polyclonal anti-human crp antibody Search Results


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  • 85
    Millipore polyclonal goat anti human crp antibody
    Infection-inflammation triggers <t>CRP</t> and L-ficolin to form complex in serum. The complex of CRP and L-ficolin was co-immunoprecipitated from the patient serum (A) or healthy serum (B) at pH 6.5 and 7.4 with or without calcium. Rabbit <t>polyclonal</t> anti-CRP was added (lanes marked with “+”) to 500 µl of 10% pre-cleared serum and incubated for 1 h at 4°C, following which protein A beads were added. As the negative controls (lanes marked with“−”), the Co-IP used rabbit polyclonal anti-CrCRP (horseshoe crab, Carcinoscorpius rotundicauda CRP antibody) instead of rabbit polyclonal anti-CRP. The immuno-precipitates (P) on the beads and the proteins in the supernatants (S) were extracted in SDS PAGE loading buffer, and the bound CRP and L-/H-ficolins were identified by mouse monoclonal anti-CRP and anti-L-/H-ficolin antibodies, respectively. In (A) and (B), Lane 1: purified CRP and L-/H-ficolins were loaded for confirmation of the specificity of immunodetection; Lanes 2–5: proteins in precipitates or supernatants under pH 6.5 without calcium; Lanes 6–9: proteins in precipitates or supernatants under pH 6.5 with 2 mM calcium. Lanes 10–13: proteins in precipitates or supernatants under pH 7.4 without calcium; Lanes 14–17: proteins in precipitates or supernatants under pH 7.4 with 2.5 mM calcium. In (B), Lanes 18–21 contained proteins in precipitates or supernatants under pH 7.4, 2.5 mM calcium with addition of 10 µg/ml CRP. (C) ELISA to test the interaction between CRP and L-/H-/M-ficolins when 0.8 µg of CRP was immobilized first. 0, 0.5, 0.8 and 1 µg of L-/H-/M-ficolins were added to the immobilized CRP, respectively, and the bound proteins were detected by the corresponding antibodies. (D) ELISA to compare the interaction between CRP and L-/M-ficolins in different orders of immobilization with 0.8 µg of either of the ficolins or CRP immobilized first. In (C) and (D), 0.8 µg HSA (instead of CRP or ficolins) was immobilized on the wells to serve as the negative control. The positive control (for 100% binding) constituted 1 µg of the binding proteins [ficolins in (C) and ficolins or CRP in (D)] directly immobilized on the wells and detected by the corresponding antibodies. OD 405 nm was read as the binding signal. Readings were subtracted off negative controls and expressed as a percentage of the corresponding 100% binding control.
    Polyclonal Goat Anti Human Crp Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 85/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/polyclonal goat anti human crp antibody/product/Millipore
    Average 85 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    polyclonal goat anti human crp antibody - by Bioz Stars, 2020-08
    85/100 stars
      Buy from Supplier

