hrp conjugate Promega Search Results


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  • 79
    Promega promega anti mouse hrp conjugate
    Promega Anti Mouse Hrp Conjugate, supplied by Promega, used in various techniques. Bioz Stars score: 79/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Promega hrp conjugate
    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
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    93
    Promega hrp conjugated
    Characterisation and purification of the royal jelly (RJ) component responsible for elevated MMP-9 production. ( A ) Heat and proteinase K treatment was performed by incubation of water royal jelly extract (WRJE) at 100 °C for 5 min and incubation with 150 μg/ml proteinase K for 1 h at 40 °C followed by heating to 98 °C for 10 min to inactivate the enzyme. Treated WRJE was incubated with HaCaT cells and conditioned equal volumes of the culture media were collected and subjected to gelatine zymography. Densitometric quantification of MMP-9 activity in culture media is presented. ( B ) Heat-treated WRJE was fractionated by a reverse phase-high performance liquid chromatography (RP-HPLC) on a C18 column (250 × 4.6 mm, 5 μm) at a flow rate 0.3 ml/min, with elution using a 10–90% gradient of acetonitrile (containing 0.1% (v/v) trifluoroacetic acid) for 85 min. ( C ) The HPLC fractions were assayed for MMP-9 induction. ( D ) HPLC fractions with maximal MMP-9 activity (51 to 59 min) were used for identification of MMP-9 inducer and were subjected to 16.5% Tricine-SDS-PAGE gels. Defensin-1 (5.5 kDa) was detected by Western blotting using a rabbit polyclonal anti-honeybee defensin-1 antibody diluted 1:2000 in blocking buffer. Horseradish <t>peroxidise-conjugated</t> secondary antibodies were applied. (The gels/blots with indicated cropping lines are shown in Supplementary Fig. S3 ). White line in gel indicates the place where two gels were spliced together. Data are expressed as means and SEMs of three independent measurements. Asterisks indicate a significant difference from the untreated group, * P
    Hrp Conjugated, supplied by Promega, used in various techniques. Bioz Stars score: 93/100, based on 95 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Promega hrp conjugated antibody
    Characterisation and purification of the royal jelly (RJ) component responsible for elevated MMP-9 production. ( A ) Heat and proteinase K treatment was performed by incubation of water royal jelly extract (WRJE) at 100 °C for 5 min and incubation with 150 μg/ml proteinase K for 1 h at 40 °C followed by heating to 98 °C for 10 min to inactivate the enzyme. Treated WRJE was incubated with HaCaT cells and conditioned equal volumes of the culture media were collected and subjected to gelatine zymography. Densitometric quantification of MMP-9 activity in culture media is presented. ( B ) Heat-treated WRJE was fractionated by a reverse phase-high performance liquid chromatography (RP-HPLC) on a C18 column (250 × 4.6 mm, 5 μm) at a flow rate 0.3 ml/min, with elution using a 10–90% gradient of acetonitrile (containing 0.1% (v/v) trifluoroacetic acid) for 85 min. ( C ) The HPLC fractions were assayed for MMP-9 induction. ( D ) HPLC fractions with maximal MMP-9 activity (51 to 59 min) were used for identification of MMP-9 inducer and were subjected to 16.5% Tricine-SDS-PAGE gels. Defensin-1 (5.5 kDa) was detected by Western blotting using a rabbit polyclonal anti-honeybee defensin-1 antibody diluted 1:2000 in blocking buffer. Horseradish <t>peroxidise-conjugated</t> secondary antibodies were applied. (The gels/blots with indicated cropping lines are shown in Supplementary Fig. S3 ). White line in gel indicates the place where two gels were spliced together. Data are expressed as means and SEMs of three independent measurements. Asterisks indicate a significant difference from the untreated group, * P
    Hrp Conjugated Antibody, supplied by Promega, used in various techniques. Bioz Stars score: 89/100, based on 37 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    82
    Promega horseradish peroxidase hrp conjugate
    Characterisation and purification of the royal jelly (RJ) component responsible for elevated MMP-9 production. ( A ) Heat and proteinase K treatment was performed by incubation of water royal jelly extract (WRJE) at 100 °C for 5 min and incubation with 150 μg/ml proteinase K for 1 h at 40 °C followed by heating to 98 °C for 10 min to inactivate the enzyme. Treated WRJE was incubated with HaCaT cells and conditioned equal volumes of the culture media were collected and subjected to gelatine zymography. Densitometric quantification of MMP-9 activity in culture media is presented. ( B ) Heat-treated WRJE was fractionated by a reverse phase-high performance liquid chromatography (RP-HPLC) on a C18 column (250 × 4.6 mm, 5 μm) at a flow rate 0.3 ml/min, with elution using a 10–90% gradient of acetonitrile (containing 0.1% (v/v) trifluoroacetic acid) for 85 min. ( C ) The HPLC fractions were assayed for MMP-9 induction. ( D ) HPLC fractions with maximal MMP-9 activity (51 to 59 min) were used for identification of MMP-9 inducer and were subjected to 16.5% Tricine-SDS-PAGE gels. Defensin-1 (5.5 kDa) was detected by Western blotting using a rabbit polyclonal anti-honeybee defensin-1 antibody diluted 1:2000 in blocking buffer. Horseradish <t>peroxidise-conjugated</t> secondary antibodies were applied. (The gels/blots with indicated cropping lines are shown in Supplementary Fig. S3 ). White line in gel indicates the place where two gels were spliced together. Data are expressed as means and SEMs of three independent measurements. Asterisks indicate a significant difference from the untreated group, * P
    Horseradish Peroxidase Hrp Conjugate, supplied by Promega, used in various techniques. Bioz Stars score: 82/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Becton Dickinson hrp conjugated secondary antibody
    Characterisation and purification of the royal jelly (RJ) component responsible for elevated MMP-9 production. ( A ) Heat and proteinase K treatment was performed by incubation of water royal jelly extract (WRJE) at 100 °C for 5 min and incubation with 150 μg/ml proteinase K for 1 h at 40 °C followed by heating to 98 °C for 10 min to inactivate the enzyme. Treated WRJE was incubated with HaCaT cells and conditioned equal volumes of the culture media were collected and subjected to gelatine zymography. Densitometric quantification of MMP-9 activity in culture media is presented. ( B ) Heat-treated WRJE was fractionated by a reverse phase-high performance liquid chromatography (RP-HPLC) on a C18 column (250 × 4.6 mm, 5 μm) at a flow rate 0.3 ml/min, with elution using a 10–90% gradient of acetonitrile (containing 0.1% (v/v) trifluoroacetic acid) for 85 min. ( C ) The HPLC fractions were assayed for MMP-9 induction. ( D ) HPLC fractions with maximal MMP-9 activity (51 to 59 min) were used for identification of MMP-9 inducer and were subjected to 16.5% Tricine-SDS-PAGE gels. Defensin-1 (5.5 kDa) was detected by Western blotting using a rabbit polyclonal anti-honeybee defensin-1 antibody diluted 1:2000 in blocking buffer. Horseradish <t>peroxidise-conjugated</t> secondary antibodies were applied. (The gels/blots with indicated cropping lines are shown in Supplementary Fig. S3 ). White line in gel indicates the place where two gels were spliced together. Data are expressed as means and SEMs of three independent measurements. Asterisks indicate a significant difference from the untreated group, * P
    Hrp Conjugated Secondary Antibody, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 96/100, based on 49 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    84
    Promega anti rabbit hrp conjugate
    Characterisation and purification of the royal jelly (RJ) component responsible for elevated MMP-9 production. ( A ) Heat and proteinase K treatment was performed by incubation of water royal jelly extract (WRJE) at 100 °C for 5 min and incubation with 150 μg/ml proteinase K for 1 h at 40 °C followed by heating to 98 °C for 10 min to inactivate the enzyme. Treated WRJE was incubated with HaCaT cells and conditioned equal volumes of the culture media were collected and subjected to gelatine zymography. Densitometric quantification of MMP-9 activity in culture media is presented. ( B ) Heat-treated WRJE was fractionated by a reverse phase-high performance liquid chromatography (RP-HPLC) on a C18 column (250 × 4.6 mm, 5 μm) at a flow rate 0.3 ml/min, with elution using a 10–90% gradient of acetonitrile (containing 0.1% (v/v) trifluoroacetic acid) for 85 min. ( C ) The HPLC fractions were assayed for MMP-9 induction. ( D ) HPLC fractions with maximal MMP-9 activity (51 to 59 min) were used for identification of MMP-9 inducer and were subjected to 16.5% Tricine-SDS-PAGE gels. Defensin-1 (5.5 kDa) was detected by Western blotting using a rabbit polyclonal anti-honeybee defensin-1 antibody diluted 1:2000 in blocking buffer. Horseradish <t>peroxidise-conjugated</t> secondary antibodies were applied. (The gels/blots with indicated cropping lines are shown in Supplementary Fig. S3 ). White line in gel indicates the place where two gels were spliced together. Data are expressed as means and SEMs of three independent measurements. Asterisks indicate a significant difference from the untreated group, * P
    Anti Rabbit Hrp Conjugate, supplied by Promega, used in various techniques. Bioz Stars score: 84/100, based on 27 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    Promega anti human hrp conjugate
