peroxidase-conjugated secondary antibody Search Results


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  • 99
    Millipore secondary peroxidase conjugated secondary antibodies
    Secondary Peroxidase Conjugated Secondary Antibodies, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc peroxidase conjugated secondary antibodies
    Immunofluorescence analysis of Rab44 and markers for haematopoietic stem cells in the bone marrow. ( a ) The fixed sections of femur containing bone marrow were blocked in PBS containing 5% normal donkey serum. The samples were incubated with rabbit polyclonal <t>anti-Rab44</t> IgG (1:1,000) as the first antibody followed by fluorescent labelling with Alexa fluor <t>488-conjugated</t> anti-rabbit IgG and then visualised by confocal laser microscopy. Bar: 20 μm. ( b , c ) The mouse bone was fixed, permeabilised with 0.1% Triton X-100 in PBS, and then allowed to react with antibodies against Rab44 and ( b ) CD117 or ( c ) Sca-1. After washing, the samples were incubated with a fluorescence-labelled <t>secondary</t> antibody and then visualised by confocal laser microscopy. Bar: 5 μm.
    Peroxidase Conjugated Secondary Antibodies, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 92/100, based on 2225 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Bio-Rad horseradish peroxidaseconjugated secondary antibody
    Immunofluorescence analysis of Rab44 and markers for haematopoietic stem cells in the bone marrow. ( a ) The fixed sections of femur containing bone marrow were blocked in PBS containing 5% normal donkey serum. The samples were incubated with rabbit polyclonal <t>anti-Rab44</t> IgG (1:1,000) as the first antibody followed by fluorescent labelling with Alexa fluor <t>488-conjugated</t> anti-rabbit IgG and then visualised by confocal laser microscopy. Bar: 20 μm. ( b , c ) The mouse bone was fixed, permeabilised with 0.1% Triton X-100 in PBS, and then allowed to react with antibodies against Rab44 and ( b ) CD117 or ( c ) Sca-1. After washing, the samples were incubated with a fluorescence-labelled <t>secondary</t> antibody and then visualised by confocal laser microscopy. Bar: 5 μm.
    Horseradish Peroxidaseconjugated Secondary Antibody, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc peroxidase conjugated secondary antibody solution
    Immunofluorescence analysis of Rab44 and markers for haematopoietic stem cells in the bone marrow. ( a ) The fixed sections of femur containing bone marrow were blocked in PBS containing 5% normal donkey serum. The samples were incubated with rabbit polyclonal <t>anti-Rab44</t> IgG (1:1,000) as the first antibody followed by fluorescent labelling with Alexa fluor <t>488-conjugated</t> anti-rabbit IgG and then visualised by confocal laser microscopy. Bar: 20 μm. ( b , c ) The mouse bone was fixed, permeabilised with 0.1% Triton X-100 in PBS, and then allowed to react with antibodies against Rab44 and ( b ) CD117 or ( c ) Sca-1. After washing, the samples were incubated with a fluorescence-labelled <t>secondary</t> antibody and then visualised by confocal laser microscopy. Bar: 5 μm.
    Peroxidase Conjugated Secondary Antibody Solution, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore peroxidase conjugated secondary antibodies
    Immunofluorescence analysis of Rab44 and markers for haematopoietic stem cells in the bone marrow. ( a ) The fixed sections of femur containing bone marrow were blocked in PBS containing 5% normal donkey serum. The samples were incubated with rabbit polyclonal <t>anti-Rab44</t> IgG (1:1,000) as the first antibody followed by fluorescent labelling with Alexa fluor <t>488-conjugated</t> anti-rabbit IgG and then visualised by confocal laser microscopy. Bar: 20 μm. ( b , c ) The mouse bone was fixed, permeabilised with 0.1% Triton X-100 in PBS, and then allowed to react with antibodies against Rab44 and ( b ) CD117 or ( c ) Sca-1. After washing, the samples were incubated with a fluorescence-labelled <t>secondary</t> antibody and then visualised by confocal laser microscopy. Bar: 5 μm.
    Peroxidase Conjugated Secondary Antibodies, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 2733 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Roche peroxidase conjugated secondary antibodies
    Immunofluorescence analysis of Rab44 and markers for haematopoietic stem cells in the bone marrow. ( a ) The fixed sections of femur containing bone marrow were blocked in PBS containing 5% normal donkey serum. The samples were incubated with rabbit polyclonal <t>anti-Rab44</t> IgG (1:1,000) as the first antibody followed by fluorescent labelling with Alexa fluor <t>488-conjugated</t> anti-rabbit IgG and then visualised by confocal laser microscopy. Bar: 20 μm. ( b , c ) The mouse bone was fixed, permeabilised with 0.1% Triton X-100 in PBS, and then allowed to react with antibodies against Rab44 and ( b ) CD117 or ( c ) Sca-1. After washing, the samples were incubated with a fluorescence-labelled <t>secondary</t> antibody and then visualised by confocal laser microscopy. Bar: 5 μm.
    Peroxidase Conjugated Secondary Antibodies, supplied by Roche, used in various techniques. Bioz Stars score: 92/100, based on 99 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Rockland Immunochemicals peroxidase conjugated secondary antibody
    Immunofluorescence analysis of Rab44 and markers for haematopoietic stem cells in the bone marrow. ( a ) The fixed sections of femur containing bone marrow were blocked in PBS containing 5% normal donkey serum. The samples were incubated with rabbit polyclonal <t>anti-Rab44</t> IgG (1:1,000) as the first antibody followed by fluorescent labelling with Alexa fluor <t>488-conjugated</t> anti-rabbit IgG and then visualised by confocal laser microscopy. Bar: 20 μm. ( b , c ) The mouse bone was fixed, permeabilised with 0.1% Triton X-100 in PBS, and then allowed to react with antibodies against Rab44 and ( b ) CD117 or ( c ) Sca-1. After washing, the samples were incubated with a fluorescence-labelled <t>secondary</t> antibody and then visualised by confocal laser microscopy. Bar: 5 μm.
    Peroxidase Conjugated Secondary Antibody, supplied by Rockland Immunochemicals, used in various techniques. Bioz Stars score: 90/100, based on 49 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Bangalore Genei peroxidase conjugated secondary antibodies