    85
    Agilent technologies polyclonal anti human crp antibodies
    Infection-inflammation triggers <t>CRP</t> and L-ficolin to form complex in serum. The complex of CRP and L-ficolin was co-immunoprecipitated from the patient serum (A) or healthy serum (B) at pH 6.5 and 7.4 with or without calcium. Rabbit <t>polyclonal</t> anti-CRP was added (lanes marked with “+”) to 500 µl of 10% pre-cleared serum and incubated for 1 h at 4°C, following which protein A beads were added. As the negative controls (lanes marked with“−”), the Co-IP used rabbit polyclonal anti-CrCRP (horseshoe crab, Carcinoscorpius rotundicauda CRP antibody) instead of rabbit polyclonal anti-CRP. The immuno-precipitates (P) on the beads and the proteins in the supernatants (S) were extracted in SDS PAGE loading buffer, and the bound CRP and L-/H-ficolins were identified by mouse monoclonal anti-CRP and anti-L-/H-ficolin antibodies, respectively. In (A) and (B), Lane 1: purified CRP and L-/H-ficolins were loaded for confirmation of the specificity of immunodetection; Lanes 2–5: proteins in precipitates or supernatants under pH 6.5 without calcium; Lanes 6–9: proteins in precipitates or supernatants under pH 6.5 with 2 mM calcium. Lanes 10–13: proteins in precipitates or supernatants under pH 7.4 without calcium; Lanes 14–17: proteins in precipitates or supernatants under pH 7.4 with 2.5 mM calcium. In (B), Lanes 18–21 contained proteins in precipitates or supernatants under pH 7.4, 2.5 mM calcium with addition of 10 µg/ml CRP. (C) ELISA to test the interaction between CRP and L-/H-/M-ficolins when 0.8 µg of CRP was immobilized first. 0, 0.5, 0.8 and 1 µg of L-/H-/M-ficolins were added to the immobilized CRP, respectively, and the bound proteins were detected by the corresponding antibodies. (D) ELISA to compare the interaction between CRP and L-/M-ficolins in different orders of immobilization with 0.8 µg of either of the ficolins or CRP immobilized first. In (C) and (D), 0.8 µg HSA (instead of CRP or ficolins) was immobilized on the wells to serve as the negative control. The positive control (for 100% binding) constituted 1 µg of the binding proteins [ficolins in (C) and ficolins or CRP in (D)] directly immobilized on the wells and detected by the corresponding antibodies. OD 405 nm was read as the binding signal. Readings were subtracted off negative controls and expressed as a percentage of the corresponding 100% binding control.
    Polyclonal Anti Human Crp Antibodies, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 85/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/polyclonal anti human crp antibodies/product/Agilent technologies
    Average 85 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    polyclonal anti human crp antibodies - by Bioz Stars, 2020-08
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    90
    Santa Cruz Biotechnology polyclonal anti human crp antibody
    Infection-inflammation triggers <t>CRP</t> and L-ficolin to form complex in serum. The complex of CRP and L-ficolin was co-immunoprecipitated from the patient serum (A) or healthy serum (B) at pH 6.5 and 7.4 with or without calcium. Rabbit <t>polyclonal</t> anti-CRP was added (lanes marked with “+”) to 500 µl of 10% pre-cleared serum and incubated for 1 h at 4°C, following which protein A beads were added. As the negative controls (lanes marked with“−”), the Co-IP used rabbit polyclonal anti-CrCRP (horseshoe crab, Carcinoscorpius rotundicauda CRP antibody) instead of rabbit polyclonal anti-CRP. The immuno-precipitates (P) on the beads and the proteins in the supernatants (S) were extracted in SDS PAGE loading buffer, and the bound CRP and L-/H-ficolins were identified by mouse monoclonal anti-CRP and anti-L-/H-ficolin antibodies, respectively. In (A) and (B), Lane 1: purified CRP and L-/H-ficolins were loaded for confirmation of the specificity of immunodetection; Lanes 2–5: proteins in precipitates or supernatants under pH 6.5 without calcium; Lanes 6–9: proteins in precipitates or supernatants under pH 6.5 with 2 mM calcium. Lanes 10–13: proteins in precipitates or supernatants under pH 7.4 without calcium; Lanes 14–17: proteins in precipitates or supernatants under pH 7.4 with 2.5 mM calcium. In (B), Lanes 18–21 contained proteins in precipitates or supernatants under pH 7.4, 2.5 mM calcium with addition of 10 µg/ml CRP. (C) ELISA to test the interaction between CRP and L-/H-/M-ficolins when 0.8 µg of CRP was immobilized first. 0, 0.5, 0.8 and 1 µg of L-/H-/M-ficolins were added to the immobilized CRP, respectively, and the bound proteins were detected by the corresponding antibodies. (D) ELISA to compare the interaction between CRP and L-/M-ficolins in different orders of immobilization with 0.8 µg of either of the ficolins or CRP immobilized first. In (C) and (D), 0.8 µg HSA (instead of CRP or ficolins) was immobilized on the wells to serve as the negative control. The positive control (for 100% binding) constituted 1 µg of the binding proteins [ficolins in (C) and ficolins or CRP in (D)] directly immobilized on the wells and detected by the corresponding antibodies. OD 405 nm was read as the binding signal. Readings were subtracted off negative controls and expressed as a percentage of the corresponding 100% binding control.
    Polyclonal Anti Human Crp Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 90/100, based on 48 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/polyclonal anti human crp antibody/product/Santa Cruz Biotechnology
    Average 90 stars, based on 48 article reviews
    Price from $9.99 to $1999.99
    polyclonal anti human crp antibody - by Bioz Stars, 2020-08
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    85
    Agilent technologies polyclonal rat anti human crp antibodies
    Infection-inflammation triggers <t>CRP</t> and L-ficolin to form complex in serum. The complex of CRP and L-ficolin was co-immunoprecipitated from the patient serum (A) or healthy serum (B) at pH 6.5 and 7.4 with or without calcium. Rabbit <t>polyclonal</t> anti-CRP was added (lanes marked with “+”) to 500 µl of 10% pre-cleared serum and incubated for 1 h at 4°C, following which protein A beads were added. As the negative controls (lanes marked with“−”), the Co-IP used rabbit polyclonal anti-CrCRP (horseshoe crab, Carcinoscorpius rotundicauda CRP antibody) instead of rabbit polyclonal anti-CRP. The immuno-precipitates (P) on the beads and the proteins in the supernatants (S) were extracted in SDS PAGE loading buffer, and the bound CRP and L-/H-ficolins were identified by mouse monoclonal anti-CRP and anti-L-/H-ficolin antibodies, respectively. In (A) and (B), Lane 1: purified CRP and L-/H-ficolins were loaded for confirmation of the specificity of immunodetection; Lanes 2–5: proteins in precipitates or supernatants under pH 6.5 without calcium; Lanes 6–9: proteins in precipitates or supernatants under pH 6.5 with 2 mM calcium. Lanes 10–13: proteins in precipitates or supernatants under pH 7.4 without calcium; Lanes 14–17: proteins in precipitates or supernatants under pH 7.4 with 2.5 mM calcium. In (B), Lanes 18–21 contained proteins in precipitates or supernatants under pH 7.4, 2.5 mM calcium with addition of 10 µg/ml CRP. (C) ELISA to test the interaction between CRP and L-/H-/M-ficolins when 0.8 µg of CRP was immobilized first. 0, 0.5, 0.8 and 1 µg of L-/H-/M-ficolins were added to the immobilized CRP, respectively, and the bound proteins were detected by the corresponding antibodies. (D) ELISA to compare the interaction between CRP and L-/M-ficolins in different orders of immobilization with 0.8 µg of either of the ficolins or CRP immobilized first. In (C) and (D), 0.8 µg HSA (instead of CRP or ficolins) was immobilized on the wells to serve as the negative control. The positive control (for 100% binding) constituted 1 µg of the binding proteins [ficolins in (C) and ficolins or CRP in (D)] directly immobilized on the wells and detected by the corresponding antibodies. OD 405 nm was read as the binding signal. Readings were subtracted off negative controls and expressed as a percentage of the corresponding 100% binding control.
