immun-blot pvdf membrane Search Results


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  • 99
    Bio-Rad immunblot polyvinylidene difluoride membrane
    2D gel and blot of biotin-labeled R. <t>parkeri</t> surface proteins. The biotinylated proteins resolved by 2D PAGE were stained with SYPRO Ruby protein gel stain (A) or transferred to a <t>PVDF</t> membrane and detected using streptavidin-HRP conjugate (B). The numbers
    Immunblot Polyvinylidene Difluoride Membrane, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 2972 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    97
    Bio-Rad immuno blot pvdf membrane
    The over-expression of RALDH1 resulted in the RAL-mediated induction of Srebp-1c in 833/15 INS-1 cells. A. The adenovirus-mediated Raldh1 mRNA expression. B. <t>Immuno-blot</t> of the over-expression of RALDH1 protein in INS-1 cells. Whole cell lysates (50 µg/sample) of the control cells (lane 1), cells infected by the indicated pfu of Ad-β-gal (lane 2) or Ad-Raldh1 (lanes 3–5) were separated in 8% SDS protein gels, and transferred to the <t>PVDF</t> membranes. Primary antibodies to RALDH1 (1∶1000 dilution in TBST containing 5% dry milk), and to β-Actin (1∶1000 dilution in TBST containing 5% bovine serum albumin) were recognized by goat anti-rabbit IgG conjugated to horseradish peroxidase, and visualized by chemiluminescence. The films were scanned and presented as described in the Material and Methods . C. RAL only induced Srebp-1c expression in cells over-expressing RALDH1, but not β-gal. D. RA induced Srebp-1c expression in cells over-expressing either β-gal or RALDH1. Results were presented as means ± SD of fold inductions (* for comparing the different dosages of RAL in cells infected by Ad-Raldh1 using one way ANOVA, n = 3, all p
    Immuno Blot Pvdf Membrane, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 97/100, based on 755 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Bio-Rad immu blot pvdf membranes
    The over-expression of RALDH1 resulted in the RAL-mediated induction of Srebp-1c in 833/15 INS-1 cells. A. The adenovirus-mediated Raldh1 mRNA expression. B. <t>Immuno-blot</t> of the over-expression of RALDH1 protein in INS-1 cells. Whole cell lysates (50 µg/sample) of the control cells (lane 1), cells infected by the indicated pfu of Ad-β-gal (lane 2) or Ad-Raldh1 (lanes 3–5) were separated in 8% SDS protein gels, and transferred to the <t>PVDF</t> membranes. Primary antibodies to RALDH1 (1∶1000 dilution in TBST containing 5% dry milk), and to β-Actin (1∶1000 dilution in TBST containing 5% bovine serum albumin) were recognized by goat anti-rabbit IgG conjugated to horseradish peroxidase, and visualized by chemiluminescence. The films were scanned and presented as described in the Material and Methods . C. RAL only induced Srebp-1c expression in cells over-expressing RALDH1, but not β-gal. D. RA induced Srebp-1c expression in cells over-expressing either β-gal or RALDH1. Results were presented as means ± SD of fold inductions (* for comparing the different dosages of RAL in cells infected by Ad-Raldh1 using one way ANOVA, n = 3, all p
    Immu Blot Pvdf Membranes, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 92/100, based on 37 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Bio-Rad immune blot pvdf membrane
    The over-expression of RALDH1 resulted in the RAL-mediated induction of Srebp-1c in 833/15 INS-1 cells. A. The adenovirus-mediated Raldh1 mRNA expression. B. <t>Immuno-blot</t> of the over-expression of RALDH1 protein in INS-1 cells. Whole cell lysates (50 µg/sample) of the control cells (lane 1), cells infected by the indicated pfu of Ad-β-gal (lane 2) or Ad-Raldh1 (lanes 3–5) were separated in 8% SDS protein gels, and transferred to the <t>PVDF</t> membranes. Primary antibodies to RALDH1 (1∶1000 dilution in TBST containing 5% dry milk), and to β-Actin (1∶1000 dilution in TBST containing 5% bovine serum albumin) were recognized by goat anti-rabbit IgG conjugated to horseradish peroxidase, and visualized by chemiluminescence. The films were scanned and presented as described in the Material and Methods . C. RAL only induced Srebp-1c expression in cells over-expressing RALDH1, but not β-gal. D. RA induced Srebp-1c expression in cells over-expressing either β-gal or RALDH1. Results were presented as means ± SD of fold inductions (* for comparing the different dosages of RAL in cells infected by Ad-Raldh1 using one way ANOVA, n = 3, all p
    Immune Blot Pvdf Membrane, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 95/100, based on 149 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Bio-Rad polyvinylidene difluoride membranes
    The over-expression of RALDH1 resulted in the RAL-mediated induction of Srebp-1c in 833/15 INS-1 cells. A. The adenovirus-mediated Raldh1 mRNA expression. B. <t>Immuno-blot</t> of the over-expression of RALDH1 protein in INS-1 cells. Whole cell lysates (50 µg/sample) of the control cells (lane 1), cells infected by the indicated pfu of Ad-β-gal (lane 2) or Ad-Raldh1 (lanes 3–5) were separated in 8% SDS protein gels, and transferred to the <t>PVDF</t> membranes. Primary antibodies to RALDH1 (1∶1000 dilution in TBST containing 5% dry milk), and to β-Actin (1∶1000 dilution in TBST containing 5% bovine serum albumin) were recognized by goat anti-rabbit IgG conjugated to horseradish peroxidase, and visualized by chemiluminescence. The films were scanned and presented as described in the Material and Methods . C. RAL only induced Srebp-1c expression in cells over-expressing RALDH1, but not β-gal. D. RA induced Srebp-1c expression in cells over-expressing either β-gal or RALDH1. Results were presented as means ± SD of fold inductions (* for comparing the different dosages of RAL in cells infected by Ad-Raldh1 using one way ANOVA, n = 3, all p
    Polyvinylidene Difluoride Membranes, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 10133 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Bio-Rad immun blot polyvinylidene difluoride transfer membrane
    The over-expression of RALDH1 resulted in the RAL-mediated induction of Srebp-1c in 833/15 INS-1 cells. A. The adenovirus-mediated Raldh1 mRNA expression. B. <t>Immuno-blot</t> of the over-expression of RALDH1 protein in INS-1 cells. Whole cell lysates (50 µg/sample) of the control cells (lane 1), cells infected by the indicated pfu of Ad-β-gal (lane 2) or Ad-Raldh1 (lanes 3–5) were separated in 8% SDS protein gels, and transferred to the <t>PVDF</t> membranes. Primary antibodies to RALDH1 (1∶1000 dilution in TBST containing 5% dry milk), and to β-Actin (1∶1000 dilution in TBST containing 5% bovine serum albumin) were recognized by goat anti-rabbit IgG conjugated to horseradish peroxidase, and visualized by chemiluminescence. The films were scanned and presented as described in the Material and Methods . C. RAL only induced Srebp-1c expression in cells over-expressing RALDH1, but not β-gal. D. RA induced Srebp-1c expression in cells over-expressing either β-gal or RALDH1. Results were presented as means ± SD of fold inductions (* for comparing the different dosages of RAL in cells infected by Ad-Raldh1 using one way ANOVA, n = 3, all p
    Immun Blot Polyvinylidene Difluoride Transfer Membrane, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 91/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Bio-Rad nitrocellulose membrane
    The over-expression of RALDH1 resulted in the RAL-mediated induction of Srebp-1c in 833/15 INS-1 cells. A. The adenovirus-mediated Raldh1 mRNA expression. B. <t>Immuno-blot</t> of the over-expression of RALDH1 protein in INS-1 cells. Whole cell lysates (50 µg/sample) of the control cells (lane 1), cells infected by the indicated pfu of Ad-β-gal (lane 2) or Ad-Raldh1 (lanes 3–5) were separated in 8% SDS protein gels, and transferred to the <t>PVDF</t> membranes. Primary antibodies to RALDH1 (1∶1000 dilution in TBST containing 5% dry milk), and to β-Actin (1∶1000 dilution in TBST containing 5% bovine serum albumin) were recognized by goat anti-rabbit IgG conjugated to horseradish peroxidase, and visualized by chemiluminescence. The films were scanned and presented as described in the Material and Methods . C. RAL only induced Srebp-1c expression in cells over-expressing RALDH1, but not β-gal. D. RA induced Srebp-1c expression in cells over-expressing either β-gal or RALDH1. Results were presented as means ± SD of fold inductions (* for comparing the different dosages of RAL in cells infected by Ad-Raldh1 using one way ANOVA, n = 3, all p