    Immunofluorescence analysis of Rab44 and markers for haematopoietic stem cells in the bone marrow. ( a ) The fixed sections of femur containing bone marrow were blocked in PBS containing 5% normal donkey serum. The samples were incubated with rabbit polyclonal <t>anti-Rab44</t> IgG (1:1,000) as the first antibody followed by fluorescent labelling with Alexa fluor <t>488-conjugated</t> anti-rabbit IgG and then visualised by confocal laser microscopy. Bar: 20 μm. ( b , c ) The mouse bone was fixed, permeabilised with 0.1% Triton X-100 in PBS, and then allowed to react with antibodies against Rab44 and ( b ) CD117 or ( c ) Sca-1. After washing, the samples were incubated with a fluorescence-labelled <t>secondary</t> antibody and then visualised by confocal laser microscopy. Bar: 5 μm.
    Peroxidase Conjugated Secondary Antibodies, supplied by Bangalore Genei, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Covalab peroxidase conjugated secondary antibodies
    Immunofluorescence analysis of Rab44 and markers for haematopoietic stem cells in the bone marrow. ( a ) The fixed sections of femur containing bone marrow were blocked in PBS containing 5% normal donkey serum. The samples were incubated with rabbit polyclonal <t>anti-Rab44</t> IgG (1:1,000) as the first antibody followed by fluorescent labelling with Alexa fluor <t>488-conjugated</t> anti-rabbit IgG and then visualised by confocal laser microscopy. Bar: 20 μm. ( b , c ) The mouse bone was fixed, permeabilised with 0.1% Triton X-100 in PBS, and then allowed to react with antibodies against Rab44 and ( b ) CD117 or ( c ) Sca-1. After washing, the samples were incubated with a fluorescence-labelled <t>secondary</t> antibody and then visualised by confocal laser microscopy. Bar: 5 μm.
    Peroxidase Conjugated Secondary Antibodies, supplied by Covalab, used in various techniques. Bioz Stars score: 92/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Agilent technologies peroxidase conjugated secondary antibodies
    Immunofluorescence analysis of Rab44 and markers for haematopoietic stem cells in the bone marrow. ( a ) The fixed sections of femur containing bone marrow were blocked in PBS containing 5% normal donkey serum. The samples were incubated with rabbit polyclonal <t>anti-Rab44</t> IgG (1:1,000) as the first antibody followed by fluorescent labelling with Alexa fluor <t>488-conjugated</t> anti-rabbit IgG and then visualised by confocal laser microscopy. Bar: 20 μm. ( b , c ) The mouse bone was fixed, permeabilised with 0.1% Triton X-100 in PBS, and then allowed to react with antibodies against Rab44 and ( b ) CD117 or ( c ) Sca-1. After washing, the samples were incubated with a fluorescence-labelled <t>secondary</t> antibody and then visualised by confocal laser microscopy. Bar: 5 μm.
    Peroxidase Conjugated Secondary Antibodies, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 93/100, based on 1205 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Beyotime peroxidase conjugated secondary antibody
    Immunofluorescence analysis of Rab44 and markers for haematopoietic stem cells in the bone marrow. ( a ) The fixed sections of femur containing bone marrow were blocked in PBS containing 5% normal donkey serum. The samples were incubated with rabbit polyclonal <t>anti-Rab44</t> IgG (1:1,000) as the first antibody followed by fluorescent labelling with Alexa fluor <t>488-conjugated</t> anti-rabbit IgG and then visualised by confocal laser microscopy. Bar: 20 μm. ( b , c ) The mouse bone was fixed, permeabilised with 0.1% Triton X-100 in PBS, and then allowed to react with antibodies against Rab44 and ( b ) CD117 or ( c ) Sca-1. After washing, the samples were incubated with a fluorescence-labelled <t>secondary</t> antibody and then visualised by confocal laser microscopy. Bar: 5 μm.
    Peroxidase Conjugated Secondary Antibody, supplied by Beyotime, used in various techniques. Bioz Stars score: 92/100, based on 563 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ge healthcare peroxidase conjugated secondary antibodies
    Avastin attenuates astrogliosis and blood vessel formation in the injured cortex. a, c Cortical sections were obtained from mice in which Avastin or PBS was infused into the ventricle 14 d post-ATP injection. GFAP and CoL1A1 were visualized with Alexa-488 and Alexa-594 <t>conjugated</t> <t>secondary</t> <t>antibodies</t> ( a ) or biotinylated secondary antibodies and DAB-based color reaction ( c ). b Relative fluorescence intensity of GFAP and CoL1A1 were measured using ZEN software and plotted. Values are means ± SEMs for animals treated with saline ( n = 4) or Avastin ( n = 3) (*, p
    Peroxidase Conjugated Secondary Antibodies, supplied by ge healthcare, used in various techniques. Bioz Stars score: 93/100, based on 7561 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Promega peroxidase conjugated secondary antibody
    Avastin attenuates astrogliosis and blood vessel formation in the injured cortex. a, c Cortical sections were obtained from mice in which Avastin or PBS was infused into the ventricle 14 d post-ATP injection. GFAP and CoL1A1 were visualized with Alexa-488 and Alexa-594 <t>conjugated</t> <t>secondary</t> <t>antibodies</t> ( a ) or biotinylated secondary antibodies and DAB-based color reaction ( c ). b Relative fluorescence intensity of GFAP and CoL1A1 were measured using ZEN software and plotted. Values are means ± SEMs for animals treated with saline ( n = 4) or Avastin ( n = 3) (*, p
    Peroxidase Conjugated Secondary Antibody, supplied by Promega, used in various techniques. Bioz Stars score: 93/100, based on 318 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology peroxidase conjugated secondary antibody
    Agonist-induced DOP receptor phosphorylation and internalization. ( A,B top) Stably HA-tagged hDOP receptor-expressing HEK293 cells were preincubated with anti-HA <t>antibody,</t> followed by stimulation with 10 µM DPDPE, DADLE, SNC80, ADL5859, AR-M1000390, deltorphin I, deltorphin II, [Met]-enkephalin, [Leu]-enkephalin, fentanyl, (−)-methadone, morphine, morphine-6-glucuronide (M6G), buprenorphine (BUP), norbuprenorphine (norBUP) or vehicle for 30 min at 37 °C. Cells were fixed, permeabilized, immunofluorescently stained, and subsequently examined using confocal microscopy. Images are representative, n = 3. Scale bar, 20 µm. (A,B bottom) HEK293 cells stably expressing HA-hDOP receptor were stimulated with the compounds listed in (A) or vehicle at concentrations ranging from 10 -9 to 10 -5 M for 10 min at 37 °C. Lysates were immunoblotted with antibodies to pT361 or pS363. Blots were stripped and reprobed with the anti-HA antibody. Blots are representative, n = 3-5. (C) Cells described in ( A ) were preincubated with anti-HA antibody and stimulated with vehicle or 10 µM of compounds listed in ( A ) for 30 min at 37 °C. Cells were fixed and labeled with a <t>peroxidase-conjugated</t> <t>secondary</t> antibody. Receptor internalization was measured by ELISA and quantified as the percentage of internalized receptors in agonist-treated cells compared to untreated cells. Data are means ± SEM of five independent experiments performed in quadruplicate. Results were analyzed by one-way ANOVA followed by Bonferroni’s post-hoc test (*p