    Characterisation and purification of the royal jelly (RJ) component responsible for elevated MMP-9 production. ( A ) Heat and proteinase K treatment was performed by incubation of water royal jelly extract (WRJE) at 100 °C for 5 min and incubation with 150 μg/ml proteinase K for 1 h at 40 °C followed by heating to 98 °C for 10 min to inactivate the enzyme. Treated WRJE was incubated with HaCaT cells and conditioned equal volumes of the culture media were collected and subjected to gelatine zymography. Densitometric quantification of MMP-9 activity in culture media is presented. ( B ) Heat-treated WRJE was fractionated by a reverse phase-high performance liquid chromatography (RP-HPLC) on a C18 column (250 × 4.6 mm, 5 μm) at a flow rate 0.3 ml/min, with elution using a 10–90% gradient of acetonitrile (containing 0.1% (v/v) trifluoroacetic acid) for 85 min. ( C ) The HPLC fractions were assayed for MMP-9 induction. ( D ) HPLC fractions with maximal MMP-9 activity (51 to 59 min) were used for identification of MMP-9 inducer and were subjected to 16.5% Tricine-SDS-PAGE gels. Defensin-1 (5.5 kDa) was detected by Western blotting using a rabbit polyclonal anti-honeybee defensin-1 antibody diluted 1:2000 in blocking buffer. Horseradish <t>peroxidise-conjugated</t> secondary antibodies were applied. (The gels/blots with indicated cropping lines are shown in Supplementary Fig. S3 ). White line in gel indicates the place where two gels were spliced together. Data are expressed as means and SEMs of three independent measurements. Asterisks indicate a significant difference from the untreated group, * P
    Anti Human Hrp Conjugate, supplied by Promega, used in various techniques. Bioz Stars score: 78/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    80
    Promega anti rabbit hrp conjugates
    Characterisation and purification of the royal jelly (RJ) component responsible for elevated MMP-9 production. ( A ) Heat and proteinase K treatment was performed by incubation of water royal jelly extract (WRJE) at 100 °C for 5 min and incubation with 150 μg/ml proteinase K for 1 h at 40 °C followed by heating to 98 °C for 10 min to inactivate the enzyme. Treated WRJE was incubated with HaCaT cells and conditioned equal volumes of the culture media were collected and subjected to gelatine zymography. Densitometric quantification of MMP-9 activity in culture media is presented. ( B ) Heat-treated WRJE was fractionated by a reverse phase-high performance liquid chromatography (RP-HPLC) on a C18 column (250 × 4.6 mm, 5 μm) at a flow rate 0.3 ml/min, with elution using a 10–90% gradient of acetonitrile (containing 0.1% (v/v) trifluoroacetic acid) for 85 min. ( C ) The HPLC fractions were assayed for MMP-9 induction. ( D ) HPLC fractions with maximal MMP-9 activity (51 to 59 min) were used for identification of MMP-9 inducer and were subjected to 16.5% Tricine-SDS-PAGE gels. Defensin-1 (5.5 kDa) was detected by Western blotting using a rabbit polyclonal anti-honeybee defensin-1 antibody diluted 1:2000 in blocking buffer. Horseradish <t>peroxidise-conjugated</t> secondary antibodies were applied. (The gels/blots with indicated cropping lines are shown in Supplementary Fig. S3 ). White line in gel indicates the place where two gels were spliced together. Data are expressed as means and SEMs of three independent measurements. Asterisks indicate a significant difference from the untreated group, * P
    Anti Rabbit Hrp Conjugates, supplied by Promega, used in various techniques. Bioz Stars score: 80/100, based on 23 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Promega horseradish peroxidase hrp
    <t>GRFT</t> prevents HSV-2 and HPV postadsorption events. (A) HSV-2 G or HPV16 PsV and different concentrations of GRFT or medium (virus control) were preincubated for 0 h, 0.5 h, and 2 h at 37°C before being added to prechilled Vero cells (for HSV-2) or HeLa cells (for HPV16 PsV) and kept at 4°C for 2 h. The cells were washed 3 times before addition of the overlay and incubation at 48 h and 37°C in a 5% CO 2 atmosphere with 98% humidity. Finally, the cells were fixed and stained prior to counting the numbers of PFU. (B) The same as in panel A for HSV-2, but after 2 h of incubation at 4°C, the cells were switched to 37°C for an additional 2 h, followed by a 2-min treatment with citric acid buffer (pH 3.0). (C) Different concentrations of CG or GRFT were added at the indicated time points, with time zero representing the time of initial HPV16 PsV inoculation. The graph shows the percent reporter gene expression (mean ± SD) relative to that for the virus control (triplicate assays were performed per condition). (D) Western blot of purified HSV-2 lysate. Membranes were incubated overnight at 4°C with mouse anti-gD MAb DL11 (lane 1) or 1 μg/ml GRFT (lane 2). The membranes were washed and incubated for 1 h at room temperature with <t>HRP-conjugated</t> anti-mouse Ig (lane 1) or were incubated overnight at 4°C with rabbit anti-GRFT antibody (lane 2), before being washed and incubated with HRP-conjugated anti-rabbit immunoglobulin antibody (1 h at room temperature). (E) HSV-2-infected Vero cells were lysed, preincubated with GRFT, and immunoprecipitated with anti-GRFT antibody. Lanes 1, cell lysate without immunoprecipitation; lanes 2, HeLa cell lysate 24 h after HSV-2 infection with immunoprecipitation in the presence of GRFT and anti-GRFT antibody; lanes 3, same as lanes 2 but 48 h after HSV-2 infection; lanes 4 and 5, immunoprecipitation controls without and with GRFT, respectively. In the experiments described in the legends to panels D and E, the membranes were processed using an ECL Western blotting detection system to capture the bands on X-ray films. A representative blot of three repeats is shown. (F) Soluble GRFT, N-glycosylated (N-glyco), nonglycosylated gD, or a mixture of N-glycosylated and nonglycosylated gD-GRFT was preincubated before addition to Vero cells. HSV-2 G was then added, and infection was detected by an immunohistochemical assay after overnight incubation. Statistical analysis was performed using the Mann-Whitney U test ( P
    Horseradish Peroxidase Hrp, supplied by Promega, used in various techniques. Bioz Stars score: 96/100, based on 142 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Promega goat anti rabbit hrp conjugated
    <t>GRFT</t> prevents HSV-2 and HPV postadsorption events. (A) HSV-2 G or HPV16 PsV and different concentrations of GRFT or medium (virus control) were preincubated for 0 h, 0.5 h, and 2 h at 37°C before being added to prechilled Vero cells (for HSV-2) or HeLa cells (for HPV16 PsV) and kept at 4°C for 2 h. The cells were washed 3 times before addition of the overlay and incubation at 48 h and 37°C in a 5% CO 2 atmosphere with 98% humidity. Finally, the cells were fixed and stained prior to counting the numbers of PFU. (B) The same as in panel A for HSV-2, but after 2 h of incubation at 4°C, the cells were switched to 37°C for an additional 2 h, followed by a 2-min treatment with citric acid buffer (pH 3.0). (C) Different concentrations of CG or GRFT were added at the indicated time points, with time zero representing the time of initial HPV16 PsV inoculation. The graph shows the percent reporter gene expression (mean ± SD) relative to that for the virus control (triplicate assays were performed per condition). (D) Western blot of purified HSV-2 lysate. Membranes were incubated overnight at 4°C with mouse anti-gD MAb DL11 (lane 1) or 1 μg/ml GRFT (lane 2). The membranes were washed and incubated for 1 h at room temperature with <t>HRP-conjugated</t> anti-mouse Ig (lane 1) or were incubated overnight at 4°C with rabbit anti-GRFT antibody (lane 2), before being washed and incubated with HRP-conjugated anti-rabbit immunoglobulin antibody (1 h at room temperature). (E) HSV-2-infected Vero cells were lysed, preincubated with GRFT, and immunoprecipitated with anti-GRFT antibody. Lanes 1, cell lysate without immunoprecipitation; lanes 2, HeLa cell lysate 24 h after HSV-2 infection with immunoprecipitation in the presence of GRFT and anti-GRFT antibody; lanes 3, same as lanes 2 but 48 h after HSV-2 infection; lanes 4 and 5, immunoprecipitation controls without and with GRFT, respectively. In the experiments described in the legends to panels D and E, the membranes were processed using an ECL Western blotting detection system to capture the bands on X-ray films. A representative blot of three repeats is shown. (F) Soluble GRFT, N-glycosylated (N-glyco), nonglycosylated gD, or a mixture of N-glycosylated and nonglycosylated gD-GRFT was preincubated before addition to Vero cells. HSV-2 G was then added, and infection was detected by an immunohistochemical assay after overnight incubation. Statistical analysis was performed using the Mann-Whitney U test ( P
    Goat Anti Rabbit Hrp Conjugated, supplied by Promega, used in various techniques. Bioz Stars score: 89/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Promega hrp conjugated anti mouse