    Polyclonal Rat Anti Human Crp Antibodies, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 85/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/polyclonal rat anti human crp antibodies/product/Agilent technologies
    Average 85 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    polyclonal rat anti human crp antibodies - by Bioz Stars, 2020-08
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    92
    Millipore polyclonal rabbit anti human crp antibody
    Infection-inflammation triggers <t>CRP</t> and L-ficolin to form complex in serum. The complex of CRP and L-ficolin was co-immunoprecipitated from the patient serum (A) or healthy serum (B) at pH 6.5 and 7.4 with or without calcium. Rabbit <t>polyclonal</t> anti-CRP was added (lanes marked with “+”) to 500 µl of 10% pre-cleared serum and incubated for 1 h at 4°C, following which protein A beads were added. As the negative controls (lanes marked with“−”), the Co-IP used rabbit polyclonal anti-CrCRP (horseshoe crab, Carcinoscorpius rotundicauda CRP antibody) instead of rabbit polyclonal anti-CRP. The immuno-precipitates (P) on the beads and the proteins in the supernatants (S) were extracted in SDS PAGE loading buffer, and the bound CRP and L-/H-ficolins were identified by mouse monoclonal anti-CRP and anti-L-/H-ficolin antibodies, respectively. In (A) and (B), Lane 1: purified CRP and L-/H-ficolins were loaded for confirmation of the specificity of immunodetection; Lanes 2–5: proteins in precipitates or supernatants under pH 6.5 without calcium; Lanes 6–9: proteins in precipitates or supernatants under pH 6.5 with 2 mM calcium. Lanes 10–13: proteins in precipitates or supernatants under pH 7.4 without calcium; Lanes 14–17: proteins in precipitates or supernatants under pH 7.4 with 2.5 mM calcium. In (B), Lanes 18–21 contained proteins in precipitates or supernatants under pH 7.4, 2.5 mM calcium with addition of 10 µg/ml CRP. (C) ELISA to test the interaction between CRP and L-/H-/M-ficolins when 0.8 µg of CRP was immobilized first. 0, 0.5, 0.8 and 1 µg of L-/H-/M-ficolins were added to the immobilized CRP, respectively, and the bound proteins were detected by the corresponding antibodies. (D) ELISA to compare the interaction between CRP and L-/M-ficolins in different orders of immobilization with 0.8 µg of either of the ficolins or CRP immobilized first. In (C) and (D), 0.8 µg HSA (instead of CRP or ficolins) was immobilized on the wells to serve as the negative control. The positive control (for 100% binding) constituted 1 µg of the binding proteins [ficolins in (C) and ficolins or CRP in (D)] directly immobilized on the wells and detected by the corresponding antibodies. OD 405 nm was read as the binding signal. Readings were subtracted off negative controls and expressed as a percentage of the corresponding 100% binding control.
    Polyclonal Rabbit Anti Human Crp Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 43 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/polyclonal rabbit anti human crp antibody/product/Millipore
    Average 92 stars, based on 43 article reviews
    Price from $9.99 to $1999.99
    polyclonal rabbit anti human crp antibody - by Bioz Stars, 2020-08
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    90
    denka seiken polyclonal rabbit anti human crp antibodies
    Infection-inflammation triggers <t>CRP</t> and L-ficolin to form complex in serum. The complex of CRP and L-ficolin was co-immunoprecipitated from the patient serum (A) or healthy serum (B) at pH 6.5 and 7.4 with or without calcium. Rabbit <t>polyclonal</t> anti-CRP was added (lanes marked with “+”) to 500 µl of 10% pre-cleared serum and incubated for 1 h at 4°C, following which protein A beads were added. As the negative controls (lanes marked with“−”), the Co-IP used rabbit polyclonal anti-CrCRP (horseshoe crab, Carcinoscorpius rotundicauda CRP antibody) instead of rabbit polyclonal anti-CRP. The immuno-precipitates (P) on the beads and the proteins in the supernatants (S) were extracted in SDS PAGE loading buffer, and the bound CRP and L-/H-ficolins were identified by mouse monoclonal anti-CRP and anti-L-/H-ficolin antibodies, respectively. In (A) and (B), Lane 1: purified CRP and L-/H-ficolins were loaded for confirmation of the specificity of immunodetection; Lanes 2–5: proteins in precipitates or supernatants under pH 6.5 without calcium; Lanes 6–9: proteins in precipitates or supernatants under pH 6.5 with 2 mM calcium. Lanes 10–13: proteins in precipitates or supernatants under pH 7.4 without calcium; Lanes 14–17: proteins in precipitates or supernatants under pH 7.4 with 2.5 mM calcium. In (B), Lanes 18–21 contained proteins in precipitates or supernatants under pH 7.4, 2.5 mM calcium with addition of 10 µg/ml CRP. (C) ELISA to test the interaction between CRP and L-/H-/M-ficolins when 0.8 µg of CRP was immobilized first. 0, 0.5, 0.8 and 1 µg of L-/H-/M-ficolins were added to the immobilized CRP, respectively, and the bound proteins were detected by the corresponding antibodies. (D) ELISA to compare the interaction between CRP and L-/M-ficolins in different orders of immobilization with 0.8 µg of either of the ficolins or CRP immobilized first. In (C) and (D), 0.8 µg HSA (instead of CRP or ficolins) was immobilized on the wells to serve as the negative control. The positive control (for 100% binding) constituted 1 µg of the binding proteins [ficolins in (C) and ficolins or CRP in (D)] directly immobilized on the wells and detected by the corresponding antibodies. OD 405 nm was read as the binding signal. Readings were subtracted off negative controls and expressed as a percentage of the corresponding 100% binding control.
    Polyclonal Rabbit Anti Human Crp Antibodies, supplied by denka seiken, used in various techniques. Bioz Stars score: 90/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 90 stars, based on 2 article reviews
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    polyclonal rabbit anti human crp antibodies - by Bioz Stars, 2020-08
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    91
    Calbioreagents goat polyclonal anti human crp antibodies
