μg 3I14 or Fm-6 IgG1, or in the absence of antibody in Tris-HCl buffer at pH 8.0 containing 2 μg ml −1 Trypsin at 37 °C. Trypsin digestion was stopped at several time-points by boiling the sample in a 100 °C water bath. Samples were run on 10% reduced SDS–PAGE and blotted using a <t>HisProbe-HRP</t> Abs. Data represent a representative experiment from three independent experiments. ( b ) 3I14 IgG1 prevented by low-pH triggered conformational rearrangements on the surface-expressed H3-A2/68 and H3-BR07. Upper panels show four various conformations of HA: uncleaved precursor (HA0, left); trypsin in neutral pH cleaved (mature HA, left middle); fusion pH cleaved (mature HA, right middle) and trimeric HA2 (HA2, right). The conformation rearrangements of surface-expressed H3 were detected by FACS staining of 3I14 (solid bars) and the head binding control mAb E730 (open bars). Binding is expressed as the percentage of binding to untreated HA (HA0). For this antibody inhibition assay, H3 was pretreated without mAb, with 3I14, or with control Ab, Fm-6 IgG1 before exposure of the cleaved HAs to pH 4.9. Data represent mean+s.d. of three independent experiments. SDS–PAGE, SDS–polyacrylamide electrophoresis.
    Hrp Conjugate, supplied by Boster Bio, used in various techniques. Bioz Stars score: 93/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hrp conjugate/product/Boster Bio
    Average 93 stars, based on 8 article reviews
    Price from $9.99 to $1999.99
    hrp conjugate - by Bioz Stars, 2020-02
    93/100 stars
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    82
    Cell Signaling Technology Inc hrp conjugates
    3I14 blocks trypsin-mediated HA maturation and pH-dependent conformational changes. ( a ) Trypsin Cleavage Inhibition Assay. 0.4 μg recombinant H3-histidine (H3-BR07) was incubated in the presence of 2.5 μg 3I14 or Fm-6 IgG1, or in the absence of antibody in Tris-HCl buffer at pH 8.0 containing 2 μg ml −1 Trypsin at 37 °C. Trypsin digestion was stopped at several time-points by boiling the sample in a 100 °C water bath. Samples were run on 10% reduced SDS–PAGE and blotted using a <t>HisProbe-HRP</t> Abs. Data represent a representative experiment from three independent experiments. ( b ) 3I14 IgG1 prevented by low-pH triggered conformational rearrangements on the surface-expressed H3-A2/68 and H3-BR07. Upper panels show four various conformations of HA: uncleaved precursor (HA0, left); trypsin in neutral pH cleaved (mature HA, left middle); fusion pH cleaved (mature HA, right middle) and trimeric HA2 (HA2, right). The conformation rearrangements of surface-expressed H3 were detected by FACS staining of 3I14 (solid bars) and the head binding control mAb E730 (open bars). Binding is expressed as the percentage of binding to untreated HA (HA0). For this antibody inhibition assay, H3 was pretreated without mAb, with 3I14, or with control Ab, Fm-6 IgG1 before exposure of the cleaved HAs to pH 4.9. Data represent mean+s.d. of three independent experiments. SDS–PAGE, SDS–polyacrylamide electrophoresis.
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    Roche hrp conjugate