    <t>GRFT</t> prevents HSV-2 and HPV postadsorption events. (A) HSV-2 G or HPV16 PsV and different concentrations of GRFT or medium (virus control) were preincubated for 0 h, 0.5 h, and 2 h at 37°C before being added to prechilled Vero cells (for HSV-2) or HeLa cells (for HPV16 PsV) and kept at 4°C for 2 h. The cells were washed 3 times before addition of the overlay and incubation at 48 h and 37°C in a 5% CO 2 atmosphere with 98% humidity. Finally, the cells were fixed and stained prior to counting the numbers of PFU. (B) The same as in panel A for HSV-2, but after 2 h of incubation at 4°C, the cells were switched to 37°C for an additional 2 h, followed by a 2-min treatment with citric acid buffer (pH 3.0). (C) Different concentrations of CG or GRFT were added at the indicated time points, with time zero representing the time of initial HPV16 PsV inoculation. The graph shows the percent reporter gene expression (mean ± SD) relative to that for the virus control (triplicate assays were performed per condition). (D) Western blot of purified HSV-2 lysate. Membranes were incubated overnight at 4°C with mouse anti-gD MAb DL11 (lane 1) or 1 μg/ml GRFT (lane 2). The membranes were washed and incubated for 1 h at room temperature with <t>HRP-conjugated</t> anti-mouse Ig (lane 1) or were incubated overnight at 4°C with rabbit anti-GRFT antibody (lane 2), before being washed and incubated with HRP-conjugated anti-rabbit immunoglobulin antibody (1 h at room temperature). (E) HSV-2-infected Vero cells were lysed, preincubated with GRFT, and immunoprecipitated with anti-GRFT antibody. Lanes 1, cell lysate without immunoprecipitation; lanes 2, HeLa cell lysate 24 h after HSV-2 infection with immunoprecipitation in the presence of GRFT and anti-GRFT antibody; lanes 3, same as lanes 2 but 48 h after HSV-2 infection; lanes 4 and 5, immunoprecipitation controls without and with GRFT, respectively. In the experiments described in the legends to panels D and E, the membranes were processed using an ECL Western blotting detection system to capture the bands on X-ray films. A representative blot of three repeats is shown. (F) Soluble GRFT, N-glycosylated (N-glyco), nonglycosylated gD, or a mixture of N-glycosylated and nonglycosylated gD-GRFT was preincubated before addition to Vero cells. HSV-2 G was then added, and infection was detected by an immunohistochemical assay after overnight incubation. Statistical analysis was performed using the Mann-Whitney U test ( P
    Hrp Conjugated Anti Mouse, supplied by Promega, used in various techniques. Bioz Stars score: 93/100, based on 175 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Promega anti rabbit hrp conjugated
    <t>GRFT</t> prevents HSV-2 and HPV postadsorption events. (A) HSV-2 G or HPV16 PsV and different concentrations of GRFT or medium (virus control) were preincubated for 0 h, 0.5 h, and 2 h at 37°C before being added to prechilled Vero cells (for HSV-2) or HeLa cells (for HPV16 PsV) and kept at 4°C for 2 h. The cells were washed 3 times before addition of the overlay and incubation at 48 h and 37°C in a 5% CO 2 atmosphere with 98% humidity. Finally, the cells were fixed and stained prior to counting the numbers of PFU. (B) The same as in panel A for HSV-2, but after 2 h of incubation at 4°C, the cells were switched to 37°C for an additional 2 h, followed by a 2-min treatment with citric acid buffer (pH 3.0). (C) Different concentrations of CG or GRFT were added at the indicated time points, with time zero representing the time of initial HPV16 PsV inoculation. The graph shows the percent reporter gene expression (mean ± SD) relative to that for the virus control (triplicate assays were performed per condition). (D) Western blot of purified HSV-2 lysate. Membranes were incubated overnight at 4°C with mouse anti-gD MAb DL11 (lane 1) or 1 μg/ml GRFT (lane 2). The membranes were washed and incubated for 1 h at room temperature with <t>HRP-conjugated</t> anti-mouse Ig (lane 1) or were incubated overnight at 4°C with rabbit anti-GRFT antibody (lane 2), before being washed and incubated with HRP-conjugated anti-rabbit immunoglobulin antibody (1 h at room temperature). (E) HSV-2-infected Vero cells were lysed, preincubated with GRFT, and immunoprecipitated with anti-GRFT antibody. Lanes 1, cell lysate without immunoprecipitation; lanes 2, HeLa cell lysate 24 h after HSV-2 infection with immunoprecipitation in the presence of GRFT and anti-GRFT antibody; lanes 3, same as lanes 2 but 48 h after HSV-2 infection; lanes 4 and 5, immunoprecipitation controls without and with GRFT, respectively. In the experiments described in the legends to panels D and E, the membranes were processed using an ECL Western blotting detection system to capture the bands on X-ray films. A representative blot of three repeats is shown. (F) Soluble GRFT, N-glycosylated (N-glyco), nonglycosylated gD, or a mixture of N-glycosylated and nonglycosylated gD-GRFT was preincubated before addition to Vero cells. HSV-2 G was then added, and infection was detected by an immunohistochemical assay after overnight incubation. Statistical analysis was performed using the Mann-Whitney U test ( P
    Anti Rabbit Hrp Conjugated, supplied by Promega, used in various techniques. Bioz Stars score: 89/100, based on 38 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    82
    Promega peroxidase hrp conjugated secondary antibodies
    <t>GRFT</t> prevents HSV-2 and HPV postadsorption events. (A) HSV-2 G or HPV16 PsV and different concentrations of GRFT or medium (virus control) were preincubated for 0 h, 0.5 h, and 2 h at 37°C before being added to prechilled Vero cells (for HSV-2) or HeLa cells (for HPV16 PsV) and kept at 4°C for 2 h. The cells were washed 3 times before addition of the overlay and incubation at 48 h and 37°C in a 5% CO 2 atmosphere with 98% humidity. Finally, the cells were fixed and stained prior to counting the numbers of PFU. (B) The same as in panel A for HSV-2, but after 2 h of incubation at 4°C, the cells were switched to 37°C for an additional 2 h, followed by a 2-min treatment with citric acid buffer (pH 3.0). (C) Different concentrations of CG or GRFT were added at the indicated time points, with time zero representing the time of initial HPV16 PsV inoculation. The graph shows the percent reporter gene expression (mean ± SD) relative to that for the virus control (triplicate assays were performed per condition). (D) Western blot of purified HSV-2 lysate. Membranes were incubated overnight at 4°C with mouse anti-gD MAb DL11 (lane 1) or 1 μg/ml GRFT (lane 2). The membranes were washed and incubated for 1 h at room temperature with <t>HRP-conjugated</t> anti-mouse Ig (lane 1) or were incubated overnight at 4°C with rabbit anti-GRFT antibody (lane 2), before being washed and incubated with HRP-conjugated anti-rabbit immunoglobulin antibody (1 h at room temperature). (E) HSV-2-infected Vero cells were lysed, preincubated with GRFT, and immunoprecipitated with anti-GRFT antibody. Lanes 1, cell lysate without immunoprecipitation; lanes 2, HeLa cell lysate 24 h after HSV-2 infection with immunoprecipitation in the presence of GRFT and anti-GRFT antibody; lanes 3, same as lanes 2 but 48 h after HSV-2 infection; lanes 4 and 5, immunoprecipitation controls without and with GRFT, respectively. In the experiments described in the legends to panels D and E, the membranes were processed using an ECL Western blotting detection system to capture the bands on X-ray films. A representative blot of three repeats is shown. (F) Soluble GRFT, N-glycosylated (N-glyco), nonglycosylated gD, or a mixture of N-glycosylated and nonglycosylated gD-GRFT was preincubated before addition to Vero cells. HSV-2 G was then added, and infection was detected by an immunohistochemical assay after overnight incubation. Statistical analysis was performed using the Mann-Whitney U test ( P
    Peroxidase Hrp Conjugated Secondary Antibodies, supplied by Promega, used in various techniques. Bioz Stars score: 82/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    Promega rabbit anti mouse igg conjugated to hrp
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    Promega donkey anti goat hrp conjugate
    TLF2 is a protein complex. One microgram of TLF2 was immunoprecipitated by antibodies to human Hp (MAb; α-Hp), human apoA-I (polyclonal antibodies from sheep and goat; α-apoA-I), and human IgM (MAb; α-IgM). Following immunoprecipitation, the pellet (P) and supernatant (S) were separated by reducing SDS-PAGE (12% gel) and transferred to PVDF membranes. The IgM μ chain was detected with rabbit anti-IgM μ-chain antibody followed by goat anti-rabbit <t>IgG-HRP</t> and exposed for 30 s by ECL.
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    Promega hrp conjugated goat antimouse igg
    TLF2 is a protein complex. One microgram of TLF2 was immunoprecipitated by antibodies to human Hp (MAb; α-Hp), human apoA-I (polyclonal antibodies from sheep and goat; α-apoA-I), and human IgM (MAb; α-IgM). Following immunoprecipitation, the pellet (P) and supernatant (S) were separated by reducing SDS-PAGE (12% gel) and transferred to PVDF membranes. The IgM μ chain was detected with rabbit anti-IgM μ-chain antibody followed by goat anti-rabbit <t>IgG-HRP</t> and exposed for 30 s by ECL.
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    SP-A does not influence cell-surface expression of EGFR in A549 cells. A549 cells were serum-starved overnight. The next day, cells were incubated with 20 μg/ml SP-A for 2 h, washed, and incubated with 0.5 mg/ml Sulfo-NHS-LC-biotin for 30 min at 4 °C. Whole-cell lysates were immunoprecipitated with the monoclonal anti-EGFR antibody (clone Ab-11) or control <t>IgG.</t> Samples were separated by SDS-PAGE, transferred onto PVDF membranes, and probed with <t>HRP-conjugated</t> streptavidin ( right panel ) or the monoclonal anti-human EGFR antibody (clone D38B1), and the bands were detected using HRP-conjugated anti-rabbit IgG ( left panel ). The data are representative of three independent experiments.
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    Promega horse radish peroxidase
    SP-A does not influence cell-surface expression of EGFR in A549 cells. A549 cells were serum-starved overnight. The next day, cells were incubated with 20 μg/ml SP-A for 2 h, washed, and incubated with 0.5 mg/ml Sulfo-NHS-LC-biotin for 30 min at 4 °C. Whole-cell lysates were immunoprecipitated with the monoclonal anti-EGFR antibody (clone Ab-11) or control <t>IgG.</t> Samples were separated by SDS-PAGE, transferred onto PVDF membranes, and probed with <t>HRP-conjugated</t> streptavidin ( right panel ) or the monoclonal anti-human EGFR antibody (clone D38B1), and the bands were detected using HRP-conjugated anti-rabbit IgG ( left panel ). The data are representative of three independent experiments.