    Nitrocellulose Membrane, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 2051 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    GE Healthcare immun blot polyvinylidene fluoride membranes
    The over-expression of RALDH1 resulted in the RAL-mediated induction of Srebp-1c in 833/15 INS-1 cells. A. The adenovirus-mediated Raldh1 mRNA expression. B. <t>Immuno-blot</t> of the over-expression of RALDH1 protein in INS-1 cells. Whole cell lysates (50 µg/sample) of the control cells (lane 1), cells infected by the indicated pfu of Ad-β-gal (lane 2) or Ad-Raldh1 (lanes 3–5) were separated in 8% SDS protein gels, and transferred to the <t>PVDF</t> membranes. Primary antibodies to RALDH1 (1∶1000 dilution in TBST containing 5% dry milk), and to β-Actin (1∶1000 dilution in TBST containing 5% bovine serum albumin) were recognized by goat anti-rabbit IgG conjugated to horseradish peroxidase, and visualized by chemiluminescence. The films were scanned and presented as described in the Material and Methods . C. RAL only induced Srebp-1c expression in cells over-expressing RALDH1, but not β-gal. D. RA induced Srebp-1c expression in cells over-expressing either β-gal or RALDH1. Results were presented as means ± SD of fold inductions (* for comparing the different dosages of RAL in cells infected by Ad-Raldh1 using one way ANOVA, n = 3, all p
    Immun Blot Polyvinylidene Fluoride Membranes, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 89/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Millipore immun blot polyvinylidene fluoride membranes
    The over-expression of RALDH1 resulted in the RAL-mediated induction of Srebp-1c in 833/15 INS-1 cells. A. The adenovirus-mediated Raldh1 mRNA expression. B. <t>Immuno-blot</t> of the over-expression of RALDH1 protein in INS-1 cells. Whole cell lysates (50 µg/sample) of the control cells (lane 1), cells infected by the indicated pfu of Ad-β-gal (lane 2) or Ad-Raldh1 (lanes 3–5) were separated in 8% SDS protein gels, and transferred to the <t>PVDF</t> membranes. Primary antibodies to RALDH1 (1∶1000 dilution in TBST containing 5% dry milk), and to β-Actin (1∶1000 dilution in TBST containing 5% bovine serum albumin) were recognized by goat anti-rabbit IgG conjugated to horseradish peroxidase, and visualized by chemiluminescence. The films were scanned and presented as described in the Material and Methods . C. RAL only induced Srebp-1c expression in cells over-expressing RALDH1, but not β-gal. D. RA induced Srebp-1c expression in cells over-expressing either β-gal or RALDH1. Results were presented as means ± SD of fold inductions (* for comparing the different dosages of RAL in cells infected by Ad-Raldh1 using one way ANOVA, n = 3, all p
    Immun Blot Polyvinylidene Fluoride Membranes, supplied by Millipore, used in various techniques. Bioz Stars score: 86/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Thermo Fisher immun blot pvdf membrane
    The over-expression of RALDH1 resulted in the RAL-mediated induction of Srebp-1c in 833/15 INS-1 cells. A. The adenovirus-mediated Raldh1 mRNA expression. B. <t>Immuno-blot</t> of the over-expression of RALDH1 protein in INS-1 cells. Whole cell lysates (50 µg/sample) of the control cells (lane 1), cells infected by the indicated pfu of Ad-β-gal (lane 2) or Ad-Raldh1 (lanes 3–5) were separated in 8% SDS protein gels, and transferred to the <t>PVDF</t> membranes. Primary antibodies to RALDH1 (1∶1000 dilution in TBST containing 5% dry milk), and to β-Actin (1∶1000 dilution in TBST containing 5% bovine serum albumin) were recognized by goat anti-rabbit IgG conjugated to horseradish peroxidase, and visualized by chemiluminescence. The films were scanned and presented as described in the Material and Methods . C. RAL only induced Srebp-1c expression in cells over-expressing RALDH1, but not β-gal. D. RA induced Srebp-1c expression in cells over-expressing either β-gal or RALDH1. Results were presented as means ± SD of fold inductions (* for comparing the different dosages of RAL in cells infected by Ad-Raldh1 using one way ANOVA, n = 3, all p
    Immun Blot Pvdf Membrane, supplied by Thermo Fisher, 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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    91
    Millipore immune blot f pvdf membranes
    The over-expression of RALDH1 resulted in the RAL-mediated induction of Srebp-1c in 833/15 INS-1 cells. A. The adenovirus-mediated Raldh1 mRNA expression. B. <t>Immuno-blot</t> of the over-expression of RALDH1 protein in INS-1 cells. Whole cell lysates (50 µg/sample) of the control cells (lane 1), cells infected by the indicated pfu of Ad-β-gal (lane 2) or Ad-Raldh1 (lanes 3–5) were separated in 8% SDS protein gels, and transferred to the <t>PVDF</t> membranes. Primary antibodies to RALDH1 (1∶1000 dilution in TBST containing 5% dry milk), and to β-Actin (1∶1000 dilution in TBST containing 5% bovine serum albumin) were recognized by goat anti-rabbit IgG conjugated to horseradish peroxidase, and visualized by chemiluminescence. The films were scanned and presented as described in the Material and Methods . C. RAL only induced Srebp-1c expression in cells over-expressing RALDH1, but not β-gal. D. RA induced Srebp-1c expression in cells over-expressing either β-gal or RALDH1. Results were presented as means ± SD of fold inductions (* for comparing the different dosages of RAL in cells infected by Ad-Raldh1 using one way ANOVA, n = 3, all p
    Immune Blot F Pvdf Membranes, supplied by Millipore, used in various techniques. Bioz Stars score: 91/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Bio-Rad immune blot low fluorescence pvdf membrane
    The over-expression of RALDH1 resulted in the RAL-mediated induction of Srebp-1c in 833/15 INS-1 cells. A. The adenovirus-mediated Raldh1 mRNA expression. B. <t>Immuno-blot</t> of the over-expression of RALDH1 protein in INS-1 cells. Whole cell lysates (50 µg/sample) of the control cells (lane 1), cells infected by the indicated pfu of Ad-β-gal (lane 2) or Ad-Raldh1 (lanes 3–5) were separated in 8% SDS protein gels, and transferred to the <t>PVDF</t> membranes. Primary antibodies to RALDH1 (1∶1000 dilution in TBST containing 5% dry milk), and to β-Actin (1∶1000 dilution in TBST containing 5% bovine serum albumin) were recognized by goat anti-rabbit IgG conjugated to horseradish peroxidase, and visualized by chemiluminescence. The films were scanned and presented as described in the Material and Methods . C. RAL only induced Srebp-1c expression in cells over-expressing RALDH1, but not β-gal. D. RA induced Srebp-1c expression in cells over-expressing either β-gal or RALDH1. Results were presented as means ± SD of fold inductions (* for comparing the different dosages of RAL in cells infected by Ad-Raldh1 using one way ANOVA, n = 3, all p
    Immune Blot Low Fluorescence Pvdf Membrane, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 92/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Bio-Rad immun blot low fluorescence polyvinylidene difluoride membranes
    YAP and WBP2 are highly expressed in human epidermal SCs and upregulated in cSCC. ( a , b ) Representative images (single optical planes) of adult ( a ) and fetal (17 weeks gestation) ( b ) human skin sections immunolabelled with the indicated antibodies and counterstained with DAPI to reveal nuclei. White dotted lines demarcate dermal-epidermal boundaries. Scale bars, 50 μm. ( c ) Western <t>blot</t> analysis of NHKs, SCC13 cells and primary cSCC cells (SCC-NR) using antibodies against WBP2. Tubulin was used as loading control. ( d , e ) Semiquantitative analysis (H-score) of YAP ( d ) and WBP2 ( e ) immunostaining intensities (individual data points) in a panel of cSCC- compared with normal skin sections (dotted line). Red lines represent the mean. ( f ) Western blot analysis of enriched populations of stem- (SC), transit amplifying- (TA), and terminally differentiated (D) cells using antibodies against YAP, WBP2, ITGβ1, and involucrin (IVL). Equal protein loading was confirmed by enhanced tryptophan <t>fluorescence</t> imaging (Bio-Rad) of PVDF <t>membranes</t> (loading control). ( g ) Representative images (maximum intensity projections) of expanding and mature SC colonies as well as abortive colonies, immunolabelled with indicated antibodies and counterstained for DAPI to reveal nuclei. Scale bars, 100 μm. PVDF, <t>polyvinylidene</t> <t>difluoride.</t>