    Infection-inflammation triggers <t>CRP</t> and L-ficolin to form complex in serum. The complex of CRP and L-ficolin was co-immunoprecipitated from the patient serum (A) or healthy serum (B) at pH 6.5 and 7.4 with or without calcium. Rabbit <t>polyclonal</t> anti-CRP was added (lanes marked with “+”) to 500 µl of 10% pre-cleared serum and incubated for 1 h at 4°C, following which protein A beads were added. As the negative controls (lanes marked with“−”), the Co-IP used rabbit polyclonal anti-CrCRP (horseshoe crab, Carcinoscorpius rotundicauda CRP antibody) instead of rabbit polyclonal anti-CRP. The immuno-precipitates (P) on the beads and the proteins in the supernatants (S) were extracted in SDS PAGE loading buffer, and the bound CRP and L-/H-ficolins were identified by mouse monoclonal anti-CRP and anti-L-/H-ficolin antibodies, respectively. In (A) and (B), Lane 1: purified CRP and L-/H-ficolins were loaded for confirmation of the specificity of immunodetection; Lanes 2–5: proteins in precipitates or supernatants under pH 6.5 without calcium; Lanes 6–9: proteins in precipitates or supernatants under pH 6.5 with 2 mM calcium. Lanes 10–13: proteins in precipitates or supernatants under pH 7.4 without calcium; Lanes 14–17: proteins in precipitates or supernatants under pH 7.4 with 2.5 mM calcium. In (B), Lanes 18–21 contained proteins in precipitates or supernatants under pH 7.4, 2.5 mM calcium with addition of 10 µg/ml CRP. (C) ELISA to test the interaction between CRP and L-/H-/M-ficolins when 0.8 µg of CRP was immobilized first. 0, 0.5, 0.8 and 1 µg of L-/H-/M-ficolins were added to the immobilized CRP, respectively, and the bound proteins were detected by the corresponding antibodies. (D) ELISA to compare the interaction between CRP and L-/M-ficolins in different orders of immobilization with 0.8 µg of either of the ficolins or CRP immobilized first. In (C) and (D), 0.8 µg HSA (instead of CRP or ficolins) was immobilized on the wells to serve as the negative control. The positive control (for 100% binding) constituted 1 µg of the binding proteins [ficolins in (C) and ficolins or CRP in (D)] directly immobilized on the wells and detected by the corresponding antibodies. OD 405 nm was read as the binding signal. Readings were subtracted off negative controls and expressed as a percentage of the corresponding 100% binding control.
    Goat Polyclonal Anti Human Crp Antibodies, supplied by Calbioreagents, used in various techniques. Bioz Stars score: 91/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/goat polyclonal anti human crp antibodies/product/Calbioreagents
    Average 91 stars, based on 5 article reviews
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    goat polyclonal anti human crp antibodies - by Bioz Stars, 2020-08
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    88
    Trinity Biotech rabbit anti human crp polyclonal antibody
    Infection-inflammation triggers <t>CRP</t> and L-ficolin to form complex in serum. The complex of CRP and L-ficolin was co-immunoprecipitated from the patient serum (A) or healthy serum (B) at pH 6.5 and 7.4 with or without calcium. Rabbit <t>polyclonal</t> anti-CRP was added (lanes marked with “+”) to 500 µl of 10% pre-cleared serum and incubated for 1 h at 4°C, following which protein A beads were added. As the negative controls (lanes marked with“−”), the Co-IP used rabbit polyclonal anti-CrCRP (horseshoe crab, Carcinoscorpius rotundicauda CRP antibody) instead of rabbit polyclonal anti-CRP. The immuno-precipitates (P) on the beads and the proteins in the supernatants (S) were extracted in SDS PAGE loading buffer, and the bound CRP and L-/H-ficolins were identified by mouse monoclonal anti-CRP and anti-L-/H-ficolin antibodies, respectively. In (A) and (B), Lane 1: purified CRP and L-/H-ficolins were loaded for confirmation of the specificity of immunodetection; Lanes 2–5: proteins in precipitates or supernatants under pH 6.5 without calcium; Lanes 6–9: proteins in precipitates or supernatants under pH 6.5 with 2 mM calcium. Lanes 10–13: proteins in precipitates or supernatants under pH 7.4 without calcium; Lanes 14–17: proteins in precipitates or supernatants under pH 7.4 with 2.5 mM calcium. In (B), Lanes 18–21 contained proteins in precipitates or supernatants under pH 7.4, 2.5 mM calcium with addition of 10 µg/ml CRP. (C) ELISA to test the interaction between CRP and L-/H-/M-ficolins when 0.8 µg of CRP was immobilized first. 0, 0.5, 0.8 and 1 µg of L-/H-/M-ficolins were added to the immobilized CRP, respectively, and the bound proteins were detected by the corresponding antibodies. (D) ELISA to compare the interaction between CRP and L-/M-ficolins in different orders of immobilization with 0.8 µg of either of the ficolins or CRP immobilized first. In (C) and (D), 0.8 µg HSA (instead of CRP or ficolins) was immobilized on the wells to serve as the negative control. The positive control (for 100% binding) constituted 1 µg of the binding proteins [ficolins in (C) and ficolins or CRP in (D)] directly immobilized on the wells and detected by the corresponding antibodies. OD 405 nm was read as the binding signal. Readings were subtracted off negative controls and expressed as a percentage of the corresponding 100% binding control.
    Rabbit Anti Human Crp Polyclonal Antibody, supplied by Trinity Biotech, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti human crp polyclonal antibody/product/Trinity Biotech
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    rabbit anti human crp polyclonal antibody - by Bioz Stars, 2020-08
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    94
    Millipore immunoaffinity purified polyclonal rabbit anti crp antibody
    Binding of <t>CRP</t> to six different immobilized proteins as a function of pH and temperature. Results of a protein ligand-binding assay are shown. Microtiter wells were coated with factor H, oxLDL, C3b, IgG, Aβ, and BSA. The unreacted sites in the wells were blocked with gelatin. CRP (10 μg/ml), diluted in TBS-Ca, pH 7.0–4.6, was then added to the wells. One set of wells was incubated at 25 °C and another at 37 °C, for 2 h. Bound CRP was detected by using a rabbit <t>polyclonal</t> anti-CRP antibody and HRP-conjugated donkey anti-rabbit IgG. The absorbance of the developed color was read at 405 nm and plotted on the y axis.
    Immunoaffinity Purified Polyclonal Rabbit Anti Crp Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Agilent technologies polyclonal rabbit antihuman crp antibody
    Binding of <t>CRP</t> to six different immobilized proteins as a function of pH and temperature. Results of a protein ligand-binding assay are shown. Microtiter wells were coated with factor H, oxLDL, C3b, IgG, Aβ, and BSA. The unreacted sites in the wells were blocked with gelatin. CRP (10 μg/ml), diluted in TBS-Ca, pH 7.0–4.6, was then added to the wells. One set of wells was incubated at 25 °C and another at 37 °C, for 2 h. Bound CRP was detected by using a rabbit <t>polyclonal</t> anti-CRP antibody and HRP-conjugated donkey anti-rabbit IgG. The absorbance of the developed color was read at 405 nm and plotted on the y axis.
    Polyclonal Rabbit Antihuman Crp Antibody, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 85/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    polyclonal rabbit antihuman crp antibody - by Bioz Stars, 2020-08
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    85
    Biogenesis Inc sheep antihuman polyclonal crp antibody
    Binding of <t>CRP</t> to six different immobilized proteins as a function of pH and temperature. Results of a protein ligand-binding assay are shown. Microtiter wells were coated with factor H, oxLDL, C3b, IgG, Aβ, and BSA. The unreacted sites in the wells were blocked with gelatin. CRP (10 μg/ml), diluted in TBS-Ca, pH 7.0–4.6, was then added to the wells. One set of wells was incubated at 25 °C and another at 37 °C, for 2 h. Bound CRP was detected by using a rabbit <t>polyclonal</t> anti-CRP antibody and HRP-conjugated donkey anti-rabbit IgG. The absorbance of the developed color was read at 405 nm and plotted on the y axis.
    Sheep Antihuman Polyclonal Crp Antibody, supplied by Biogenesis Inc, used in various techniques. Bioz Stars score: 85/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    sheep antihuman polyclonal crp antibody - by Bioz Stars, 2020-08