    Peroxidase Conjugated Secondary Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 94/100, based on 5446 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Boehringer Mannheim peroxidase conjugated secondary antibodies
    Agonist-induced DOP receptor phosphorylation and internalization. ( A,B top) Stably HA-tagged hDOP receptor-expressing HEK293 cells were preincubated with anti-HA <t>antibody,</t> followed by stimulation with 10 µM DPDPE, DADLE, SNC80, ADL5859, AR-M1000390, deltorphin I, deltorphin II, [Met]-enkephalin, [Leu]-enkephalin, fentanyl, (−)-methadone, morphine, morphine-6-glucuronide (M6G), buprenorphine (BUP), norbuprenorphine (norBUP) or vehicle for 30 min at 37 °C. Cells were fixed, permeabilized, immunofluorescently stained, and subsequently examined using confocal microscopy. Images are representative, n = 3. Scale bar, 20 µm. (A,B bottom) HEK293 cells stably expressing HA-hDOP receptor were stimulated with the compounds listed in (A) or vehicle at concentrations ranging from 10 -9 to 10 -5 M for 10 min at 37 °C. Lysates were immunoblotted with antibodies to pT361 or pS363. Blots were stripped and reprobed with the anti-HA antibody. Blots are representative, n = 3-5. (C) Cells described in ( A ) were preincubated with anti-HA antibody and stimulated with vehicle or 10 µM of compounds listed in ( A ) for 30 min at 37 °C. Cells were fixed and labeled with a <t>peroxidase-conjugated</t> <t>secondary</t> antibody. Receptor internalization was measured by ELISA and quantified as the percentage of internalized receptors in agonist-treated cells compared to untreated cells. Data are means ± SEM of five independent experiments performed in quadruplicate. Results were analyzed by one-way ANOVA followed by Bonferroni’s post-hoc test (*p
    Peroxidase Conjugated Secondary Antibodies, supplied by Boehringer Mannheim, used in various techniques. Bioz Stars score: 92/100, based on 65 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Proteintech peroxidase conjugated secondary antibody
    Agonist-induced DOP receptor phosphorylation and internalization. ( A,B top) Stably HA-tagged hDOP receptor-expressing HEK293 cells were preincubated with anti-HA <t>antibody,</t> followed by stimulation with 10 µM DPDPE, DADLE, SNC80, ADL5859, AR-M1000390, deltorphin I, deltorphin II, [Met]-enkephalin, [Leu]-enkephalin, fentanyl, (−)-methadone, morphine, morphine-6-glucuronide (M6G), buprenorphine (BUP), norbuprenorphine (norBUP) or vehicle for 30 min at 37 °C. Cells were fixed, permeabilized, immunofluorescently stained, and subsequently examined using confocal microscopy. Images are representative, n = 3. Scale bar, 20 µm. (A,B bottom) HEK293 cells stably expressing HA-hDOP receptor were stimulated with the compounds listed in (A) or vehicle at concentrations ranging from 10 -9 to 10 -5 M for 10 min at 37 °C. Lysates were immunoblotted with antibodies to pT361 or pS363. Blots were stripped and reprobed with the anti-HA antibody. Blots are representative, n = 3-5. (C) Cells described in ( A ) were preincubated with anti-HA antibody and stimulated with vehicle or 10 µM of compounds listed in ( A ) for 30 min at 37 °C. Cells were fixed and labeled with a <t>peroxidase-conjugated</t> <t>secondary</t> antibody. Receptor internalization was measured by ELISA and quantified as the percentage of internalized receptors in agonist-treated cells compared to untreated cells. Data are means ± SEM of five independent experiments performed in quadruplicate. Results were analyzed by one-way ANOVA followed by Bonferroni’s post-hoc test (*p
    Peroxidase Conjugated Secondary Antibody, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 372 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Thermo Fisher peroxidase conjugated secondary antibodies
    Agonist-induced DOP receptor phosphorylation and internalization. ( A,B top) Stably HA-tagged hDOP receptor-expressing HEK293 cells were preincubated with anti-HA <t>antibody,</t> followed by stimulation with 10 µM DPDPE, DADLE, SNC80, ADL5859, AR-M1000390, deltorphin I, deltorphin II, [Met]-enkephalin, [Leu]-enkephalin, fentanyl, (−)-methadone, morphine, morphine-6-glucuronide (M6G), buprenorphine (BUP), norbuprenorphine (norBUP) or vehicle for 30 min at 37 °C. Cells were fixed, permeabilized, immunofluorescently stained, and subsequently examined using confocal microscopy. Images are representative, n = 3. Scale bar, 20 µm. (A,B bottom) HEK293 cells stably expressing HA-hDOP receptor were stimulated with the compounds listed in (A) or vehicle at concentrations ranging from 10 -9 to 10 -5 M for 10 min at 37 °C. Lysates were immunoblotted with antibodies to pT361 or pS363. Blots were stripped and reprobed with the anti-HA antibody. Blots are representative, n = 3-5. (C) Cells described in ( A ) were preincubated with anti-HA antibody and stimulated with vehicle or 10 µM of compounds listed in ( A ) for 30 min at 37 °C. Cells were fixed and labeled with a <t>peroxidase-conjugated</t> <t>secondary</t> antibody. Receptor internalization was measured by ELISA and quantified as the percentage of internalized receptors in agonist-treated cells compared to untreated cells. Data are means ± SEM of five independent experiments performed in quadruplicate. Results were analyzed by one-way ANOVA followed by Bonferroni’s post-hoc test (*p
    Peroxidase Conjugated Secondary Antibodies, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 5275 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Immunofluorescence analysis of Rab44 and markers for haematopoietic stem cells in the bone marrow. ( a ) The fixed sections of femur containing bone marrow were blocked in PBS containing 5% normal donkey serum. The samples were incubated with rabbit polyclonal anti-Rab44 IgG (1:1,000) as the first antibody followed by fluorescent labelling with Alexa fluor 488-conjugated anti-rabbit IgG and then visualised by confocal laser microscopy. Bar: 20 μm. ( b , c ) The mouse bone was fixed, permeabilised with 0.1% Triton X-100 in PBS, and then allowed to react with antibodies against Rab44 and ( b ) CD117 or ( c ) Sca-1. After washing, the samples were incubated with a fluorescence-labelled secondary antibody and then visualised by confocal laser microscopy. Bar: 5 μm.