    Immun Blot Low Fluorescence Polyvinylidene Difluoride Membranes, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 93/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    GE Healthcare immune blot pvdf membranes
    YAP and WBP2 are highly expressed in human epidermal SCs and upregulated in cSCC. ( a , b ) Representative images (single optical planes) of adult ( a ) and fetal (17 weeks gestation) ( b ) human skin sections immunolabelled with the indicated antibodies and counterstained with DAPI to reveal nuclei. White dotted lines demarcate dermal-epidermal boundaries. Scale bars, 50 μm. ( c ) Western <t>blot</t> analysis of NHKs, SCC13 cells and primary cSCC cells (SCC-NR) using antibodies against WBP2. Tubulin was used as loading control. ( d , e ) Semiquantitative analysis (H-score) of YAP ( d ) and WBP2 ( e ) immunostaining intensities (individual data points) in a panel of cSCC- compared with normal skin sections (dotted line). Red lines represent the mean. ( f ) Western blot analysis of enriched populations of stem- (SC), transit amplifying- (TA), and terminally differentiated (D) cells using antibodies against YAP, WBP2, ITGβ1, and involucrin (IVL). Equal protein loading was confirmed by enhanced tryptophan <t>fluorescence</t> imaging (Bio-Rad) of PVDF <t>membranes</t> (loading control). ( g ) Representative images (maximum intensity projections) of expanding and mature SC colonies as well as abortive colonies, immunolabelled with indicated antibodies and counterstained for DAPI to reveal nuclei. Scale bars, 100 μm. PVDF, <t>polyvinylidene</t> <t>difluoride.</t>
    Immune Blot Pvdf Membranes, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 94/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Roche immun blot pvdf membrane
    YAP and WBP2 are highly expressed in human epidermal SCs and upregulated in cSCC. ( a , b ) Representative images (single optical planes) of adult ( a ) and fetal (17 weeks gestation) ( b ) human skin sections immunolabelled with the indicated antibodies and counterstained with DAPI to reveal nuclei. White dotted lines demarcate dermal-epidermal boundaries. Scale bars, 50 μm. ( c ) Western <t>blot</t> analysis of NHKs, SCC13 cells and primary cSCC cells (SCC-NR) using antibodies against WBP2. Tubulin was used as loading control. ( d , e ) Semiquantitative analysis (H-score) of YAP ( d ) and WBP2 ( e ) immunostaining intensities (individual data points) in a panel of cSCC- compared with normal skin sections (dotted line). Red lines represent the mean. ( f ) Western blot analysis of enriched populations of stem- (SC), transit amplifying- (TA), and terminally differentiated (D) cells using antibodies against YAP, WBP2, ITGβ1, and involucrin (IVL). Equal protein loading was confirmed by enhanced tryptophan <t>fluorescence</t> imaging (Bio-Rad) of PVDF <t>membranes</t> (loading control). ( g ) Representative images (maximum intensity projections) of expanding and mature SC colonies as well as abortive colonies, immunolabelled with indicated antibodies and counterstained for DAPI to reveal nuclei. Scale bars, 100 μm. PVDF, <t>polyvinylidene</t> <t>difluoride.</t>
    Immun Blot Pvdf Membrane, supplied by Roche, used in various techniques. Bioz Stars score: 93/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Bio-Rad immun blot polyvinylidene difluoride pvdf western blotting membrane
    YAP and WBP2 are highly expressed in human epidermal SCs and upregulated in cSCC. ( a , b ) Representative images (single optical planes) of adult ( a ) and fetal (17 weeks gestation) ( b ) human skin sections immunolabelled with the indicated antibodies and counterstained with DAPI to reveal nuclei. White dotted lines demarcate dermal-epidermal boundaries. Scale bars, 50 μm. ( c ) Western <t>blot</t> analysis of NHKs, SCC13 cells and primary cSCC cells (SCC-NR) using antibodies against WBP2. Tubulin was used as loading control. ( d , e ) Semiquantitative analysis (H-score) of YAP ( d ) and WBP2 ( e ) immunostaining intensities (individual data points) in a panel of cSCC- compared with normal skin sections (dotted line). Red lines represent the mean. ( f ) Western blot analysis of enriched populations of stem- (SC), transit amplifying- (TA), and terminally differentiated (D) cells using antibodies against YAP, WBP2, ITGβ1, and involucrin (IVL). Equal protein loading was confirmed by enhanced tryptophan <t>fluorescence</t> imaging (Bio-Rad) of PVDF <t>membranes</t> (loading control). ( g ) Representative images (maximum intensity projections) of expanding and mature SC colonies as well as abortive colonies, immunolabelled with indicated antibodies and counterstained for DAPI to reveal nuclei. Scale bars, 100 μm. PVDF, <t>polyvinylidene</t> <t>difluoride.</t>
    Immun Blot Polyvinylidene Difluoride Pvdf Western Blotting Membrane, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Bio-Rad low fluorescence pvdf membranes
    YAP and WBP2 are highly expressed in human epidermal SCs and upregulated in cSCC. ( a , b ) Representative images (single optical planes) of adult ( a ) and fetal (17 weeks gestation) ( b ) human skin sections immunolabelled with the indicated antibodies and counterstained with DAPI to reveal nuclei. White dotted lines demarcate dermal-epidermal boundaries. Scale bars, 50 μm. ( c ) Western <t>blot</t> analysis of NHKs, SCC13 cells and primary cSCC cells (SCC-NR) using antibodies against WBP2. Tubulin was used as loading control. ( d , e ) Semiquantitative analysis (H-score) of YAP ( d ) and WBP2 ( e ) immunostaining intensities (individual data points) in a panel of cSCC- compared with normal skin sections (dotted line). Red lines represent the mean. ( f ) Western blot analysis of enriched populations of stem- (SC), transit amplifying- (TA), and terminally differentiated (D) cells using antibodies against YAP, WBP2, ITGβ1, and involucrin (IVL). Equal protein loading was confirmed by enhanced tryptophan <t>fluorescence</t> imaging (Bio-Rad) of PVDF <t>membranes</t> (loading control). ( g ) Representative images (maximum intensity projections) of expanding and mature SC colonies as well as abortive colonies, immunolabelled with indicated antibodies and counterstained for DAPI to reveal nuclei. Scale bars, 100 μm. PVDF, <t>polyvinylidene</t> <t>difluoride.</t>
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    YAP and WBP2 are highly expressed in human epidermal SCs and upregulated in cSCC. ( a , b ) Representative images (single optical planes) of adult ( a ) and fetal (17 weeks gestation) ( b ) human skin sections immunolabelled with the indicated antibodies and counterstained with DAPI to reveal nuclei. White dotted lines demarcate dermal-epidermal boundaries. Scale bars, 50 μm. ( c ) Western <t>blot</t> analysis of NHKs, SCC13 cells and primary cSCC cells (SCC-NR) using antibodies against WBP2. Tubulin was used as loading control. ( d , e ) Semiquantitative analysis (H-score) of YAP ( d ) and WBP2 ( e ) immunostaining intensities (individual data points) in a panel of cSCC- compared with normal skin sections (dotted line). Red lines represent the mean. ( f ) Western blot analysis of enriched populations of stem- (SC), transit amplifying- (TA), and terminally differentiated (D) cells using antibodies against YAP, WBP2, ITGβ1, and involucrin (IVL). Equal protein loading was confirmed by enhanced tryptophan <t>fluorescence</t> imaging (Bio-Rad) of PVDF <t>membranes</t> (loading control). ( g ) Representative images (maximum intensity projections) of expanding and mature SC colonies as well as abortive colonies, immunolabelled with indicated antibodies and counterstained for DAPI to reveal nuclei. Scale bars, 100 μm. PVDF, <t>polyvinylidene</t> <t>difluoride.</t>
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    Millipore immuno blot pvdf membrane