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    85
    Thermo Fisher polyclonal goat anti human crp
    Binding of <t>CRP</t> to six different immobilized proteins as a function of pH and temperature. Results of a protein ligand-binding assay are shown. Microtiter wells were coated with factor H, oxLDL, C3b, IgG, Aβ, and BSA. The unreacted sites in the wells were blocked with gelatin. CRP (10 μg/ml), diluted in TBS-Ca, pH 7.0–4.6, was then added to the wells. One set of wells was incubated at 25 °C and another at 37 °C, for 2 h. Bound CRP was detected by using a rabbit <t>polyclonal</t> anti-CRP antibody and HRP-conjugated donkey anti-rabbit IgG. The absorbance of the developed color was read at 405 nm and plotted on the y axis.
    Polyclonal Goat Anti Human Crp, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 85 stars, based on 4 article reviews
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    polyclonal goat anti human crp - by Bioz Stars, 2020-08
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    94
    Acris Antibodies polyclonal goat anti human crp
    Binding of <t>CRP</t> to six different immobilized proteins as a function of pH and temperature. Results of a protein ligand-binding assay are shown. Microtiter wells were coated with factor H, oxLDL, C3b, IgG, Aβ, and BSA. The unreacted sites in the wells were blocked with gelatin. CRP (10 μg/ml), diluted in TBS-Ca, pH 7.0–4.6, was then added to the wells. One set of wells was incubated at 25 °C and another at 37 °C, for 2 h. Bound CRP was detected by using a rabbit <t>polyclonal</t> anti-CRP antibody and HRP-conjugated donkey anti-rabbit IgG. The absorbance of the developed color was read at 405 nm and plotted on the y axis.
    Polyclonal Goat Anti Human Crp, supplied by Acris Antibodies, used in various techniques. Bioz Stars score: 94/100, based on 22 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/polyclonal goat anti human crp/product/Acris Antibodies
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    93
    R&D Systems human lrp 1 cluster ii antibody
    Binding of <t>CRP</t> to six different immobilized proteins as a function of pH and temperature. Results of a protein ligand-binding assay are shown. Microtiter wells were coated with factor H, oxLDL, C3b, IgG, Aβ, and BSA. The unreacted sites in the wells were blocked with gelatin. CRP (10 μg/ml), diluted in TBS-Ca, pH 7.0–4.6, was then added to the wells. One set of wells was incubated at 25 °C and another at 37 °C, for 2 h. Bound CRP was detected by using a rabbit <t>polyclonal</t> anti-CRP antibody and HRP-conjugated donkey anti-rabbit IgG. The absorbance of the developed color was read at 405 nm and plotted on the y axis.
    Human Lrp 1 Cluster Ii Antibody, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Bethyl hrp goat anti human crp
    Binding of <t>CRP</t> to six different immobilized proteins as a function of pH and temperature. Results of a protein ligand-binding assay are shown. Microtiter wells were coated with factor H, oxLDL, C3b, IgG, Aβ, and BSA. The unreacted sites in the wells were blocked with gelatin. CRP (10 μg/ml), diluted in TBS-Ca, pH 7.0–4.6, was then added to the wells. One set of wells was incubated at 25 °C and another at 37 °C, for 2 h. Bound CRP was detected by using a rabbit <t>polyclonal</t> anti-CRP antibody and HRP-conjugated donkey anti-rabbit IgG. The absorbance of the developed color was read at 405 nm and plotted on the y axis.
    Hrp Goat Anti Human Crp, supplied by Bethyl, used in various techniques. Bioz Stars score: 86/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Bethyl fitc labeled goat anti human crp antibody
    Binding of <t>CRP</t> to six different immobilized proteins as a function of pH and temperature. Results of a protein ligand-binding assay are shown. Microtiter wells were coated with factor H, oxLDL, C3b, IgG, Aβ, and BSA. The unreacted sites in the wells were blocked with gelatin. CRP (10 μg/ml), diluted in TBS-Ca, pH 7.0–4.6, was then added to the wells. One set of wells was incubated at 25 °C and another at 37 °C, for 2 h. Bound CRP was detected by using a rabbit <t>polyclonal</t> anti-CRP antibody and HRP-conjugated donkey anti-rabbit IgG. The absorbance of the developed color was read at 405 nm and plotted on the y axis.
    Fitc Labeled Goat Anti Human Crp Antibody, supplied by Bethyl, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore rabbit anti human crp pab
    Binding of <t>CRP</t> to six different immobilized proteins as a function of pH and temperature. Results of a protein ligand-binding assay are shown. Microtiter wells were coated with factor H, oxLDL, C3b, IgG, Aβ, and BSA. The unreacted sites in the wells were blocked with gelatin. CRP (10 μg/ml), diluted in TBS-Ca, pH 7.0–4.6, was then added to the wells. One set of wells was incubated at 25 °C and another at 37 °C, for 2 h. Bound CRP was detected by using a rabbit <t>polyclonal</t> anti-CRP antibody and HRP-conjugated donkey anti-rabbit IgG. The absorbance of the developed color was read at 405 nm and plotted on the y axis.
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    R&D Systems human crp antibody af1707
    Binding of <t>CRP</t> to six different immobilized proteins as a function of pH and temperature. Results of a protein ligand-binding assay are shown. Microtiter wells were coated with factor H, oxLDL, C3b, IgG, Aβ, and BSA. The unreacted sites in the wells were blocked with gelatin. CRP (10 μg/ml), diluted in TBS-Ca, pH 7.0–4.6, was then added to the wells. One set of wells was incubated at 25 °C and another at 37 °C, for 2 h. Bound CRP was detected by using a rabbit <t>polyclonal</t> anti-CRP antibody and HRP-conjugated donkey anti-rabbit IgG. The absorbance of the developed color was read at 405 nm and plotted on the y axis.
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    Cell Signaling Technology Inc anti cleaved caspase 3 antibody
    Binding of <t>CRP</t> to six different immobilized proteins as a function of pH and temperature. Results of a protein ligand-binding assay are shown. Microtiter wells were coated with factor H, oxLDL, C3b, IgG, Aβ, and BSA. The unreacted sites in the wells were blocked with gelatin. CRP (10 μg/ml), diluted in TBS-Ca, pH 7.0–4.6, was then added to the wells. One set of wells was incubated at 25 °C and another at 37 °C, for 2 h. Bound CRP was detected by using a rabbit <t>polyclonal</t> anti-CRP antibody and HRP-conjugated donkey anti-rabbit IgG. The absorbance of the developed color was read at 405 nm and plotted on the y axis.
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    Cambridge Bioscience anti giantin rabbit polyclonal antibody
    Binding of <t>CRP</t> to six different immobilized proteins as a function of pH and temperature. Results of a protein ligand-binding assay are shown. Microtiter wells were coated with factor H, oxLDL, C3b, IgG, Aβ, and BSA. The unreacted sites in the wells were blocked with gelatin. CRP (10 μg/ml), diluted in TBS-Ca, pH 7.0–4.6, was then added to the wells. One set of wells was incubated at 25 °C and another at 37 °C, for 2 h. Bound CRP was detected by using a rabbit <t>polyclonal</t> anti-CRP antibody and HRP-conjugated donkey anti-rabbit IgG. The absorbance of the developed color was read at 405 nm and plotted on the y axis.
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    Image Search Results