    3I14 blocks trypsin-mediated HA maturation and pH-dependent conformational changes. ( a ) Trypsin Cleavage Inhibition Assay. 0.4 μg recombinant H3-histidine (H3-BR07) was incubated in the presence of 2.5 μg 3I14 or Fm-6 IgG1, or in the absence of antibody in Tris-HCl buffer at pH 8.0 containing 2 μg ml −1 Trypsin at 37 °C. Trypsin digestion was stopped at several time-points by boiling the sample in a 100 °C water bath. Samples were run on 10% reduced SDS–PAGE and blotted using a <t>HisProbe-HRP</t> Abs. Data represent a representative experiment from three independent experiments. ( b ) 3I14 IgG1 prevented by low-pH triggered conformational rearrangements on the surface-expressed H3-A2/68 and H3-BR07. Upper panels show four various conformations of HA: uncleaved precursor (HA0, left); trypsin in neutral pH cleaved (mature HA, left middle); fusion pH cleaved (mature HA, right middle) and trimeric HA2 (HA2, right). The conformation rearrangements of surface-expressed H3 were detected by FACS staining of 3I14 (solid bars) and the head binding control mAb E730 (open bars). Binding is expressed as the percentage of binding to untreated HA (HA0). For this antibody inhibition assay, H3 was pretreated without mAb, with 3I14, or with control Ab, Fm-6 IgG1 before exposure of the cleaved HAs to pH 4.9. Data represent mean+s.d. of three independent experiments. SDS–PAGE, SDS–polyacrylamide electrophoresis.
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    Cell Signaling Technology Inc hrp conjugate
    3I14 blocks trypsin-mediated HA maturation and pH-dependent conformational changes. ( a ) Trypsin Cleavage Inhibition Assay. 0.4 μg recombinant H3-histidine (H3-BR07) was incubated in the presence of 2.5 μg 3I14 or Fm-6 IgG1, or in the absence of antibody in Tris-HCl buffer at pH 8.0 containing 2 μg ml −1 Trypsin at 37 °C. Trypsin digestion was stopped at several time-points by boiling the sample in a 100 °C water bath. Samples were run on 10% reduced SDS–PAGE and blotted using a <t>HisProbe-HRP</t> Abs. Data represent a representative experiment from three independent experiments. ( b ) 3I14 IgG1 prevented by low-pH triggered conformational rearrangements on the surface-expressed H3-A2/68 and H3-BR07. Upper panels show four various conformations of HA: uncleaved precursor (HA0, left); trypsin in neutral pH cleaved (mature HA, left middle); fusion pH cleaved (mature HA, right middle) and trimeric HA2 (HA2, right). The conformation rearrangements of surface-expressed H3 were detected by FACS staining of 3I14 (solid bars) and the head binding control mAb E730 (open bars). Binding is expressed as the percentage of binding to untreated HA (HA0). For this antibody inhibition assay, H3 was pretreated without mAb, with 3I14, or with control Ab, Fm-6 IgG1 before exposure of the cleaved HAs to pH 4.9. Data represent mean+s.d. of three independent experiments. SDS–PAGE, SDS–polyacrylamide electrophoresis.
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    GE Healthcare hrp conjugates
    3I14 blocks trypsin-mediated HA maturation and pH-dependent conformational changes. ( a ) Trypsin Cleavage Inhibition Assay. 0.4 μg recombinant H3-histidine (H3-BR07) was incubated in the presence of 2.5 μg 3I14 or Fm-6 IgG1, or in the absence of antibody in Tris-HCl buffer at pH 8.0 containing 2 μg ml −1 Trypsin at 37 °C. Trypsin digestion was stopped at several time-points by boiling the sample in a 100 °C water bath. Samples were run on 10% reduced SDS–PAGE and blotted using a <t>HisProbe-HRP</t> Abs. Data represent a representative experiment from three independent experiments. ( b ) 3I14 IgG1 prevented by low-pH triggered conformational rearrangements on the surface-expressed H3-A2/68 and H3-BR07. Upper panels show four various conformations of HA: uncleaved precursor (HA0, left); trypsin in neutral pH cleaved (mature HA, left middle); fusion pH cleaved (mature HA, right middle) and trimeric HA2 (HA2, right). The conformation rearrangements of surface-expressed H3 were detected by FACS staining of 3I14 (solid bars) and the head binding control mAb E730 (open bars). Binding is expressed as the percentage of binding to untreated HA (HA0). For this antibody inhibition assay, H3 was pretreated without mAb, with 3I14, or with control Ab, Fm-6 IgG1 before exposure of the cleaved HAs to pH 4.9. Data represent mean+s.d. of three independent experiments. SDS–PAGE, SDS–polyacrylamide electrophoresis.