    YAP and WBP2 are highly expressed in human epidermal SCs and upregulated in cSCC. ( a , b ) Representative images (single optical planes) of adult ( a ) and fetal (17 weeks gestation) ( b ) human skin sections immunolabelled with the indicated antibodies and counterstained with DAPI to reveal nuclei. White dotted lines demarcate dermal-epidermal boundaries. Scale bars, 50 μm. ( c ) Western <t>blot</t> analysis of NHKs, SCC13 cells and primary cSCC cells (SCC-NR) using antibodies against WBP2. Tubulin was used as loading control. ( d , e ) Semiquantitative analysis (H-score) of YAP ( d ) and WBP2 ( e ) immunostaining intensities (individual data points) in a panel of cSCC- compared with normal skin sections (dotted line). Red lines represent the mean. ( f ) Western blot analysis of enriched populations of stem- (SC), transit amplifying- (TA), and terminally differentiated (D) cells using antibodies against YAP, WBP2, ITGβ1, and involucrin (IVL). Equal protein loading was confirmed by enhanced tryptophan <t>fluorescence</t> imaging (Bio-Rad) of PVDF <t>membranes</t> (loading control). ( g ) Representative images (maximum intensity projections) of expanding and mature SC colonies as well as abortive colonies, immunolabelled with indicated antibodies and counterstained for DAPI to reveal nuclei. Scale bars, 100 μm. PVDF, <t>polyvinylidene</t> <t>difluoride.</t>
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    GE Healthcare immuno blot pvdf membrane
    YAP and WBP2 are highly expressed in human epidermal SCs and upregulated in cSCC. ( a , b ) Representative images (single optical planes) of adult ( a ) and fetal (17 weeks gestation) ( b ) human skin sections immunolabelled with the indicated antibodies and counterstained with DAPI to reveal nuclei. White dotted lines demarcate dermal-epidermal boundaries. Scale bars, 50 μm. ( c ) Western <t>blot</t> analysis of NHKs, SCC13 cells and primary cSCC cells (SCC-NR) using antibodies against WBP2. Tubulin was used as loading control. ( d , e ) Semiquantitative analysis (H-score) of YAP ( d ) and WBP2 ( e ) immunostaining intensities (individual data points) in a panel of cSCC- compared with normal skin sections (dotted line). Red lines represent the mean. ( f ) Western blot analysis of enriched populations of stem- (SC), transit amplifying- (TA), and terminally differentiated (D) cells using antibodies against YAP, WBP2, ITGβ1, and involucrin (IVL). Equal protein loading was confirmed by enhanced tryptophan <t>fluorescence</t> imaging (Bio-Rad) of PVDF <t>membranes</t> (loading control). ( g ) Representative images (maximum intensity projections) of expanding and mature SC colonies as well as abortive colonies, immunolabelled with indicated antibodies and counterstained for DAPI to reveal nuclei. Scale bars, 100 μm. PVDF, <t>polyvinylidene</t> <t>difluoride.</t>
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    YAP and WBP2 are highly expressed in human epidermal SCs and upregulated in cSCC. ( a , b ) Representative images (single optical planes) of adult ( a ) and fetal (17 weeks gestation) ( b ) human skin sections immunolabelled with the indicated antibodies and counterstained with DAPI to reveal nuclei. White dotted lines demarcate dermal-epidermal boundaries. Scale bars, 50 μm. ( c ) Western <t>blot</t> analysis of NHKs, SCC13 cells and primary cSCC cells (SCC-NR) using antibodies against WBP2. Tubulin was used as loading control. ( d , e ) Semiquantitative analysis (H-score) of YAP ( d ) and WBP2 ( e ) immunostaining intensities (individual data points) in a panel of cSCC- compared with normal skin sections (dotted line). Red lines represent the mean. ( f ) Western blot analysis of enriched populations of stem- (SC), transit amplifying- (TA), and terminally differentiated (D) cells using antibodies against YAP, WBP2, ITGβ1, and involucrin (IVL). Equal protein loading was confirmed by enhanced tryptophan <t>fluorescence</t> imaging (Bio-Rad) of PVDF <t>membranes</t> (loading control). ( g ) Representative images (maximum intensity projections) of expanding and mature SC colonies as well as abortive colonies, immunolabelled with indicated antibodies and counterstained for DAPI to reveal nuclei. Scale bars, 100 μm. PVDF, <t>polyvinylidene</t> <t>difluoride.</t>
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    YAP and WBP2 are highly expressed in human epidermal SCs and upregulated in cSCC. ( a , b ) Representative images (single optical planes) of adult ( a ) and fetal (17 weeks gestation) ( b ) human skin sections immunolabelled with the indicated antibodies and counterstained with DAPI to reveal nuclei. White dotted lines demarcate dermal-epidermal boundaries. Scale bars, 50 μm. ( c ) Western <t>blot</t> analysis of NHKs, SCC13 cells and primary cSCC cells (SCC-NR) using antibodies against WBP2. Tubulin was used as loading control. ( d , e ) Semiquantitative analysis (H-score) of YAP ( d ) and WBP2 ( e ) immunostaining intensities (individual data points) in a panel of cSCC- compared with normal skin sections (dotted line). Red lines represent the mean. ( f ) Western blot analysis of enriched populations of stem- (SC), transit amplifying- (TA), and terminally differentiated (D) cells using antibodies against YAP, WBP2, ITGβ1, and involucrin (IVL). Equal protein loading was confirmed by enhanced tryptophan <t>fluorescence</t> imaging (Bio-Rad) of PVDF <t>membranes</t> (loading control). ( g ) Representative images (maximum intensity projections) of expanding and mature SC colonies as well as abortive colonies, immunolabelled with indicated antibodies and counterstained for DAPI to reveal nuclei. Scale bars, 100 μm. PVDF, <t>polyvinylidene</t> <t>difluoride.</t>
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    Thermo Fisher pre soaked immuno blot pvdf membranes
    YAP and WBP2 are highly expressed in human epidermal SCs and upregulated in cSCC. ( a , b ) Representative images (single optical planes) of adult ( a ) and fetal (17 weeks gestation) ( b ) human skin sections immunolabelled with the indicated antibodies and counterstained with DAPI to reveal nuclei. White dotted lines demarcate dermal-epidermal boundaries. Scale bars, 50 μm. ( c ) Western <t>blot</t> analysis of NHKs, SCC13 cells and primary cSCC cells (SCC-NR) using antibodies against WBP2. Tubulin was used as loading control. ( d , e ) Semiquantitative analysis (H-score) of YAP ( d ) and WBP2 ( e ) immunostaining intensities (individual data points) in a panel of cSCC- compared with normal skin sections (dotted line). Red lines represent the mean. ( f ) Western blot analysis of enriched populations of stem- (SC), transit amplifying- (TA), and terminally differentiated (D) cells using antibodies against YAP, WBP2, ITGβ1, and involucrin (IVL). Equal protein loading was confirmed by enhanced tryptophan <t>fluorescence</t> imaging (Bio-Rad) of PVDF <t>membranes</t> (loading control). ( g ) Representative images (maximum intensity projections) of expanding and mature SC colonies as well as abortive colonies, immunolabelled with indicated antibodies and counterstained for DAPI to reveal nuclei. Scale bars, 100 μm. PVDF, <t>polyvinylidene</t> <t>difluoride.</t>
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    Merck KGaA immuno blot polyvinylidene fluoride pvdf membrane
    YAP and WBP2 are highly expressed in human epidermal SCs and upregulated in cSCC. ( a , b ) Representative images (single optical planes) of adult ( a ) and fetal (17 weeks gestation) ( b ) human skin sections immunolabelled with the indicated antibodies and counterstained with DAPI to reveal nuclei. White dotted lines demarcate dermal-epidermal boundaries. Scale bars, 50 μm. ( c ) Western <t>blot</t> analysis of NHKs, SCC13 cells and primary cSCC cells (SCC-NR) using antibodies against WBP2. Tubulin was used as loading control. ( d , e ) Semiquantitative analysis (H-score) of YAP ( d ) and WBP2 ( e ) immunostaining intensities (individual data points) in a panel of cSCC- compared with normal skin sections (dotted line). Red lines represent the mean. ( f ) Western blot analysis of enriched populations of stem- (SC), transit amplifying- (TA), and terminally differentiated (D) cells using antibodies against YAP, WBP2, ITGβ1, and involucrin (IVL). Equal protein loading was confirmed by enhanced tryptophan <t>fluorescence</t> imaging (Bio-Rad) of PVDF <t>membranes</t> (loading control). ( g ) Representative images (maximum intensity projections) of expanding and mature SC colonies as well as abortive colonies, immunolabelled with indicated antibodies and counterstained for DAPI to reveal nuclei. Scale bars, 100 μm. PVDF, <t>polyvinylidene</t> <t>difluoride.</t>
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    Image Search Results