    Infection-inflammation triggers CRP and L-ficolin to form complex in serum. The complex of CRP and L-ficolin was co-immunoprecipitated from the patient serum (A) or healthy serum (B) at pH 6.5 and 7.4 with or without calcium. Rabbit polyclonal anti-CRP was added (lanes marked with “+”) to 500 µl of 10% pre-cleared serum and incubated for 1 h at 4°C, following which protein A beads were added. As the negative controls (lanes marked with“−”), the Co-IP used rabbit polyclonal anti-CrCRP (horseshoe crab, Carcinoscorpius rotundicauda CRP antibody) instead of rabbit polyclonal anti-CRP. The immuno-precipitates (P) on the beads and the proteins in the supernatants (S) were extracted in SDS PAGE loading buffer, and the bound CRP and L-/H-ficolins were identified by mouse monoclonal anti-CRP and anti-L-/H-ficolin antibodies, respectively. In (A) and (B), Lane 1: purified CRP and L-/H-ficolins were loaded for confirmation of the specificity of immunodetection; Lanes 2–5: proteins in precipitates or supernatants under pH 6.5 without calcium; Lanes 6–9: proteins in precipitates or supernatants under pH 6.5 with 2 mM calcium. Lanes 10–13: proteins in precipitates or supernatants under pH 7.4 without calcium; Lanes 14–17: proteins in precipitates or supernatants under pH 7.4 with 2.5 mM calcium. In (B), Lanes 18–21 contained proteins in precipitates or supernatants under pH 7.4, 2.5 mM calcium with addition of 10 µg/ml CRP. (C) ELISA to test the interaction between CRP and L-/H-/M-ficolins when 0.8 µg of CRP was immobilized first. 0, 0.5, 0.8 and 1 µg of L-/H-/M-ficolins were added to the immobilized CRP, respectively, and the bound proteins were detected by the corresponding antibodies. (D) ELISA to compare the interaction between CRP and L-/M-ficolins in different orders of immobilization with 0.8 µg of either of the ficolins or CRP immobilized first. In (C) and (D), 0.8 µg HSA (instead of CRP or ficolins) was immobilized on the wells to serve as the negative control. The positive control (for 100% binding) constituted 1 µg of the binding proteins [ficolins in (C) and ficolins or CRP in (D)] directly immobilized on the wells and detected by the corresponding antibodies. OD 405 nm was read as the binding signal. Readings were subtracted off negative controls and expressed as a percentage of the corresponding 100% binding control.