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    93
    Merck KGaA hrp conjugate
    3I14 blocks trypsin-mediated HA maturation and pH-dependent conformational changes. ( a ) Trypsin Cleavage Inhibition Assay. 0.4 μg recombinant H3-histidine (H3-BR07) was incubated in the presence of 2.5 μg 3I14 or Fm-6 IgG1, or in the absence of antibody in Tris-HCl buffer at pH 8.0 containing 2 μg ml −1 Trypsin at 37 °C. Trypsin digestion was stopped at several time-points by boiling the sample in a 100 °C water bath. Samples were run on 10% reduced SDS–PAGE and blotted using a <t>HisProbe-HRP</t> Abs. Data represent a representative experiment from three independent experiments. ( b ) 3I14 IgG1 prevented by low-pH triggered conformational rearrangements on the surface-expressed H3-A2/68 and H3-BR07. Upper panels show four various conformations of HA: uncleaved precursor (HA0, left); trypsin in neutral pH cleaved (mature HA, left middle); fusion pH cleaved (mature HA, right middle) and trimeric HA2 (HA2, right). The conformation rearrangements of surface-expressed H3 were detected by FACS staining of 3I14 (solid bars) and the head binding control mAb E730 (open bars). Binding is expressed as the percentage of binding to untreated HA (HA0). For this antibody inhibition assay, H3 was pretreated without mAb, with 3I14, or with control Ab, Fm-6 IgG1 before exposure of the cleaved HAs to pH 4.9. Data represent mean+s.d. of three independent experiments. SDS–PAGE, SDS–polyacrylamide electrophoresis.
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    Bio-Rad hrp conjugate
    3I14 blocks trypsin-mediated HA maturation and pH-dependent conformational changes. ( a ) Trypsin Cleavage Inhibition Assay. 0.4 μg recombinant H3-histidine (H3-BR07) was incubated in the presence of 2.5 μg 3I14 or Fm-6 IgG1, or in the absence of antibody in Tris-HCl buffer at pH 8.0 containing 2 μg ml −1 Trypsin at 37 °C. Trypsin digestion was stopped at several time-points by boiling the sample in a 100 °C water bath. Samples were run on 10% reduced SDS–PAGE and blotted using a <t>HisProbe-HRP</t> Abs. Data represent a representative experiment from three independent experiments. ( b ) 3I14 IgG1 prevented by low-pH triggered conformational rearrangements on the surface-expressed H3-A2/68 and H3-BR07. Upper panels show four various conformations of HA: uncleaved precursor (HA0, left); trypsin in neutral pH cleaved (mature HA, left middle); fusion pH cleaved (mature HA, right middle) and trimeric HA2 (HA2, right). The conformation rearrangements of surface-expressed H3 were detected by FACS staining of 3I14 (solid bars) and the head binding control mAb E730 (open bars). Binding is expressed as the percentage of binding to untreated HA (HA0). For this antibody inhibition assay, H3 was pretreated without mAb, with 3I14, or with control Ab, Fm-6 IgG1 before exposure of the cleaved HAs to pH 4.9. Data represent mean+s.d. of three independent experiments. SDS–PAGE, SDS–polyacrylamide electrophoresis.
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    Proteintech hrp conjugate