    2D gel and blot of biotin-labeled R. parkeri surface proteins. The biotinylated proteins resolved by 2D PAGE were stained with SYPRO Ruby protein gel stain (A) or transferred to a PVDF membrane and detected using streptavidin-HRP conjugate (B). The numbers

    Journal: Infection and Immunity

    Article Title: Proteomic Analysis of Rickettsia parkeri Strain Portsmouth ▿

    doi: 10.1128/IAI.00911-09

    Figure Lengend Snippet: 2D gel and blot of biotin-labeled R. parkeri surface proteins. The biotinylated proteins resolved by 2D PAGE were stained with SYPRO Ruby protein gel stain (A) or transferred to a PVDF membrane and detected using streptavidin-HRP conjugate (B). The numbers

    Article Snippet: Unlabeled or biotin-labeled R. parkeri proteins separated by 2D PAGE were electroblotted onto Immun-Blot polyvinylidene difluoride (PVDF) membranes (Bio-Rad) by using an XCell II blot module (Invitrogen) according to the manufacturer's protocol.

    Techniques: Two-Dimensional Gel Electrophoresis, Labeling, Polyacrylamide Gel Electrophoresis, Staining

    2D immunoblot of R. parkeri protein extract. The proteins separated by 2D PAGE were transferred to a PVDF membrane and probed with R. parkeri index patient serum. The numbers refer to the protein identities shown in Table . Arrows indicate

    Journal: Infection and Immunity

    Article Title: Proteomic Analysis of Rickettsia parkeri Strain Portsmouth ▿

    doi: 10.1128/IAI.00911-09

    Figure Lengend Snippet: 2D immunoblot of R. parkeri protein extract. The proteins separated by 2D PAGE were transferred to a PVDF membrane and probed with R. parkeri index patient serum. The numbers refer to the protein identities shown in Table . Arrows indicate

    Article Snippet: Unlabeled or biotin-labeled R. parkeri proteins separated by 2D PAGE were electroblotted onto Immun-Blot polyvinylidene difluoride (PVDF) membranes (Bio-Rad) by using an XCell II blot module (Invitrogen) according to the manufacturer's protocol.

    Techniques: Polyacrylamide Gel Electrophoresis

    Immunoblot analysis of purified C. difficile toxins A and B. Purified proteins (80 µg each) were subjected to 6% PAGE and transferred onto PVDF membranes. Each membrane was probed using monoclonal primary antibodies specific for toxin A or B. The Pierce ECL Western Blotting Kit was used to detect the bound antibodies. The membrane was exposed to X-ray film (Molecular Technologies, St Louis, MO) and processed using a Konica film processor (Konica Corporation, Tokyo, Japan). Sup, crude culture supernatant; Toxin A, purified toxin A; Toxin B, purified toxin B.

    Journal: PLoS ONE

    Article Title: Bile Salt Inhibition of Host Cell Damage by Clostridium Difficile Toxins

    doi: 10.1371/journal.pone.0079631

    Figure Lengend Snippet: Immunoblot analysis of purified C. difficile toxins A and B. Purified proteins (80 µg each) were subjected to 6% PAGE and transferred onto PVDF membranes. Each membrane was probed using monoclonal primary antibodies specific for toxin A or B. The Pierce ECL Western Blotting Kit was used to detect the bound antibodies. The membrane was exposed to X-ray film (Molecular Technologies, St Louis, MO) and processed using a Konica film processor (Konica Corporation, Tokyo, Japan). Sup, crude culture supernatant; Toxin A, purified toxin A; Toxin B, purified toxin B.

    Article Snippet: Purified C. difficile toxins A and B (80 µg each) were separated on 6% polyacrylamide electrophoresis (PAGE) gels and transferred onto Immun-Blot PVDF membrane (BioRad, Hercules, CA) using a Trans-Blot cell (BioRad) transfer apparatus.

    Techniques: Purification, Polyacrylamide Gel Electrophoresis, Western Blot

    Specificity of anti-GPCR serum IgG. ( a ) Anti-hNPFFR 2 IgG binding to deglycosylated hNPFFR 2 receptor. Total cell membrane prepared from hNPFFR 2 -expressing CHO cells were incubated (+) or not (−) with Peptide N Glycosidase F enzyme for 1 hour at 37°C. Membrane protein extracts were run on SDS-polyacrylamide gels and then probed with anti-hNPFFR 2 serum IgG after transfer onto PVDF membrane. The ability of anti-hNPFFR 2 antibodies to discriminate human NPFFR 2 used for immunization from highly homologous NPFFR 2 of murine origin was examined by cytofluorometry ( b ) and Western-blotting ( c ). In ( b ), anti-hNPFFR 2 serum IgG were incubated with wild-type CHO-K1 cells (open histogram) or CHO cells expressing NPFFR 2 (grey histogram) originating from human (hNPFFR 2 /CHO, left panel), mouse (mNPFFR 2 /CHO, middle panel) and rat (rNPFFR 2 /CHO, right panel) for 30 min at 4°C. Bound IgG were then revealed with biotin-conjugated goat anti-mouse antibodies followed by an additional incubation with allophycocyanin-labeled streptavidin. Staining of NPFFR 2 -expressing CHO cells by control serum IgG from normal non-immunized mice is shown in dotted lines. The figure shows one representative experiment out of 3 performed. In ( c ), membrane protein lysates from wild-type CHO-K1 (wt), hNPFFR 2 /CHO (h), mNPFFR 2 /CHO (m) and rNPFFR 2 /CHO (r) were run on SDS-polyacrylamide gels and then probed with either anti-hNPFFR 2 serum IgG (left panel) or normal serum IgG from non-immunized mouse (right panel) after transfer onto PVDF membrane. ( d ) The ability of anti-hMOR antibodies to bind to NH 2 -terminal extracellular segment of the hMOR was determined by Western-blotting. Cell membrane proteins from wild-type CHO-K1 (wt) and CHO cells expressing full-length (hMOR) or NH 2 -terminal truncated (Δ1-61hMOR) human MOR were probed with anti-hMOR serum IgG.