    Journal: PLoS Pathogens

    Article Title: Local Inflammation Induces Complement Crosstalk Which Amplifies the Antimicrobial Response

    doi: 10.1371/journal.ppat.1000282

    Figure Lengend Snippet: Infection-inflammation triggers CRP and L-ficolin to form complex in serum. The complex of CRP and L-ficolin was co-immunoprecipitated from the patient serum (A) or healthy serum (B) at pH 6.5 and 7.4 with or without calcium. Rabbit polyclonal anti-CRP was added (lanes marked with “+”) to 500 µl of 10% pre-cleared serum and incubated for 1 h at 4°C, following which protein A beads were added. As the negative controls (lanes marked with“−”), the Co-IP used rabbit polyclonal anti-CrCRP (horseshoe crab, Carcinoscorpius rotundicauda CRP antibody) instead of rabbit polyclonal anti-CRP. The immuno-precipitates (P) on the beads and the proteins in the supernatants (S) were extracted in SDS PAGE loading buffer, and the bound CRP and L-/H-ficolins were identified by mouse monoclonal anti-CRP and anti-L-/H-ficolin antibodies, respectively. In (A) and (B), Lane 1: purified CRP and L-/H-ficolins were loaded for confirmation of the specificity of immunodetection; Lanes 2–5: proteins in precipitates or supernatants under pH 6.5 without calcium; Lanes 6–9: proteins in precipitates or supernatants under pH 6.5 with 2 mM calcium. Lanes 10–13: proteins in precipitates or supernatants under pH 7.4 without calcium; Lanes 14–17: proteins in precipitates or supernatants under pH 7.4 with 2.5 mM calcium. In (B), Lanes 18–21 contained proteins in precipitates or supernatants under pH 7.4, 2.5 mM calcium with addition of 10 µg/ml CRP. (C) ELISA to test the interaction between CRP and L-/H-/M-ficolins when 0.8 µg of CRP was immobilized first. 0, 0.5, 0.8 and 1 µg of L-/H-/M-ficolins were added to the immobilized CRP, respectively, and the bound proteins were detected by the corresponding antibodies. (D) ELISA to compare the interaction between CRP and L-/M-ficolins in different orders of immobilization with 0.8 µg of either of the ficolins or CRP immobilized first. In (C) and (D), 0.8 µg HSA (instead of CRP or ficolins) was immobilized on the wells to serve as the negative control. The positive control (for 100% binding) constituted 1 µg of the binding proteins [ficolins in (C) and ficolins or CRP in (D)] directly immobilized on the wells and detected by the corresponding antibodies. OD 405 nm was read as the binding signal. Readings were subtracted off negative controls and expressed as a percentage of the corresponding 100% binding control.