    3I14 blocks trypsin-mediated HA maturation and pH-dependent conformational changes. ( a ) Trypsin Cleavage Inhibition Assay. 0.4 μg recombinant H3-histidine (H3-BR07) was incubated in the presence of 2.5 μg 3I14 or Fm-6 IgG1, or in the absence of antibody in Tris-HCl buffer at pH 8.0 containing 2 μg ml −1 Trypsin at 37 °C. Trypsin digestion was stopped at several time-points by boiling the sample in a 100 °C water bath. Samples were run on 10% reduced SDS–PAGE and blotted using a <t>HisProbe-HRP</t> Abs. Data represent a representative experiment from three independent experiments. ( b ) 3I14 IgG1 prevented by low-pH triggered conformational rearrangements on the surface-expressed H3-A2/68 and H3-BR07. Upper panels show four various conformations of HA: uncleaved precursor (HA0, left); trypsin in neutral pH cleaved (mature HA, left middle); fusion pH cleaved (mature HA, right middle) and trimeric HA2 (HA2, right). The conformation rearrangements of surface-expressed H3 were detected by FACS staining of 3I14 (solid bars) and the head binding control mAb E730 (open bars). Binding is expressed as the percentage of binding to untreated HA (HA0). For this antibody inhibition assay, H3 was pretreated without mAb, with 3I14, or with control Ab, Fm-6 IgG1 before exposure of the cleaved HAs to pH 4.9. Data represent mean+s.d. of three independent experiments. SDS–PAGE, SDS–polyacrylamide electrophoresis.
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    Santa Cruz Biotechnology hrp conjugate
    3I14 blocks trypsin-mediated HA maturation and pH-dependent conformational changes. ( a ) Trypsin Cleavage Inhibition Assay. 0.4 μg recombinant H3-histidine (H3-BR07) was incubated in the presence of 2.5 μg 3I14 or Fm-6 IgG1, or in the absence of antibody in Tris-HCl buffer at pH 8.0 containing 2 μg ml −1 Trypsin at 37 °C. Trypsin digestion was stopped at several time-points by boiling the sample in a 100 °C water bath. Samples were run on 10% reduced SDS–PAGE and blotted using a <t>HisProbe-HRP</t> Abs. Data represent a representative experiment from three independent experiments. ( b ) 3I14 IgG1 prevented by low-pH triggered conformational rearrangements on the surface-expressed H3-A2/68 and H3-BR07. Upper panels show four various conformations of HA: uncleaved precursor (HA0, left); trypsin in neutral pH cleaved (mature HA, left middle); fusion pH cleaved (mature HA, right middle) and trimeric HA2 (HA2, right). The conformation rearrangements of surface-expressed H3 were detected by FACS staining of 3I14 (solid bars) and the head binding control mAb E730 (open bars). Binding is expressed as the percentage of binding to untreated HA (HA0). For this antibody inhibition assay, H3 was pretreated without mAb, with 3I14, or with control Ab, Fm-6 IgG1 before exposure of the cleaved HAs to pH 4.9. Data represent mean+s.d. of three independent experiments. SDS–PAGE, SDS–polyacrylamide electrophoresis.
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    Agilent technologies hrp conjugate
    3I14 blocks trypsin-mediated HA maturation and pH-dependent conformational changes. ( a ) Trypsin Cleavage Inhibition Assay. 0.4 μg recombinant H3-histidine (H3-BR07) was incubated in the presence of 2.5 μg 3I14 or Fm-6 IgG1, or in the absence of antibody in Tris-HCl buffer at pH 8.0 containing 2 μg ml −1 Trypsin at 37 °C. Trypsin digestion was stopped at several time-points by boiling the sample in a 100 °C water bath. Samples were run on 10% reduced SDS–PAGE and blotted using a <t>HisProbe-HRP</t> Abs. Data represent a representative experiment from three independent experiments. ( b ) 3I14 IgG1 prevented by low-pH triggered conformational rearrangements on the surface-expressed H3-A2/68 and H3-BR07. Upper panels show four various conformations of HA: uncleaved precursor (HA0, left); trypsin in neutral pH cleaved (mature HA, left middle); fusion pH cleaved (mature HA, right middle) and trimeric HA2 (HA2, right). The conformation rearrangements of surface-expressed H3 were detected by FACS staining of 3I14 (solid bars) and the head binding control mAb E730 (open bars). Binding is expressed as the percentage of binding to untreated HA (HA0). For this antibody inhibition assay, H3 was pretreated without mAb, with 3I14, or with control Ab, Fm-6 IgG1 before exposure of the cleaved HAs to pH 4.9. Data represent mean+s.d. of three independent experiments. SDS–PAGE, SDS–polyacrylamide electrophoresis.