    Journal: PLoS ONE

    Article Title: Denatured G-Protein Coupled Receptors as Immunogens to Generate Highly Specific Antibodies

    doi: 10.1371/journal.pone.0046348

    Figure Lengend Snippet: Specificity of anti-GPCR serum IgG. ( a ) Anti-hNPFFR 2 IgG binding to deglycosylated hNPFFR 2 receptor. Total cell membrane prepared from hNPFFR 2 -expressing CHO cells were incubated (+) or not (−) with Peptide N Glycosidase F enzyme for 1 hour at 37°C. Membrane protein extracts were run on SDS-polyacrylamide gels and then probed with anti-hNPFFR 2 serum IgG after transfer onto PVDF membrane. The ability of anti-hNPFFR 2 antibodies to discriminate human NPFFR 2 used for immunization from highly homologous NPFFR 2 of murine origin was examined by cytofluorometry ( b ) and Western-blotting ( c ). In ( b ), anti-hNPFFR 2 serum IgG were incubated with wild-type CHO-K1 cells (open histogram) or CHO cells expressing NPFFR 2 (grey histogram) originating from human (hNPFFR 2 /CHO, left panel), mouse (mNPFFR 2 /CHO, middle panel) and rat (rNPFFR 2 /CHO, right panel) for 30 min at 4°C. Bound IgG were then revealed with biotin-conjugated goat anti-mouse antibodies followed by an additional incubation with allophycocyanin-labeled streptavidin. Staining of NPFFR 2 -expressing CHO cells by control serum IgG from normal non-immunized mice is shown in dotted lines. The figure shows one representative experiment out of 3 performed. In ( c ), membrane protein lysates from wild-type CHO-K1 (wt), hNPFFR 2 /CHO (h), mNPFFR 2 /CHO (m) and rNPFFR 2 /CHO (r) were run on SDS-polyacrylamide gels and then probed with either anti-hNPFFR 2 serum IgG (left panel) or normal serum IgG from non-immunized mouse (right panel) after transfer onto PVDF membrane. ( d ) The ability of anti-hMOR antibodies to bind to NH 2 -terminal extracellular segment of the hMOR was determined by Western-blotting. Cell membrane proteins from wild-type CHO-K1 (wt) and CHO cells expressing full-length (hMOR) or NH 2 -terminal truncated (Δ1-61hMOR) human MOR were probed with anti-hMOR serum IgG.

    Article Snippet: Western blot analysis Protein lysates prepared from Pichia pastoris cell extracts, GPCR-expressing CHO membranes, mouse olfactory bulb and cerebellum cell membranes or human spermatozoa were run on sodium dodecyl sulfate (SDS) 10% polyacrylamide gel electrophoresis and transferred onto a PVDF immun-blot membrane (Bio-Rad Laboratories, Hercules, CA).

    Techniques: Binding Assay, Expressing, Incubation, Western Blot, Labeling, Staining, Mouse Assay

    Purity of GPCR-enriched samples used as immunogens. Recombinant hNPFFR 2 (a), hKOR (b) and hMOR (c) with six histidine residues and a c-myc tag fused to their C-terminus were over-expressed in Pichia Pastoris . GPCR-enriched crude fractions obtained by differential centrifugation of GPCR-expressing yeast cell lysates were solubilized and then chromatographed on a nickel affinity column. Ni-bound GPCRs were eluted with imidazole-containing buffer. GPCR-enriched samples run in SDS-polyacrylamide gels were stained by silver nitrate (left panels) or probed with anti-c-myc monoclonal antibody after transfer onto PVDF membrane (right panels).

    Journal: PLoS ONE

    Article Title: Denatured G-Protein Coupled Receptors as Immunogens to Generate Highly Specific Antibodies

    doi: 10.1371/journal.pone.0046348

    Figure Lengend Snippet: Purity of GPCR-enriched samples used as immunogens. Recombinant hNPFFR 2 (a), hKOR (b) and hMOR (c) with six histidine residues and a c-myc tag fused to their C-terminus were over-expressed in Pichia Pastoris . GPCR-enriched crude fractions obtained by differential centrifugation of GPCR-expressing yeast cell lysates were solubilized and then chromatographed on a nickel affinity column. Ni-bound GPCRs were eluted with imidazole-containing buffer. GPCR-enriched samples run in SDS-polyacrylamide gels were stained by silver nitrate (left panels) or probed with anti-c-myc monoclonal antibody after transfer onto PVDF membrane (right panels).

    Article Snippet: Western blot analysis Protein lysates prepared from Pichia pastoris cell extracts, GPCR-expressing CHO membranes, mouse olfactory bulb and cerebellum cell membranes or human spermatozoa were run on sodium dodecyl sulfate (SDS) 10% polyacrylamide gel electrophoresis and transferred onto a PVDF immun-blot membrane (Bio-Rad Laboratories, Hercules, CA).

    Techniques: Recombinant, Centrifugation, Expressing, Affinity Column, Staining

    Binding of immune serum IgG to recombinant wild-type GPCRs expressed in CHO cells. The ability of immune serum IgG from mice immunized against hNPFFR 2 (upper panels), hKOR (middle panels) and hMOR (lower panels) to specifically bind to their corresponding receptors ( i.e. used for immunization) was assessed by western-blotting (a), confocal immunofluorescence microscopy (b), and cytofluorometry (c). In (a), membrane proteins extracted from untransfected CHO-K1 cells (left lanes) or from CHO-K1 cells expressing either hNPFFR 2 (hNPFFR 2 /CHO), hKOR (hKOR/CHO) or hMOR (hMOR/CHO) (right lanes) were run on SDS-polyacrylamide gel and transferred onto PVDF membrane. Protein extracts were probed with corresponding mouse immune sera. Bound IgG were revealed using horseradish peroxidase-labeled rabbit anti-mouse IgG antibodies. In (b), CHO cells expressing wild-type GPCR including hNPFFR 2 /CHO, hKOR/CHO, hMOR/CHO or CHO-K1 cells (insert) were incubated with immune sera collected from mice immunized against the corresponding receptor. Bound IgG were then revealed with Alexa 488-labeled goat anti-mouse IgG antibodies (green staining). Cell nuclei were stained in red with propidium iodide. Fluorescence images were acquired by confocal microscopy. In (c), the binding of immune serum IgG to CHO cells expressing their corresponding receptors was examined by cytofluorometry: hNPFFR 2 /CHO cells (upper panel), hKOR/CHO cells (middle panel) and hMOR/CHO cells (lower panels). GPCR-expressing CHO cells (grey histogram) and CHO-K1 cells (open histogram) were incubated with immune sera for 30 min at 4°C. Bound IgG were then revealed with biotin-conjugated goat anti-mouse antibodies followed by an additional incubation with allophycocyanin-labeled streptavidin. Backgrounds (dotted line) correspond to GPCR-expressing CHO cells or wild-type CHO-K1 cells stained with normal serum IgG from non-immunized mouse. The figure shows one representative experiment out of 3 performed.