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    SP-A does not influence cell-surface expression of EGFR in A549 cells. A549 cells were serum-starved overnight. The next day, cells were incubated with 20 μg/ml SP-A for 2 h, washed, and incubated with 0.5 mg/ml Sulfo-NHS-LC-biotin for 30 min at 4 °C. Whole-cell lysates were immunoprecipitated with the monoclonal anti-EGFR antibody (clone Ab-11) or control <t>IgG.</t> Samples were separated by SDS-PAGE, transferred onto PVDF membranes, and probed with <t>HRP-conjugated</t> streptavidin ( right panel ) or the monoclonal anti-human EGFR antibody (clone D38B1), and the bands were detected using HRP-conjugated anti-rabbit IgG ( left panel ). The data are representative of three independent experiments.
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    Promega horseradish peroxidase hrp conjugated secondary antibodies
    SP-A does not influence cell-surface expression of EGFR in A549 cells. A549 cells were serum-starved overnight. The next day, cells were incubated with 20 μg/ml SP-A for 2 h, washed, and incubated with 0.5 mg/ml Sulfo-NHS-LC-biotin for 30 min at 4 °C. Whole-cell lysates were immunoprecipitated with the monoclonal anti-EGFR antibody (clone Ab-11) or control <t>IgG.</t> Samples were separated by SDS-PAGE, transferred onto PVDF membranes, and probed with <t>HRP-conjugated</t> streptavidin ( right panel ) or the monoclonal anti-human EGFR antibody (clone D38B1), and the bands were detected using HRP-conjugated anti-rabbit IgG ( left panel ). The data are representative of three independent experiments.
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    Promega hrp conjugated anti chicken igy
    SP-A does not influence cell-surface expression of EGFR in A549 cells. A549 cells were serum-starved overnight. The next day, cells were incubated with 20 μg/ml SP-A for 2 h, washed, and incubated with 0.5 mg/ml Sulfo-NHS-LC-biotin for 30 min at 4 °C. Whole-cell lysates were immunoprecipitated with the monoclonal anti-EGFR antibody (clone Ab-11) or control <t>IgG.</t> Samples were separated by SDS-PAGE, transferred onto PVDF membranes, and probed with <t>HRP-conjugated</t> streptavidin ( right panel ) or the monoclonal anti-human EGFR antibody (clone D38B1), and the bands were detected using HRP-conjugated anti-rabbit IgG ( left panel ). The data are representative of three independent experiments.
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    SP-A does not influence cell-surface expression of EGFR in A549 cells. A549 cells were serum-starved overnight. The next day, cells were incubated with 20 μg/ml SP-A for 2 h, washed, and incubated with 0.5 mg/ml Sulfo-NHS-LC-biotin for 30 min at 4 °C. Whole-cell lysates were immunoprecipitated with the monoclonal anti-EGFR antibody (clone Ab-11) or control <t>IgG.</t> Samples were separated by SDS-PAGE, transferred onto PVDF membranes, and probed with <t>HRP-conjugated</t> streptavidin ( right panel ) or the monoclonal anti-human EGFR antibody (clone D38B1), and the bands were detected using HRP-conjugated anti-rabbit IgG ( left panel ). The data are representative of three independent experiments.
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    SP-A does not influence cell-surface expression of EGFR in A549 cells. A549 cells were serum-starved overnight. The next day, cells were incubated with 20 μg/ml SP-A for 2 h, washed, and incubated with 0.5 mg/ml Sulfo-NHS-LC-biotin for 30 min at 4 °C. Whole-cell lysates were immunoprecipitated with the monoclonal anti-EGFR antibody (clone Ab-11) or control <t>IgG.</t> Samples were separated by SDS-PAGE, transferred onto PVDF membranes, and probed with <t>HRP-conjugated</t> streptavidin ( right panel ) or the monoclonal anti-human EGFR antibody (clone D38B1), and the bands were detected using HRP-conjugated anti-rabbit IgG ( left panel ). The data are representative of three independent experiments.
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    Promega goat anti rabbit igg conjugated to hrp
    SP-A does not influence cell-surface expression of EGFR in A549 cells. A549 cells were serum-starved overnight. The next day, cells were incubated with 20 μg/ml SP-A for 2 h, washed, and incubated with 0.5 mg/ml Sulfo-NHS-LC-biotin for 30 min at 4 °C. Whole-cell lysates were immunoprecipitated with the monoclonal anti-EGFR antibody (clone Ab-11) or control <t>IgG.</t> Samples were separated by SDS-PAGE, transferred onto PVDF membranes, and probed with <t>HRP-conjugated</t> streptavidin ( right panel ) or the monoclonal anti-human EGFR antibody (clone D38B1), and the bands were detected using HRP-conjugated anti-rabbit IgG ( left panel ). The data are representative of three independent experiments.
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    Promega hrp conjugated donkey anti goat
    SP-A does not influence cell-surface expression of EGFR in A549 cells. A549 cells were serum-starved overnight. The next day, cells were incubated with 20 μg/ml SP-A for 2 h, washed, and incubated with 0.5 mg/ml Sulfo-NHS-LC-biotin for 30 min at 4 °C. Whole-cell lysates were immunoprecipitated with the monoclonal anti-EGFR antibody (clone Ab-11) or control <t>IgG.</t> Samples were separated by SDS-PAGE, transferred onto PVDF membranes, and probed with <t>HRP-conjugated</t> streptavidin ( right panel ) or the monoclonal anti-human EGFR antibody (clone D38B1), and the bands were detected using HRP-conjugated anti-rabbit IgG ( left panel ). The data are representative of three independent experiments.
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    Promega hrp conjugated anti mouse igg
    Priming with the coexpression vector m8 Δ-Env/hCD40Lm induces greater amounts of Env-specific antibodies. Serum from individual immunized mice was analyzed using an HIV-1 JR-CSF gp160 ELISA assay. The plates were developed with <t>HRP-conjugated</t> anti-mouse <t>IgG</t> antibody. (A) The titer of Env-specific antibodies was determined by OD 450 values subtracted from the background values. Data are mean ± SD of the Env-specific antibody titer of all animals in each group (n = 16 for group G and I; n = 8 for group H and J; n = 5 for group B and M). (B) Endpoint binding titer of sera against HIV-1 JR-CSF gp160 from each of vaccine groups was plotted. The titer in the group primed with m8ΔEnv/hCD40Lm was significantly different from all other groups. There are no significant differences in env-specific antibody titer among the group G, H and J.
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    Priming with the coexpression vector m8 Δ-Env/hCD40Lm induces greater amounts of Env-specific antibodies. Serum from individual immunized mice was analyzed using an HIV-1 JR-CSF gp160 ELISA assay. The plates were developed with <t>HRP-conjugated</t> anti-mouse <t>IgG</t> antibody. (A) The titer of Env-specific antibodies was determined by OD 450 values subtracted from the background values. Data are mean ± SD of the Env-specific antibody titer of all animals in each group (n = 16 for group G and I; n = 8 for group H and J; n = 5 for group B and M). (B) Endpoint binding titer of sera against HIV-1 JR-CSF gp160 from each of vaccine groups was plotted. The titer in the group primed with m8ΔEnv/hCD40Lm was significantly different from all other groups. There are no significant differences in env-specific antibody titer among the group G, H and J.
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    Promega anti mouse horseradish peroxidase hrp conjugate
    Priming with the coexpression vector m8 Δ-Env/hCD40Lm induces greater amounts of Env-specific antibodies. Serum from individual immunized mice was analyzed using an HIV-1 JR-CSF gp160 ELISA assay. The plates were developed with <t>HRP-conjugated</t> anti-mouse <t>IgG</t> antibody. (A) The titer of Env-specific antibodies was determined by OD 450 values subtracted from the background values. Data are mean ± SD of the Env-specific antibody titer of all animals in each group (n = 16 for group G and I; n = 8 for group H and J; n = 5 for group B and M). (B) Endpoint binding titer of sera against HIV-1 JR-CSF gp160 from each of vaccine groups was plotted. The titer in the group primed with m8ΔEnv/hCD40Lm was significantly different from all other groups. There are no significant differences in env-specific antibody titer among the group G, H and J.
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    Priming with the coexpression vector m8 Δ-Env/hCD40Lm induces greater amounts of Env-specific antibodies. Serum from individual immunized mice was analyzed using an HIV-1 JR-CSF gp160 ELISA assay. The plates were developed with <t>HRP-conjugated</t> anti-mouse <t>IgG</t> antibody. (A) The titer of Env-specific antibodies was determined by OD 450 values subtracted from the background values. Data are mean ± SD of the Env-specific antibody titer of all animals in each group (n = 16 for group G and I; n = 8 for group H and J; n = 5 for group B and M). (B) Endpoint binding titer of sera against HIV-1 JR-CSF gp160 from each of vaccine groups was plotted. The titer in the group primed with m8ΔEnv/hCD40Lm was significantly different from all other groups. There are no significant differences in env-specific antibody titer among the group G, H and J.
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    Image Search Results