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    Cell Signaling Technology Inc hpr conjugated secondary antibodies
    3I14 blocks trypsin-mediated HA maturation and pH-dependent conformational changes. ( a ) Trypsin Cleavage Inhibition Assay. 0.4 μg recombinant H3-histidine (H3-BR07) was incubated in the presence of 2.5 μg 3I14 or Fm-6 IgG1, or in the absence of antibody in Tris-HCl buffer at pH 8.0 containing 2 μg ml −1 Trypsin at 37 °C. Trypsin digestion was stopped at several time-points by boiling the sample in a 100 °C water bath. Samples were run on 10% reduced SDS–PAGE and blotted using a <t>HisProbe-HRP</t> Abs. Data represent a representative experiment from three independent experiments. ( b ) 3I14 IgG1 prevented by low-pH triggered conformational rearrangements on the surface-expressed H3-A2/68 and H3-BR07. Upper panels show four various conformations of HA: uncleaved precursor (HA0, left); trypsin in neutral pH cleaved (mature HA, left middle); fusion pH cleaved (mature HA, right middle) and trimeric HA2 (HA2, right). The conformation rearrangements of surface-expressed H3 were detected by FACS staining of 3I14 (solid bars) and the head binding control mAb E730 (open bars). Binding is expressed as the percentage of binding to untreated HA (HA0). For this antibody inhibition assay, H3 was pretreated without mAb, with 3I14, or with control Ab, Fm-6 IgG1 before exposure of the cleaved HAs to pH 4.9. Data represent mean+s.d. of three independent experiments. SDS–PAGE, SDS–polyacrylamide electrophoresis.
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    Agilent technologies hrp conjugates
    3I14 blocks trypsin-mediated HA maturation and pH-dependent conformational changes. ( a ) Trypsin Cleavage Inhibition Assay. 0.4 μg recombinant H3-histidine (H3-BR07) was incubated in the presence of 2.5 μg 3I14 or Fm-6 IgG1, or in the absence of antibody in Tris-HCl buffer at pH 8.0 containing 2 μg ml −1 Trypsin at 37 °C. Trypsin digestion was stopped at several time-points by boiling the sample in a 100 °C water bath. Samples were run on 10% reduced SDS–PAGE and blotted using a <t>HisProbe-HRP</t> Abs. Data represent a representative experiment from three independent experiments. ( b ) 3I14 IgG1 prevented by low-pH triggered conformational rearrangements on the surface-expressed H3-A2/68 and H3-BR07. Upper panels show four various conformations of HA: uncleaved precursor (HA0, left); trypsin in neutral pH cleaved (mature HA, left middle); fusion pH cleaved (mature HA, right middle) and trimeric HA2 (HA2, right). The conformation rearrangements of surface-expressed H3 were detected by FACS staining of 3I14 (solid bars) and the head binding control mAb E730 (open bars). Binding is expressed as the percentage of binding to untreated HA (HA0). For this antibody inhibition assay, H3 was pretreated without mAb, with 3I14, or with control Ab, Fm-6 IgG1 before exposure of the cleaved HAs to pH 4.9. Data represent mean+s.d. of three independent experiments. SDS–PAGE, SDS–polyacrylamide electrophoresis.
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    Image Search Results