    Journal: PLoS ONE

    Article Title: Denatured G-Protein Coupled Receptors as Immunogens to Generate Highly Specific Antibodies

    doi: 10.1371/journal.pone.0046348

    Figure Lengend Snippet: Binding of immune serum IgG to recombinant wild-type GPCRs expressed in CHO cells. The ability of immune serum IgG from mice immunized against hNPFFR 2 (upper panels), hKOR (middle panels) and hMOR (lower panels) to specifically bind to their corresponding receptors ( i.e. used for immunization) was assessed by western-blotting (a), confocal immunofluorescence microscopy (b), and cytofluorometry (c). In (a), membrane proteins extracted from untransfected CHO-K1 cells (left lanes) or from CHO-K1 cells expressing either hNPFFR 2 (hNPFFR 2 /CHO), hKOR (hKOR/CHO) or hMOR (hMOR/CHO) (right lanes) were run on SDS-polyacrylamide gel and transferred onto PVDF membrane. Protein extracts were probed with corresponding mouse immune sera. Bound IgG were revealed using horseradish peroxidase-labeled rabbit anti-mouse IgG antibodies. In (b), CHO cells expressing wild-type GPCR including hNPFFR 2 /CHO, hKOR/CHO, hMOR/CHO or CHO-K1 cells (insert) were incubated with immune sera collected from mice immunized against the corresponding receptor. Bound IgG were then revealed with Alexa 488-labeled goat anti-mouse IgG antibodies (green staining). Cell nuclei were stained in red with propidium iodide. Fluorescence images were acquired by confocal microscopy. In (c), the binding of immune serum IgG to CHO cells expressing their corresponding receptors was examined by cytofluorometry: hNPFFR 2 /CHO cells (upper panel), hKOR/CHO cells (middle panel) and hMOR/CHO cells (lower panels). GPCR-expressing CHO cells (grey histogram) and CHO-K1 cells (open histogram) were incubated with immune sera for 30 min at 4°C. Bound IgG were then revealed with biotin-conjugated goat anti-mouse antibodies followed by an additional incubation with allophycocyanin-labeled streptavidin. Backgrounds (dotted line) correspond to GPCR-expressing CHO cells or wild-type CHO-K1 cells stained with normal serum IgG from non-immunized mouse. The figure shows one representative experiment out of 3 performed.

    Article Snippet: Western blot analysis Protein lysates prepared from Pichia pastoris cell extracts, GPCR-expressing CHO membranes, mouse olfactory bulb and cerebellum cell membranes or human spermatozoa were run on sodium dodecyl sulfate (SDS) 10% polyacrylamide gel electrophoresis and transferred onto a PVDF immun-blot membrane (Bio-Rad Laboratories, Hercules, CA).

    Techniques: Binding Assay, Recombinant, Mouse Assay, Western Blot, Immunofluorescence, Microscopy, Expressing, Labeling, Incubation, Staining, Fluorescence, Confocal Microscopy

    Binding of immune serum IgG to endogenously expressed GPCRs. In ( a ), protein lysates prepared from human spermatozoids were run on SDS-polyacrylamide gels and then probed with either control serum IgG from normal non-immunized mice, anti-hMOR serum IgG or anti-hKOR serum IgG after transfer onto PVDF membrane. In ( b ), human SH-SY5Y neuroblastoma cells were permeabilized with 0.05% Triton ×100 prior to be incubated with anti-hMOR serum IgG. Bound IgG were revealed with Alexa 488-labeled goat anti-mouse IgG antibodies (green staining). Cell nuclei were stained in blue with DAPI. Fluorescence images were acquired by confocal microscopy. Original magnification ×63. ( c ) The cross-reactivity of anti-hMOR antibodies towards murine MOR-containing tissue-extract antigens was examined by Western-blotting. Membrane protein lysates from hMOR/CHO (hMOR), mouse cerebellum (mCVT) and mouse olfactory bulb (mOB) were run on SDS-polyacrylamide gels and then probed with anti-hMOR serum IgG.

    Journal: PLoS ONE

    Article Title: Denatured G-Protein Coupled Receptors as Immunogens to Generate Highly Specific Antibodies

    doi: 10.1371/journal.pone.0046348

    Figure Lengend Snippet: Binding of immune serum IgG to endogenously expressed GPCRs. In ( a ), protein lysates prepared from human spermatozoids were run on SDS-polyacrylamide gels and then probed with either control serum IgG from normal non-immunized mice, anti-hMOR serum IgG or anti-hKOR serum IgG after transfer onto PVDF membrane. In ( b ), human SH-SY5Y neuroblastoma cells were permeabilized with 0.05% Triton ×100 prior to be incubated with anti-hMOR serum IgG. Bound IgG were revealed with Alexa 488-labeled goat anti-mouse IgG antibodies (green staining). Cell nuclei were stained in blue with DAPI. Fluorescence images were acquired by confocal microscopy. Original magnification ×63. ( c ) The cross-reactivity of anti-hMOR antibodies towards murine MOR-containing tissue-extract antigens was examined by Western-blotting. Membrane protein lysates from hMOR/CHO (hMOR), mouse cerebellum (mCVT) and mouse olfactory bulb (mOB) were run on SDS-polyacrylamide gels and then probed with anti-hMOR serum IgG.

    Article Snippet: Western blot analysis Protein lysates prepared from Pichia pastoris cell extracts, GPCR-expressing CHO membranes, mouse olfactory bulb and cerebellum cell membranes or human spermatozoa were run on sodium dodecyl sulfate (SDS) 10% polyacrylamide gel electrophoresis and transferred onto a PVDF immun-blot membrane (Bio-Rad Laboratories, Hercules, CA).

    Techniques: Binding Assay, Mouse Assay, Incubation, Labeling, Staining, Fluorescence, Confocal Microscopy, Western Blot

    Detection of nuclear proteins specifically bound to the CORE motif. A, Gel mobility shift assay using the CORE probe. Fifteen micrograms of nucleoproteins (lanes 2–6) from rice germinating embryos were incubated with 3 ng of 32 P-labeled CORE probe at room temperature and then separated by PAGE. A nonlabeled probe was added as a competitor in the binding reaction (6 ng in lane 3, 12 ng in lane 4, and 24 ng in lane 5, respectively). Poly(dI-dC)·poly(dI-dC) was added by 30 ng in lanes 1 to 5 and 60 ng in lane 6, respectively. An asterisk indicates that poly(dI-dC)·poly(dI-dC) was used as a nonspecific competitor. The signal bands of specific complexes are indicated by arrowheads. B, Gel mobility shift assay using the mutant probes. Binding reactions were carried out with 15 μ g of nucleoproteins, 3 ng of 32 P-labeled CORE probe or mutant probes (M1, M2, and M3), and 50 ng of poly(dI-dC)·poly(dI-dC). C, Southwestern blot using the CORE probe. Ten or 15 μ g of nucleoproteins from rice germinating embryos was fractionated by SDS-PAGE and then blotted onto a polyvinylidene difluoride membrane. The blot was probed with 32 P-labeled CORE fragment or mutated CORE fragments (M1, M2, and M3).

    Journal: Plant Physiology

    Article Title: A Novel cis-Element That Is Responsive to Oxidative Stress Regulates Three Antioxidant Defense Genes in Rice 1

    doi: 10.1104/pp.104.045658

    Figure Lengend Snippet: Detection of nuclear proteins specifically bound to the CORE motif. A, Gel mobility shift assay using the CORE probe. Fifteen micrograms of nucleoproteins (lanes 2–6) from rice germinating embryos were incubated with 3 ng of 32 P-labeled CORE probe at room temperature and then separated by PAGE. A nonlabeled probe was added as a competitor in the binding reaction (6 ng in lane 3, 12 ng in lane 4, and 24 ng in lane 5, respectively). Poly(dI-dC)·poly(dI-dC) was added by 30 ng in lanes 1 to 5 and 60 ng in lane 6, respectively. An asterisk indicates that poly(dI-dC)·poly(dI-dC) was used as a nonspecific competitor. The signal bands of specific complexes are indicated by arrowheads. B, Gel mobility shift assay using the mutant probes. Binding reactions were carried out with 15 μ g of nucleoproteins, 3 ng of 32 P-labeled CORE probe or mutant probes (M1, M2, and M3), and 50 ng of poly(dI-dC)·poly(dI-dC). C, Southwestern blot using the CORE probe. Ten or 15 μ g of nucleoproteins from rice germinating embryos was fractionated by SDS-PAGE and then blotted onto a polyvinylidene difluoride membrane. The blot was probed with 32 P-labeled CORE fragment or mutated CORE fragments (M1, M2, and M3).