    Journal: Scientific Reports

    Article Title: Expression and localisation of Rab44 in immune-related cells change during cell differentiation and stimulation

    doi: 10.1038/s41598-020-67638-7

    Figure Lengend Snippet: Immunofluorescence analysis of Rab44 and markers for haematopoietic stem cells in the bone marrow. ( a ) The fixed sections of femur containing bone marrow were blocked in PBS containing 5% normal donkey serum. The samples were incubated with rabbit polyclonal anti-Rab44 IgG (1:1,000) as the first antibody followed by fluorescent labelling with Alexa fluor 488-conjugated anti-rabbit IgG and then visualised by confocal laser microscopy. Bar: 20 μm. ( b , c ) The mouse bone was fixed, permeabilised with 0.1% Triton X-100 in PBS, and then allowed to react with antibodies against Rab44 and ( b ) CD117 or ( c ) Sca-1. After washing, the samples were incubated with a fluorescence-labelled secondary antibody and then visualised by confocal laser microscopy. Bar: 5 μm.

    Article Snippet: The blots were blocked with 5% nonfat milk solution containing Tris-buffered saline (TBS)/0.1% Tween 20 for 1 h at 25 °C, probed with various antibodies overnight at 4 °C, washed, incubated with horseradish peroxidase-conjugated secondary antibodies (Cell Signaling Technology, Danvers, MA, USA), and finally detected with ECL-Prime (GE Healthcare Life Sciences, Tokyo, Japan).