    Characterisation and purification of the royal jelly (RJ) component responsible for elevated MMP-9 production. ( A ) Heat and proteinase K treatment was performed by incubation of water royal jelly extract (WRJE) at 100 °C for 5 min and incubation with 150 μg/ml proteinase K for 1 h at 40 °C followed by heating to 98 °C for 10 min to inactivate the enzyme. Treated WRJE was incubated with HaCaT cells and conditioned equal volumes of the culture media were collected and subjected to gelatine zymography. Densitometric quantification of MMP-9 activity in culture media is presented. ( B ) Heat-treated WRJE was fractionated by a reverse phase-high performance liquid chromatography (RP-HPLC) on a C18 column (250 × 4.6 mm, 5 μm) at a flow rate 0.3 ml/min, with elution using a 10–90% gradient of acetonitrile (containing 0.1% (v/v) trifluoroacetic acid) for 85 min. ( C ) The HPLC fractions were assayed for MMP-9 induction. ( D ) HPLC fractions with maximal MMP-9 activity (51 to 59 min) were used for identification of MMP-9 inducer and were subjected to 16.5% Tricine-SDS-PAGE gels. Defensin-1 (5.5 kDa) was detected by Western blotting using a rabbit polyclonal anti-honeybee defensin-1 antibody diluted 1:2000 in blocking buffer. Horseradish peroxidise-conjugated secondary antibodies were applied. (The gels/blots with indicated cropping lines are shown in Supplementary Fig. S3 ). White line in gel indicates the place where two gels were spliced together. Data are expressed as means and SEMs of three independent measurements. Asterisks indicate a significant difference from the untreated group, * P