    Internalization of functional HRP by Tat13-ST and R 9 -ST. (A) Analysis of enzymatic HRP activities upon internalization of His 6 - Strep -tag II complexed with Ni-NTA-HRP or biotin-HRP, by the indicated Transtactins. Cells treated with either ST alone, or Ni-NTA-HRP complexed with His 6 - Strep -tag II, or biotin-HRP, showed no HRP activities (data not shown). (B) Absorbance was recalculated to the amount of both internalized HRP and total protein. Uptake results are expressed as pmol of HPR per mg of total protein.

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: Transtactin: a universal transmembrane delivery system for Strep-tag II-fused cargos

    doi: 10.1111/j.1582-4934.2009.00846.x

    Figure Lengend Snippet: Internalization of functional HRP by Tat13-ST and R 9 -ST. (A) Analysis of enzymatic HRP activities upon internalization of His 6 - Strep -tag II complexed with Ni-NTA-HRP or biotin-HRP, by the indicated Transtactins. Cells treated with either ST alone, or Ni-NTA-HRP complexed with His 6 - Strep -tag II, or biotin-HRP, showed no HRP activities (data not shown). (B) Absorbance was recalculated to the amount of both internalized HRP and total protein. Uptake results are expressed as pmol of HPR per mg of total protein.

    Article Snippet: To this end, Tat13-ST or R9 -ST Transtactins were complexed with His6 -Strep -tag II and Ni-NTA-HRP.

    Techniques: Functional Assay, Strep-tag

    3I14 blocks trypsin-mediated HA maturation and pH-dependent conformational changes. ( a ) Trypsin Cleavage Inhibition Assay. 0.4 μg recombinant H3-histidine (H3-BR07) was incubated in the presence of 2.5 μg 3I14 or Fm-6 IgG1, or in the absence of antibody in Tris-HCl buffer at pH 8.0 containing 2 μg ml −1 Trypsin at 37 °C. Trypsin digestion was stopped at several time-points by boiling the sample in a 100 °C water bath. Samples were run on 10% reduced SDS–PAGE and blotted using a HisProbe-HRP Abs. Data represent a representative experiment from three independent experiments. ( b ) 3I14 IgG1 prevented by low-pH triggered conformational rearrangements on the surface-expressed H3-A2/68 and H3-BR07. Upper panels show four various conformations of HA: uncleaved precursor (HA0, left); trypsin in neutral pH cleaved (mature HA, left middle); fusion pH cleaved (mature HA, right middle) and trimeric HA2 (HA2, right). The conformation rearrangements of surface-expressed H3 were detected by FACS staining of 3I14 (solid bars) and the head binding control mAb E730 (open bars). Binding is expressed as the percentage of binding to untreated HA (HA0). For this antibody inhibition assay, H3 was pretreated without mAb, with 3I14, or with control Ab, Fm-6 IgG1 before exposure of the cleaved HAs to pH 4.9. Data represent mean+s.d. of three independent experiments. SDS–PAGE, SDS–polyacrylamide electrophoresis.

    Journal: Nature Communications

    Article Title: A broadly neutralizing anti-influenza antibody reveals ongoing capacity of haemagglutinin-specific memory B cells to evolve

    doi: 10.1038/ncomms12780

    Figure Lengend Snippet: 3I14 blocks trypsin-mediated HA maturation and pH-dependent conformational changes. ( a ) Trypsin Cleavage Inhibition Assay. 0.4 μg recombinant H3-histidine (H3-BR07) was incubated in the presence of 2.5 μg 3I14 or Fm-6 IgG1, or in the absence of antibody in Tris-HCl buffer at pH 8.0 containing 2 μg ml −1 Trypsin at 37 °C. Trypsin digestion was stopped at several time-points by boiling the sample in a 100 °C water bath. Samples were run on 10% reduced SDS–PAGE and blotted using a HisProbe-HRP Abs. Data represent a representative experiment from three independent experiments. ( b ) 3I14 IgG1 prevented by low-pH triggered conformational rearrangements on the surface-expressed H3-A2/68 and H3-BR07. Upper panels show four various conformations of HA: uncleaved precursor (HA0, left); trypsin in neutral pH cleaved (mature HA, left middle); fusion pH cleaved (mature HA, right middle) and trimeric HA2 (HA2, right). The conformation rearrangements of surface-expressed H3 were detected by FACS staining of 3I14 (solid bars) and the head binding control mAb E730 (open bars). Binding is expressed as the percentage of binding to untreated HA (HA0). For this antibody inhibition assay, H3 was pretreated without mAb, with 3I14, or with control Ab, Fm-6 IgG1 before exposure of the cleaved HAs to pH 4.9. Data represent mean+s.d. of three independent experiments. SDS–PAGE, SDS–polyacrylamide electrophoresis.

    Article Snippet: Samples were run on 10% SDS–polyacrylamide electrophoresis gel under reducing conditions and blotted using a HisProbe-horseradish peroxidase and SuperSignal West HisProbe Kit (Pierce Biotechnology, Rockford, IL).

    Techniques: Inhibition, Recombinant, Incubation, SDS Page, FACS, Staining, Binding Assay, Electrophoresis