    Techniques: Immunofluorescence, Incubation, Microscopy, Fluorescence

    Avastin attenuates astrogliosis and blood vessel formation in the injured cortex. a, c Cortical sections were obtained from mice in which Avastin or PBS was infused into the ventricle 14 d post-ATP injection. GFAP and CoL1A1 were visualized with Alexa-488 and Alexa-594 conjugated secondary antibodies ( a ) or biotinylated secondary antibodies and DAB-based color reaction ( c ). b Relative fluorescence intensity of GFAP and CoL1A1 were measured using ZEN software and plotted. Values are means ± SEMs for animals treated with saline ( n = 4) or Avastin ( n = 3) (*, p

    Journal: Molecular Brain

    Article Title: Region-specific astrogliosis: differential vessel formation contributes to different patterns of astrogliosis in the cortex and striatum

    doi: 10.1186/s13041-020-00642-0

    Figure Lengend Snippet: Avastin attenuates astrogliosis and blood vessel formation in the injured cortex. a, c Cortical sections were obtained from mice in which Avastin or PBS was infused into the ventricle 14 d post-ATP injection. GFAP and CoL1A1 were visualized with Alexa-488 and Alexa-594 conjugated secondary antibodies ( a ) or biotinylated secondary antibodies and DAB-based color reaction ( c ). b Relative fluorescence intensity of GFAP and CoL1A1 were measured using ZEN software and plotted. Values are means ± SEMs for animals treated with saline ( n = 4) or Avastin ( n = 3) (*, p

    Article Snippet: After blocking with 5% skim milk (Seoul Dairy Coop, Seoul, Korea), the nitrocellulose membrane was sequentially incubated with primary antibodies (Table ), peroxidase-conjugated secondary antibodies (Koma Biotech, Seoul, Korea), and enhanced chemiluminescence reagents (Daeil Lab Services, Seoul, Korea).

    Techniques: Mouse Assay, Injection, Fluorescence, Software

    Region-specific blood vessel formation and locations of perivascular cells in the injured brain. a Sections obtained from the intact and ATP-injected cortex and striatum at the indicated times were immunostained for CD31 to label blood vessels. Arrowheads, vessels located along the meninges in the intact cortex; arrows, vessels in the parenchyma in intact and injured brains. b Colocalization of CD31 and Col1a1. Sections from intact and ATP-injected brains were double-labeled with antibodies for CD31 and Col1a1 (perivascular fibroblasts), and visualized using Alexa 488- and 594-conjugated secondary antibodies. CD31 and Col1a1 were colocalized in the intact and injured cortex and striatum (arrows). Dotted lines, edges of the damage areas. c Sections were double-labeled with antibodies for GFAP and CoL1A1. Arrows, astrocytes near blood vessels and/or in vessel-rich regions; arrowheads, astrocytes in vessel-rare regions. Relative intensities of GFAP and CoL1A1 in the regions of interest (white boxes) were plotted

    Journal: Molecular Brain

    Article Title: Region-specific astrogliosis: differential vessel formation contributes to different patterns of astrogliosis in the cortex and striatum

    doi: 10.1186/s13041-020-00642-0

    Figure Lengend Snippet: Region-specific blood vessel formation and locations of perivascular cells in the injured brain. a Sections obtained from the intact and ATP-injected cortex and striatum at the indicated times were immunostained for CD31 to label blood vessels. Arrowheads, vessels located along the meninges in the intact cortex; arrows, vessels in the parenchyma in intact and injured brains. b Colocalization of CD31 and Col1a1. Sections from intact and ATP-injected brains were double-labeled with antibodies for CD31 and Col1a1 (perivascular fibroblasts), and visualized using Alexa 488- and 594-conjugated secondary antibodies. CD31 and Col1a1 were colocalized in the intact and injured cortex and striatum (arrows). Dotted lines, edges of the damage areas. c Sections were double-labeled with antibodies for GFAP and CoL1A1. Arrows, astrocytes near blood vessels and/or in vessel-rich regions; arrowheads, astrocytes in vessel-rare regions. Relative intensities of GFAP and CoL1A1 in the regions of interest (white boxes) were plotted

    Article Snippet: After blocking with 5% skim milk (Seoul Dairy Coop, Seoul, Korea), the nitrocellulose membrane was sequentially incubated with primary antibodies (Table ), peroxidase-conjugated secondary antibodies (Koma Biotech, Seoul, Korea), and enhanced chemiluminescence reagents (Daeil Lab Services, Seoul, Korea).

    Techniques: Injection, Labeling

    Agonist-induced DOP receptor phosphorylation and internalization. ( A,B top) Stably HA-tagged hDOP receptor-expressing HEK293 cells were preincubated with anti-HA antibody, followed by stimulation with 10 µM DPDPE, DADLE, SNC80, ADL5859, AR-M1000390, deltorphin I, deltorphin II, [Met]-enkephalin, [Leu]-enkephalin, fentanyl, (−)-methadone, morphine, morphine-6-glucuronide (M6G), buprenorphine (BUP), norbuprenorphine (norBUP) or vehicle for 30 min at 37 °C. Cells were fixed, permeabilized, immunofluorescently stained, and subsequently examined using confocal microscopy. Images are representative, n = 3. Scale bar, 20 µm. (A,B bottom) HEK293 cells stably expressing HA-hDOP receptor were stimulated with the compounds listed in (A) or vehicle at concentrations ranging from 10 -9 to 10 -5 M for 10 min at 37 °C. Lysates were immunoblotted with antibodies to pT361 or pS363. Blots were stripped and reprobed with the anti-HA antibody. Blots are representative, n = 3-5. (C) Cells described in ( A ) were preincubated with anti-HA antibody and stimulated with vehicle or 10 µM of compounds listed in ( A ) for 30 min at 37 °C. Cells were fixed and labeled with a peroxidase-conjugated secondary antibody. Receptor internalization was measured by ELISA and quantified as the percentage of internalized receptors in agonist-treated cells compared to untreated cells. Data are means ± SEM of five independent experiments performed in quadruplicate. Results were analyzed by one-way ANOVA followed by Bonferroni’s post-hoc test (*p