    Journal: Scientific Reports

    Article Title: Bee-derived antibacterial peptide, defensin-1, promotes wound re-epithelialisation in vitro and in vivo

    doi: 10.1038/s41598-017-07494-0

    Figure Lengend Snippet: Characterisation and purification of the royal jelly (RJ) component responsible for elevated MMP-9 production. ( A ) Heat and proteinase K treatment was performed by incubation of water royal jelly extract (WRJE) at 100 °C for 5 min and incubation with 150 μg/ml proteinase K for 1 h at 40 °C followed by heating to 98 °C for 10 min to inactivate the enzyme. Treated WRJE was incubated with HaCaT cells and conditioned equal volumes of the culture media were collected and subjected to gelatine zymography. Densitometric quantification of MMP-9 activity in culture media is presented. ( B ) Heat-treated WRJE was fractionated by a reverse phase-high performance liquid chromatography (RP-HPLC) on a C18 column (250 × 4.6 mm, 5 μm) at a flow rate 0.3 ml/min, with elution using a 10–90% gradient of acetonitrile (containing 0.1% (v/v) trifluoroacetic acid) for 85 min. ( C ) The HPLC fractions were assayed for MMP-9 induction. ( D ) HPLC fractions with maximal MMP-9 activity (51 to 59 min) were used for identification of MMP-9 inducer and were subjected to 16.5% Tricine-SDS-PAGE gels. Defensin-1 (5.5 kDa) was detected by Western blotting using a rabbit polyclonal anti-honeybee defensin-1 antibody diluted 1:2000 in blocking buffer. Horseradish peroxidise-conjugated secondary antibodies were applied. (The gels/blots with indicated cropping lines are shown in Supplementary Fig. S3 ). White line in gel indicates the place where two gels were spliced together. Data are expressed as means and SEMs of three independent measurements. Asterisks indicate a significant difference from the untreated group, * P

    Article Snippet: Rabbit polyclonal anti-bee defensin-1 (Def-1) was purchased from GenCust Europe (Luxembourg), and horseradish peroxidise-conjugated secondary antibodies were obtained from Promega (USA).

    Techniques: Purification, Incubation, Zymography, Activity Assay, High Performance Liquid Chromatography, Flow Cytometry, SDS Page, Western Blot, Blocking Assay