    Article Snippet: Nucleoprotein separated by SDS-PAGE thorough 12% (w/v) gel was transferred to a polyvinylidene difluoride (PVDF) membrane (Immun-Blot PVDF Membrane; Bio-Rad).

    Techniques: Mobility Shift, Incubation, Labeling, Polyacrylamide Gel Electrophoresis, Binding Assay, Mutagenesis, Southwestern Blot, SDS Page

    The over-expression of RALDH1 resulted in the RAL-mediated induction of Srebp-1c in 833/15 INS-1 cells. A. The adenovirus-mediated Raldh1 mRNA expression. B. Immuno-blot of the over-expression of RALDH1 protein in INS-1 cells. Whole cell lysates (50 µg/sample) of the control cells (lane 1), cells infected by the indicated pfu of Ad-β-gal (lane 2) or Ad-Raldh1 (lanes 3–5) were separated in 8% SDS protein gels, and transferred to the PVDF membranes. Primary antibodies to RALDH1 (1∶1000 dilution in TBST containing 5% dry milk), and to β-Actin (1∶1000 dilution in TBST containing 5% bovine serum albumin) were recognized by goat anti-rabbit IgG conjugated to horseradish peroxidase, and visualized by chemiluminescence. The films were scanned and presented as described in the Material and Methods . C. RAL only induced Srebp-1c expression in cells over-expressing RALDH1, but not β-gal. D. RA induced Srebp-1c expression in cells over-expressing either β-gal or RALDH1. Results were presented as means ± SD of fold inductions (* for comparing the different dosages of RAL in cells infected by Ad-Raldh1 using one way ANOVA, n = 3, all p

    Journal: PLoS ONE

    Article Title: The Hepatic Raldh1 Expression Is elevated in Zucker Fatty Rats and Its Over-Expression Introduced the Retinal-Induced Srebp-1c Expression in INS-1 Cells

    doi: 10.1371/journal.pone.0045210

    Figure Lengend Snippet: The over-expression of RALDH1 resulted in the RAL-mediated induction of Srebp-1c in 833/15 INS-1 cells. A. The adenovirus-mediated Raldh1 mRNA expression. B. Immuno-blot of the over-expression of RALDH1 protein in INS-1 cells. Whole cell lysates (50 µg/sample) of the control cells (lane 1), cells infected by the indicated pfu of Ad-β-gal (lane 2) or Ad-Raldh1 (lanes 3–5) were separated in 8% SDS protein gels, and transferred to the PVDF membranes. Primary antibodies to RALDH1 (1∶1000 dilution in TBST containing 5% dry milk), and to β-Actin (1∶1000 dilution in TBST containing 5% bovine serum albumin) were recognized by goat anti-rabbit IgG conjugated to horseradish peroxidase, and visualized by chemiluminescence. The films were scanned and presented as described in the Material and Methods . C. RAL only induced Srebp-1c expression in cells over-expressing RALDH1, but not β-gal. D. RA induced Srebp-1c expression in cells over-expressing either β-gal or RALDH1. Results were presented as means ± SD of fold inductions (* for comparing the different dosages of RAL in cells infected by Ad-Raldh1 using one way ANOVA, n = 3, all p

    Article Snippet: Proteins (40 μg/lane) in whole cell lysates were separated on SDS-PAGE, transferred to BIO-RAD Immuno-Blot PVDF membrane (Hercules, CA) and detected with primary antibodies to RALDH1 (for , catalog #2052-1, Epitomics, Burlingame, CA 94010), RALDH1 (for , catalog #AP1465a, Abgent, San Diego, CA 92121), CYP26A1 (catalog # CYP26A11-A, Alpha Diagnostics International, TX 78244), and β-Actin (#4970 s, Cell Signaling Technology, Danvers, MA 01923) according to the protocols provided by the manufacturers.

    Techniques: Over Expression, Expressing, Infection

    YAP and WBP2 are highly expressed in human epidermal SCs and upregulated in cSCC. ( a , b ) Representative images (single optical planes) of adult ( a ) and fetal (17 weeks gestation) ( b ) human skin sections immunolabelled with the indicated antibodies and counterstained with DAPI to reveal nuclei. White dotted lines demarcate dermal-epidermal boundaries. Scale bars, 50 μm. ( c ) Western blot analysis of NHKs, SCC13 cells and primary cSCC cells (SCC-NR) using antibodies against WBP2. Tubulin was used as loading control. ( d , e ) Semiquantitative analysis (H-score) of YAP ( d ) and WBP2 ( e ) immunostaining intensities (individual data points) in a panel of cSCC- compared with normal skin sections (dotted line). Red lines represent the mean. ( f ) Western blot analysis of enriched populations of stem- (SC), transit amplifying- (TA), and terminally differentiated (D) cells using antibodies against YAP, WBP2, ITGβ1, and involucrin (IVL). Equal protein loading was confirmed by enhanced tryptophan fluorescence imaging (Bio-Rad) of PVDF membranes (loading control). ( g ) Representative images (maximum intensity projections) of expanding and mature SC colonies as well as abortive colonies, immunolabelled with indicated antibodies and counterstained for DAPI to reveal nuclei. Scale bars, 100 μm. PVDF, polyvinylidene difluoride.

    Journal: Nature Communications

    Article Title: A genome-wide screen identifies YAP/WBP2 interplay conferring growth advantage on human epidermal stem cells

    doi: 10.1038/ncomms14744

    Figure Lengend Snippet: YAP and WBP2 are highly expressed in human epidermal SCs and upregulated in cSCC. ( a , b ) Representative images (single optical planes) of adult ( a ) and fetal (17 weeks gestation) ( b ) human skin sections immunolabelled with the indicated antibodies and counterstained with DAPI to reveal nuclei. White dotted lines demarcate dermal-epidermal boundaries. Scale bars, 50 μm. ( c ) Western blot analysis of NHKs, SCC13 cells and primary cSCC cells (SCC-NR) using antibodies against WBP2. Tubulin was used as loading control. ( d , e ) Semiquantitative analysis (H-score) of YAP ( d ) and WBP2 ( e ) immunostaining intensities (individual data points) in a panel of cSCC- compared with normal skin sections (dotted line). Red lines represent the mean. ( f ) Western blot analysis of enriched populations of stem- (SC), transit amplifying- (TA), and terminally differentiated (D) cells using antibodies against YAP, WBP2, ITGβ1, and involucrin (IVL). Equal protein loading was confirmed by enhanced tryptophan fluorescence imaging (Bio-Rad) of PVDF membranes (loading control). ( g ) Representative images (maximum intensity projections) of expanding and mature SC colonies as well as abortive colonies, immunolabelled with indicated antibodies and counterstained for DAPI to reveal nuclei. Scale bars, 100 μm. PVDF, polyvinylidene difluoride.

    Article Snippet: Equivalent quantities of RIPA-solubilized proteins were resolved by SDS-PAGE in 4–20% Criterion TGX Stain-Free Precast Gels and transferred to Immun-Blot Low Fluorescence polyvinylidene difluoride membranes (Bio-Rad Laboratories) using the Trans-Blot Turbo transfer system (Bio-Rad Laboratories).

    Techniques: Western Blot, Immunostaining, Fluorescence, Imaging