    Journal: Scientific Reports

    Article Title: Agonist-induced phosphorylation bar code and differential post-activation signaling of the delta opioid receptor revealed by phosphosite-specific antibodies

    doi: 10.1038/s41598-020-65589-7

    Figure Lengend Snippet: Agonist-induced DOP receptor phosphorylation and internalization. ( A,B top) Stably HA-tagged hDOP receptor-expressing HEK293 cells were preincubated with anti-HA antibody, followed by stimulation with 10 µM DPDPE, DADLE, SNC80, ADL5859, AR-M1000390, deltorphin I, deltorphin II, [Met]-enkephalin, [Leu]-enkephalin, fentanyl, (−)-methadone, morphine, morphine-6-glucuronide (M6G), buprenorphine (BUP), norbuprenorphine (norBUP) or vehicle for 30 min at 37 °C. Cells were fixed, permeabilized, immunofluorescently stained, and subsequently examined using confocal microscopy. Images are representative, n = 3. Scale bar, 20 µm. (A,B bottom) HEK293 cells stably expressing HA-hDOP receptor were stimulated with the compounds listed in (A) or vehicle at concentrations ranging from 10 -9 to 10 -5 M for 10 min at 37 °C. Lysates were immunoblotted with antibodies to pT361 or pS363. Blots were stripped and reprobed with the anti-HA antibody. Blots are representative, n = 3-5. (C) Cells described in ( A ) were preincubated with anti-HA antibody and stimulated with vehicle or 10 µM of compounds listed in ( A ) for 30 min at 37 °C. Cells were fixed and labeled with a peroxidase-conjugated secondary antibody. Receptor internalization was measured by ELISA and quantified as the percentage of internalized receptors in agonist-treated cells compared to untreated cells. Data are means ± SEM of five independent experiments performed in quadruplicate. Results were analyzed by one-way ANOVA followed by Bonferroni’s post-hoc test (*p

    Article Snippet: Cells were washed several times with PBS and incubated with a peroxidase-conjugated secondary antibody (Santa Cruz; Heidelberg, Germany).

    Techniques: Stable Transfection, Expressing, Staining, Confocal Microscopy, Labeling, Enzyme-linked Immunosorbent Assay

    Time course of DPDPE-induced DOP receptor phosphorylation, concentration-dependent DOP receptor phosphorylation and internalization. ( A ) HEK293 cells stably expressing HA-tagged hDOP receptor were preincubated with anti-HA antibody and stimulated with the indicated DPDPE concentrations for 30 min at 37 °C. After stimulation, cells were fixed, permeabilized, immunofluorescently stained and examined using confocal microscopy. Images are representative from one of three independent experiments. Scale bar, 20 µm. (B) Cells described in (A) were preincubated with anti-HA antibody and stimulated with the indicated DPDPE concentrations for 30 min at 37 °C. After fixation, cells were labeled with a peroxidase-conjugated secondary antibody and receptor internalization was measured by enzyme-linked immunosorbent assay. Receptor internalization was measured by ELISA and quantified as the percentage of internalized receptors compared to untreated cells. Data are means ± SEM of four independent experiments performed in quadruplicate. (C,D) Cells described in ( A ) were exposed to 1 µM DPDPE for the indicated times and temperatures ( C ) at 37 °C, ( D ) at 22 °C (room temperature, RT) and lysates were immunoblotted with anti-pT361 or anti-pS363 antibodies. Blots are representative of n = 4 ( C ) or n = 5 ( D ) independent experiments. (E) Cells described in (A) were preincubated with anti-HA antibody and thereafter stimulated with 1 µM DPDPE for the indicated durations at 37 °C. Cells were fixed, permeabilized, immunofluorescently stained and examined using confocal microscopy. Images are representative from one of three independent experiments. Scale bar, 20 µm. (F) Cells described in ( A ) were preincubated with anti-HA antibody and stimulated with 10 µM DPDPE for the indicated durations at 37 °C. Cells were fixed and labeled with peroxidase-conjugated secondary antibody. Receptor internalization was measured by ELISA and quantified as the percentage of internalized receptors in agonist-treated cells compared to untreated cells. Data are mean ± SEM of five independent experiments performed in quadruplicate.