    GRFT prevents HSV-2 and HPV postadsorption events. (A) HSV-2 G or HPV16 PsV and different concentrations of GRFT or medium (virus control) were preincubated for 0 h, 0.5 h, and 2 h at 37°C before being added to prechilled Vero cells (for HSV-2) or HeLa cells (for HPV16 PsV) and kept at 4°C for 2 h. The cells were washed 3 times before addition of the overlay and incubation at 48 h and 37°C in a 5% CO 2 atmosphere with 98% humidity. Finally, the cells were fixed and stained prior to counting the numbers of PFU. (B) The same as in panel A for HSV-2, but after 2 h of incubation at 4°C, the cells were switched to 37°C for an additional 2 h, followed by a 2-min treatment with citric acid buffer (pH 3.0). (C) Different concentrations of CG or GRFT were added at the indicated time points, with time zero representing the time of initial HPV16 PsV inoculation. The graph shows the percent reporter gene expression (mean ± SD) relative to that for the virus control (triplicate assays were performed per condition). (D) Western blot of purified HSV-2 lysate. Membranes were incubated overnight at 4°C with mouse anti-gD MAb DL11 (lane 1) or 1 μg/ml GRFT (lane 2). The membranes were washed and incubated for 1 h at room temperature with HRP-conjugated anti-mouse Ig (lane 1) or were incubated overnight at 4°C with rabbit anti-GRFT antibody (lane 2), before being washed and incubated with HRP-conjugated anti-rabbit immunoglobulin antibody (1 h at room temperature). (E) HSV-2-infected Vero cells were lysed, preincubated with GRFT, and immunoprecipitated with anti-GRFT antibody. Lanes 1, cell lysate without immunoprecipitation; lanes 2, HeLa cell lysate 24 h after HSV-2 infection with immunoprecipitation in the presence of GRFT and anti-GRFT antibody; lanes 3, same as lanes 2 but 48 h after HSV-2 infection; lanes 4 and 5, immunoprecipitation controls without and with GRFT, respectively. In the experiments described in the legends to panels D and E, the membranes were processed using an ECL Western blotting detection system to capture the bands on X-ray films. A representative blot of three repeats is shown. (F) Soluble GRFT, N-glycosylated (N-glyco), nonglycosylated gD, or a mixture of N-glycosylated and nonglycosylated gD-GRFT was preincubated before addition to Vero cells. HSV-2 G was then added, and infection was detected by an immunohistochemical assay after overnight incubation. Statistical analysis was performed using the Mann-Whitney U test ( P

    Journal: Antimicrobial Agents and Chemotherapy

    Article Title: Griffithsin and Carrageenan Combination To Target Herpes Simplex Virus 2 and Human Papillomavirus

    doi: 10.1128/AAC.01816-15

    Figure Lengend Snippet: GRFT prevents HSV-2 and HPV postadsorption events. (A) HSV-2 G or HPV16 PsV and different concentrations of GRFT or medium (virus control) were preincubated for 0 h, 0.5 h, and 2 h at 37°C before being added to prechilled Vero cells (for HSV-2) or HeLa cells (for HPV16 PsV) and kept at 4°C for 2 h. The cells were washed 3 times before addition of the overlay and incubation at 48 h and 37°C in a 5% CO 2 atmosphere with 98% humidity. Finally, the cells were fixed and stained prior to counting the numbers of PFU. (B) The same as in panel A for HSV-2, but after 2 h of incubation at 4°C, the cells were switched to 37°C for an additional 2 h, followed by a 2-min treatment with citric acid buffer (pH 3.0). (C) Different concentrations of CG or GRFT were added at the indicated time points, with time zero representing the time of initial HPV16 PsV inoculation. The graph shows the percent reporter gene expression (mean ± SD) relative to that for the virus control (triplicate assays were performed per condition). (D) Western blot of purified HSV-2 lysate. Membranes were incubated overnight at 4°C with mouse anti-gD MAb DL11 (lane 1) or 1 μg/ml GRFT (lane 2). The membranes were washed and incubated for 1 h at room temperature with HRP-conjugated anti-mouse Ig (lane 1) or were incubated overnight at 4°C with rabbit anti-GRFT antibody (lane 2), before being washed and incubated with HRP-conjugated anti-rabbit immunoglobulin antibody (1 h at room temperature). (E) HSV-2-infected Vero cells were lysed, preincubated with GRFT, and immunoprecipitated with anti-GRFT antibody. Lanes 1, cell lysate without immunoprecipitation; lanes 2, HeLa cell lysate 24 h after HSV-2 infection with immunoprecipitation in the presence of GRFT and anti-GRFT antibody; lanes 3, same as lanes 2 but 48 h after HSV-2 infection; lanes 4 and 5, immunoprecipitation controls without and with GRFT, respectively. In the experiments described in the legends to panels D and E, the membranes were processed using an ECL Western blotting detection system to capture the bands on X-ray films. A representative blot of three repeats is shown. (F) Soluble GRFT, N-glycosylated (N-glyco), nonglycosylated gD, or a mixture of N-glycosylated and nonglycosylated gD-GRFT was preincubated before addition to Vero cells. HSV-2 G was then added, and infection was detected by an immunohistochemical assay after overnight incubation. Statistical analysis was performed using the Mann-Whitney U test ( P

    Article Snippet: The membranes were washed and incubated with rabbit polyclonal anti-GRFT (Pacific Immunology, Ramona, CA) or anti-mouse immunoglobulin conjugated with horseradish peroxidase (HRP) (Promega, Madison, WI).

    Techniques: Incubation, Staining, Expressing, Western Blot, Purification, Infection, Immunoprecipitation, Immunohistochemistry, MANN-WHITNEY

    TLF2 is a protein complex. One microgram of TLF2 was immunoprecipitated by antibodies to human Hp (MAb; α-Hp), human apoA-I (polyclonal antibodies from sheep and goat; α-apoA-I), and human IgM (MAb; α-IgM). Following immunoprecipitation, the pellet (P) and supernatant (S) were separated by reducing SDS-PAGE (12% gel) and transferred to PVDF membranes. The IgM μ chain was detected with rabbit anti-IgM μ-chain antibody followed by goat anti-rabbit IgG-HRP and exposed for 30 s by ECL.

    Journal: Infection and Immunity

    Article Title: Characterization of a Novel Trypanosome Lytic Factor from Human Serum

    doi:

    Figure Lengend Snippet: TLF2 is a protein complex. One microgram of TLF2 was immunoprecipitated by antibodies to human Hp (MAb; α-Hp), human apoA-I (polyclonal antibodies from sheep and goat; α-apoA-I), and human IgM (MAb; α-IgM). Following immunoprecipitation, the pellet (P) and supernatant (S) were separated by reducing SDS-PAGE (12% gel) and transferred to PVDF membranes. The IgM μ chain was detected with rabbit anti-IgM μ-chain antibody followed by goat anti-rabbit IgG-HRP and exposed for 30 s by ECL.

    Article Snippet: The secondary antibodies, goat anti-rabbit IgG conjugated to horseradish peroxidase (HRP) (W401B; Promega), rabbit anti-sheep IgG conjugated to HRP (605 345; Boehringer Mannheim), and rabbit anti-mouse IgG conjugated to HRP (W402B; Promega), were diluted 1:20,000 in TBST containing 4% BSA.

    Techniques: Immunoprecipitation, SDS Page

    SP-A does not influence cell-surface expression of EGFR in A549 cells. A549 cells were serum-starved overnight. The next day, cells were incubated with 20 μg/ml SP-A for 2 h, washed, and incubated with 0.5 mg/ml Sulfo-NHS-LC-biotin for 30 min at 4 °C. Whole-cell lysates were immunoprecipitated with the monoclonal anti-EGFR antibody (clone Ab-11) or control IgG. Samples were separated by SDS-PAGE, transferred onto PVDF membranes, and probed with HRP-conjugated streptavidin ( right panel ) or the monoclonal anti-human EGFR antibody (clone D38B1), and the bands were detected using HRP-conjugated anti-rabbit IgG ( left panel ). The data are representative of three independent experiments.