    Journal: Scientific Reports

    Article Title: Agonist-induced phosphorylation bar code and differential post-activation signaling of the delta opioid receptor revealed by phosphosite-specific antibodies

    doi: 10.1038/s41598-020-65589-7

    Figure Lengend Snippet: Time course of DPDPE-induced DOP receptor phosphorylation, concentration-dependent DOP receptor phosphorylation and internalization. ( A ) HEK293 cells stably expressing HA-tagged hDOP receptor were preincubated with anti-HA antibody and stimulated with the indicated DPDPE concentrations for 30 min at 37 °C. After stimulation, cells were fixed, permeabilized, immunofluorescently stained and examined using confocal microscopy. Images are representative from one of three independent experiments. Scale bar, 20 µm. (B) Cells described in (A) were preincubated with anti-HA antibody and stimulated with the indicated DPDPE concentrations for 30 min at 37 °C. After fixation, cells were labeled with a peroxidase-conjugated secondary antibody and receptor internalization was measured by enzyme-linked immunosorbent assay. Receptor internalization was measured by ELISA and quantified as the percentage of internalized receptors compared to untreated cells. Data are means ± SEM of four independent experiments performed in quadruplicate. (C,D) Cells described in ( A ) were exposed to 1 µM DPDPE for the indicated times and temperatures ( C ) at 37 °C, ( D ) at 22 °C (room temperature, RT) and lysates were immunoblotted with anti-pT361 or anti-pS363 antibodies. Blots are representative of n = 4 ( C ) or n = 5 ( D ) independent experiments. (E) Cells described in (A) were preincubated with anti-HA antibody and thereafter stimulated with 1 µM DPDPE for the indicated durations at 37 °C. Cells were fixed, permeabilized, immunofluorescently stained and examined using confocal microscopy. Images are representative from one of three independent experiments. Scale bar, 20 µm. (F) Cells described in ( A ) were preincubated with anti-HA antibody and stimulated with 10 µM DPDPE for the indicated durations at 37 °C. Cells were fixed and labeled with peroxidase-conjugated secondary antibody. Receptor internalization was measured by ELISA and quantified as the percentage of internalized receptors in agonist-treated cells compared to untreated cells. Data are mean ± SEM of five independent experiments performed in quadruplicate.

    Article Snippet: Cells were washed several times with PBS and incubated with a peroxidase-conjugated secondary antibody (Santa Cruz; Heidelberg, Germany).

    Techniques: Concentration Assay, Stable Transfection, Expressing, Staining, Confocal Microscopy, Labeling, Enzyme-linked Immunosorbent Assay

    Characterization of phosphosite-specific DOP receptor antibodies using λ-phosphatase and receptor mutants. ( A ) Schematic representation of the human DOP receptor (hDOP). Potential intracellular phosphorylation sites are depicted in gray. T361 was targeted for the generation of the phosphosite-specific anti-pT361 antibody and anti-pS363 antibody was acquired commercially. (B) Characterization of phosphosite-specific antibodies directed against T361 and S363 using λ-phosphatase. Stably HA-tagged hDOP-receptor expressing HEK293 cells were either not treated (−) or treated (+) with 10 µM DADLE for 10 min. Lysates were then either not incubated (−) or incubated (+) with λ-phosphatase and immunoblotted with the phosphosite-specific antibodies anti-pT361 {5038} or anti-pS363. Blots were stripped and reprobed with the anti-HA antibody {2238} as a loading control. Blots are representative, n = 3. Molecular mass markers (kDA) are indicated, left. (C) Sequence of the carboxyl-terminal tail of hDOP receptor showing all potential phosphorylation sites. Serine (S) and threonine (T) residues indicated were exchanged to alanine. (D) HEK293 cells stably expressing HA-hDOP receptor, T361A/S363A or 7 S/TA were not treated (−) or treated (+) with 1 µM DPDPE for 10 min and lysates were immunoblotted with the antibodies to pT361 or pS363. Blots were stripped and reprobed with the anti-HA antibody. Blots are representative, n = 5. (E) Cells described in (D) were preincubated with antibody to HA-tag and subsequently exposed to 10 µM DPDPE or vehicle for 30 min at 37 °C. Cells were fixed, permeabilized, immunofluorescently stained and examined using confocal microscopy. Images are representative from one of three independent experiments. Scale bar, 20 µm. (F) Receptor internalization was quantified by ELISA. Cells described in (D) were preincubated with antibody to HA-tag and stimulated with 10 µM DPDPE or vehicle at 37 °C for 30 min. Cells were fixed and labeled with a peroxidase-conjugated secondary antibody. Receptor internalization was measured by enzyme-linked immunosorbent assay and quantified as the percentage of internalized receptors in DPDPE-treated cells. Data are mean ± SEM of five independent experiments performed in quadruplicate. Results were analyzed by one-way ANOVA followed by Bonferroni’s post-hoc test (*p

    Journal: Scientific Reports

    Article Title: Agonist-induced phosphorylation bar code and differential post-activation signaling of the delta opioid receptor revealed by phosphosite-specific antibodies

    doi: 10.1038/s41598-020-65589-7

    Figure Lengend Snippet: Characterization of phosphosite-specific DOP receptor antibodies using λ-phosphatase and receptor mutants. ( A ) Schematic representation of the human DOP receptor (hDOP). Potential intracellular phosphorylation sites are depicted in gray. T361 was targeted for the generation of the phosphosite-specific anti-pT361 antibody and anti-pS363 antibody was acquired commercially. (B) Characterization of phosphosite-specific antibodies directed against T361 and S363 using λ-phosphatase. Stably HA-tagged hDOP-receptor expressing HEK293 cells were either not treated (−) or treated (+) with 10 µM DADLE for 10 min. Lysates were then either not incubated (−) or incubated (+) with λ-phosphatase and immunoblotted with the phosphosite-specific antibodies anti-pT361 {5038} or anti-pS363. Blots were stripped and reprobed with the anti-HA antibody {2238} as a loading control. Blots are representative, n = 3. Molecular mass markers (kDA) are indicated, left. (C) Sequence of the carboxyl-terminal tail of hDOP receptor showing all potential phosphorylation sites. Serine (S) and threonine (T) residues indicated were exchanged to alanine. (D) HEK293 cells stably expressing HA-hDOP receptor, T361A/S363A or 7 S/TA were not treated (−) or treated (+) with 1 µM DPDPE for 10 min and lysates were immunoblotted with the antibodies to pT361 or pS363. Blots were stripped and reprobed with the anti-HA antibody. Blots are representative, n = 5. (E) Cells described in (D) were preincubated with antibody to HA-tag and subsequently exposed to 10 µM DPDPE or vehicle for 30 min at 37 °C. Cells were fixed, permeabilized, immunofluorescently stained and examined using confocal microscopy. Images are representative from one of three independent experiments. Scale bar, 20 µm. (F) Receptor internalization was quantified by ELISA. Cells described in (D) were preincubated with antibody to HA-tag and stimulated with 10 µM DPDPE or vehicle at 37 °C for 30 min. Cells were fixed and labeled with a peroxidase-conjugated secondary antibody. Receptor internalization was measured by enzyme-linked immunosorbent assay and quantified as the percentage of internalized receptors in DPDPE-treated cells. Data are mean ± SEM of five independent experiments performed in quadruplicate. Results were analyzed by one-way ANOVA followed by Bonferroni’s post-hoc test (*p

    Article Snippet: Cells were washed several times with PBS and incubated with a peroxidase-conjugated secondary antibody (Santa Cruz; Heidelberg, Germany).

    Techniques: Stable Transfection, Expressing, Incubation, Sequencing, Staining, Confocal Microscopy, Enzyme-linked Immunosorbent Assay, Labeling

    Antagonist-selective inhibition of DPDPE-induced DOP receptor phosphorylation, internalization and G protein signaling. ( A ) Stably HA-hDOP receptor-expressing HEK293 cells were either not preincubated (−) or preincubated (+) with 5 µM naloxone, naltrindole, naltriben or naltrexone for 30 min at 37 °C, then stimulated with vehicle (water, -) or with 1 µM DPDPE (+) for 10 min at 37 °C. Cell lysates were then immunoblotted with antibodies to pT361 or pS363. Blots were stripped and reprobed with the anti-HA antibody. Blots are representative, n = 4. (B) Cells described in ( A ) were preincubated with anti-HA antibody and then treated with vehicle (DMSO), 5 µM naloxone, naltrindole or naltriben and with or without 1 µM DPDPE for 10 min at 37 °C. After fixation, cells were permeabilized, immunofluorescently stained and examined using confocal microscopy. Images are representative, n = 3. Scale bar, 20 µm. (C) Cells described in ( A ) were preincubated with anti-HA antibody and stimulated with vehicle (DMSO), 5 µM naloxone, naltrindole or naltriben and with or without 1 µM DPDPE for 10 min at 37 °C. Cells were then fixed and labeled with a peroxidase-conjugated secondary antibody. Receptor internalization was measured by ELISA and quantified as percentage of internalized receptors in agonist-treated cells. Data are means ± SEM from five independent experiments performed in quadruplicate. *p

    Journal: Scientific Reports

    Article Title: Agonist-induced phosphorylation bar code and differential post-activation signaling of the delta opioid receptor revealed by phosphosite-specific antibodies

    doi: 10.1038/s41598-020-65589-7

    Figure Lengend Snippet: Antagonist-selective inhibition of DPDPE-induced DOP receptor phosphorylation, internalization and G protein signaling. ( A ) Stably HA-hDOP receptor-expressing HEK293 cells were either not preincubated (−) or preincubated (+) with 5 µM naloxone, naltrindole, naltriben or naltrexone for 30 min at 37 °C, then stimulated with vehicle (water, -) or with 1 µM DPDPE (+) for 10 min at 37 °C. Cell lysates were then immunoblotted with antibodies to pT361 or pS363. Blots were stripped and reprobed with the anti-HA antibody. Blots are representative, n = 4. (B) Cells described in ( A ) were preincubated with anti-HA antibody and then treated with vehicle (DMSO), 5 µM naloxone, naltrindole or naltriben and with or without 1 µM DPDPE for 10 min at 37 °C. After fixation, cells were permeabilized, immunofluorescently stained and examined using confocal microscopy. Images are representative, n = 3. Scale bar, 20 µm. (C) Cells described in ( A ) were preincubated with anti-HA antibody and stimulated with vehicle (DMSO), 5 µM naloxone, naltrindole or naltriben and with or without 1 µM DPDPE for 10 min at 37 °C. Cells were then fixed and labeled with a peroxidase-conjugated secondary antibody. Receptor internalization was measured by ELISA and quantified as percentage of internalized receptors in agonist-treated cells. Data are means ± SEM from five independent experiments performed in quadruplicate. *p

    Article Snippet: Cells were washed several times with PBS and incubated with a peroxidase-conjugated secondary antibody (Santa Cruz; Heidelberg, Germany).

    Techniques: Inhibition, Stable Transfection, Expressing, Staining, Confocal Microscopy, Labeling, Enzyme-linked Immunosorbent Assay