    Journal: The Journal of Biological Chemistry

    Article Title: Surfactant protein A down-regulates epidermal growth factor receptor by mechanisms different from those of surfactant protein D

    doi: 10.1074/jbc.M117.800771

    Figure Lengend Snippet: SP-A does not influence cell-surface expression of EGFR in A549 cells. A549 cells were serum-starved overnight. The next day, cells were incubated with 20 μg/ml SP-A for 2 h, washed, and incubated with 0.5 mg/ml Sulfo-NHS-LC-biotin for 30 min at 4 °C. Whole-cell lysates were immunoprecipitated with the monoclonal anti-EGFR antibody (clone Ab-11) or control IgG. Samples were separated by SDS-PAGE, transferred onto PVDF membranes, and probed with HRP-conjugated streptavidin ( right panel ) or the monoclonal anti-human EGFR antibody (clone D38B1), and the bands were detected using HRP-conjugated anti-rabbit IgG ( left panel ). The data are representative of three independent experiments.

    Article Snippet: Anti-rabbit HRP IgG (catalog no. W4011) and anti-mouse HRP IgG (catalog no. W4021) were from Promega (Madison, WI).

    Techniques: Expressing, Incubation, Immunoprecipitation, SDS Page

    SP-A binds to EGFR in A549 cells, H441 cells, and CHOK1 cells stably expressing EGFR. A, whole-cell lysate of A549 cells was immunoprecipitated ( IP ) with anti-EGFR monoclonal antibody Ab-11 or control IgG (0. 8 μg) at 4 °C for 16 h. The samples and BSA (200 ng/lane) were subjected to SDS-PAGE and transferred onto PVDF membranes. The membranes were incubated with or without SP-A (1 μg/ml) for 16 h. The membranes not incubated with SP-A were subjected to Western blotting using an anti-human EGFR monoclonal antibody ( WB: EGFR ). The membranes incubated with SP-A were then treated with an anti-human SP-A polyclonal antibody ( SP-A pAb ) or monoclonal antibodies PE10 ( SP-A mAb (PE10 )) or PC6 ( SP-A mAb (PC6 )), which was followed by incubation with HRP-labeled anti-rabbit IgG or anti-mouse IgG ( upper panel ). As a negative control, the membranes in the absence of incubation with SP-A were also incubated with an anti-human SP-A polyclonal antibody ( WB: SP-A pAb ) or monoclonal antibodies PE10 ( WB: SP-A mAb (PE10 )) or PC6 ( WB: SP-A mAb (PC6 )), which was followed by incubation with HRP-labeled anti-rabbit IgG or anti-mouse IgG ( lower panel ). The data are representative of three independent experiments. B and C, experimental paradigm described in A was performed in H441 cells ( B ) and CHOK1 cells stably expressing EGFR ( C ) by using an anti-human SP-A polyclonal antibody, which was followed by incubation with HRP-labeled anti-rabbit IgG. The data are representative of three independent experiments.

    Journal: The Journal of Biological Chemistry

    Article Title: Surfactant protein A down-regulates epidermal growth factor receptor by mechanisms different from those of surfactant protein D

    doi: 10.1074/jbc.M117.800771

    Figure Lengend Snippet: SP-A binds to EGFR in A549 cells, H441 cells, and CHOK1 cells stably expressing EGFR. A, whole-cell lysate of A549 cells was immunoprecipitated ( IP ) with anti-EGFR monoclonal antibody Ab-11 or control IgG (0. 8 μg) at 4 °C for 16 h. The samples and BSA (200 ng/lane) were subjected to SDS-PAGE and transferred onto PVDF membranes. The membranes were incubated with or without SP-A (1 μg/ml) for 16 h. The membranes not incubated with SP-A were subjected to Western blotting using an anti-human EGFR monoclonal antibody ( WB: EGFR ). The membranes incubated with SP-A were then treated with an anti-human SP-A polyclonal antibody ( SP-A pAb ) or monoclonal antibodies PE10 ( SP-A mAb (PE10 )) or PC6 ( SP-A mAb (PC6 )), which was followed by incubation with HRP-labeled anti-rabbit IgG or anti-mouse IgG ( upper panel ). As a negative control, the membranes in the absence of incubation with SP-A were also incubated with an anti-human SP-A polyclonal antibody ( WB: SP-A pAb ) or monoclonal antibodies PE10 ( WB: SP-A mAb (PE10 )) or PC6 ( WB: SP-A mAb (PC6 )), which was followed by incubation with HRP-labeled anti-rabbit IgG or anti-mouse IgG ( lower panel ). The data are representative of three independent experiments. B and C, experimental paradigm described in A was performed in H441 cells ( B ) and CHOK1 cells stably expressing EGFR ( C ) by using an anti-human SP-A polyclonal antibody, which was followed by incubation with HRP-labeled anti-rabbit IgG. The data are representative of three independent experiments.

    Article Snippet: Anti-rabbit HRP IgG (catalog no. W4011) and anti-mouse HRP IgG (catalog no. W4021) were from Promega (Madison, WI).

    Techniques: Stable Transfection, Expressing, Immunoprecipitation, SDS Page, Incubation, Western Blot, Labeling, Negative Control

    Priming with the coexpression vector m8 Δ-Env/hCD40Lm induces greater amounts of Env-specific antibodies. Serum from individual immunized mice was analyzed using an HIV-1 JR-CSF gp160 ELISA assay. The plates were developed with HRP-conjugated anti-mouse IgG antibody. (A) The titer of Env-specific antibodies was determined by OD 450 values subtracted from the background values. Data are mean ± SD of the Env-specific antibody titer of all animals in each group (n = 16 for group G and I; n = 8 for group H and J; n = 5 for group B and M). (B) Endpoint binding titer of sera against HIV-1 JR-CSF gp160 from each of vaccine groups was plotted. The titer in the group primed with m8ΔEnv/hCD40Lm was significantly different from all other groups. There are no significant differences in env-specific antibody titer among the group G, H and J.

    Journal: PLoS ONE

    Article Title: Elicitation of Both Anti HIV-1 Env Humoral and Cellular Immunities by Replicating Vaccinia Prime Sendai Virus Boost Regimen and Boosting by CD40Lm

    doi: 10.1371/journal.pone.0051633

    Figure Lengend Snippet: Priming with the coexpression vector m8 Δ-Env/hCD40Lm induces greater amounts of Env-specific antibodies. Serum from individual immunized mice was analyzed using an HIV-1 JR-CSF gp160 ELISA assay. The plates were developed with HRP-conjugated anti-mouse IgG antibody. (A) The titer of Env-specific antibodies was determined by OD 450 values subtracted from the background values. Data are mean ± SD of the Env-specific antibody titer of all animals in each group (n = 16 for group G and I; n = 8 for group H and J; n = 5 for group B and M). (B) Endpoint binding titer of sera against HIV-1 JR-CSF gp160 from each of vaccine groups was plotted. The titer in the group primed with m8ΔEnv/hCD40Lm was significantly different from all other groups. There are no significant differences in env-specific antibody titer among the group G, H and J.

    Article Snippet: HRP-conjugated anti-mouse IgA (Bethyl Laboratories; 1∶10,000) or HRP-conjugated anti-mouse IgG (Promega, Sunnyvale, US) was used as the secondary antibody at a dilution of 1∶2500.

    Techniques: Plasmid Preparation, Mouse Assay, Enzyme-linked Immunosorbent Assay, Binding Assay