    Article Snippet: Proteins and sera Human C1 complex, C4, CRP and polyclonal goat anti-human CRP antibody were purchased from Sigma.

    Techniques: Infection, Immunoprecipitation, Incubation, Co-Immunoprecipitation Assay, SDS Page, Purification, Immunodetection, Enzyme-linked Immunosorbent Assay, Negative Control, Positive Control, Binding Assay

    Binding of CRP to six different immobilized proteins as a function of pH and temperature. Results of a protein ligand-binding assay are shown. Microtiter wells were coated with factor H, oxLDL, C3b, IgG, Aβ, and BSA. The unreacted sites in the wells were blocked with gelatin. CRP (10 μg/ml), diluted in TBS-Ca, pH 7.0–4.6, was then added to the wells. One set of wells was incubated at 25 °C and another at 37 °C, for 2 h. Bound CRP was detected by using a rabbit polyclonal anti-CRP antibody and HRP-conjugated donkey anti-rabbit IgG. The absorbance of the developed color was read at 405 nm and plotted on the y axis.

    Journal: The Journal of Biological Chemistry

    Article Title: Identification of Acidic pH-dependent Ligands of Pentameric C-reactive Protein *

    doi: 10.1074/jbc.M110.142026

    Figure Lengend Snippet: Binding of CRP to six different immobilized proteins as a function of pH and temperature. Results of a protein ligand-binding assay are shown. Microtiter wells were coated with factor H, oxLDL, C3b, IgG, Aβ, and BSA. The unreacted sites in the wells were blocked with gelatin. CRP (10 μg/ml), diluted in TBS-Ca, pH 7.0–4.6, was then added to the wells. One set of wells was incubated at 25 °C and another at 37 °C, for 2 h. Bound CRP was detected by using a rabbit polyclonal anti-CRP antibody and HRP-conjugated donkey anti-rabbit IgG. The absorbance of the developed color was read at 405 nm and plotted on the y axis.

    Article Snippet: Immunoaffinity purified polyclonal rabbit anti-CRP antibody was purified from the rabbit anti-human CRP antiserum (Sigma) by affinity chromatography on a CRP-conjugated agarose column prepared by using the AminoLink Immobilization kit (Pierce), as described previously ( ).

    Techniques: Binding Assay, Ligand Binding Assay, Incubation

    Reversible decrease in the PC-binding activity of CRP at acidic pH. Results of a PnC-binding assay are shown. Microtiter wells were coated with PnC. The unreacted sites in the wells were blocked with gelatin. CRP was then added to the wells and incubated at 37 °C for 2 h. Bound CRP was detected using a polyclonal anti-CRP antibody, anti-CRP mAbs HD2.4 and 3H12, and corresponding HRP-conjugated secondary antibodies. The absorbance of the developed color was read at 405 nm and plotted on the y axis. A , CRP was in TBS-Ca, pH 7.2. B , CRP was in TBS-Ca, pH 4.6, and incubated at 37 °C for 2 h before adding to the wells. C , as in B , except that the pH was neutralized before adding CRP to the wells.

    Journal: The Journal of Biological Chemistry

    Article Title: Identification of Acidic pH-dependent Ligands of Pentameric C-reactive Protein *

    doi: 10.1074/jbc.M110.142026

    Figure Lengend Snippet: Reversible decrease in the PC-binding activity of CRP at acidic pH. Results of a PnC-binding assay are shown. Microtiter wells were coated with PnC. The unreacted sites in the wells were blocked with gelatin. CRP was then added to the wells and incubated at 37 °C for 2 h. Bound CRP was detected using a polyclonal anti-CRP antibody, anti-CRP mAbs HD2.4 and 3H12, and corresponding HRP-conjugated secondary antibodies. The absorbance of the developed color was read at 405 nm and plotted on the y axis. A , CRP was in TBS-Ca, pH 7.2. B , CRP was in TBS-Ca, pH 4.6, and incubated at 37 °C for 2 h before adding to the wells. C , as in B , except that the pH was neutralized before adding CRP to the wells.

    Article Snippet: Immunoaffinity purified polyclonal rabbit anti-CRP antibody was purified from the rabbit anti-human CRP antiserum (Sigma) by affinity chromatography on a CRP-conjugated agarose column prepared by using the AminoLink Immobilization kit (Pierce), as described previously ( ).

    Techniques: Binding Assay, Activity Assay, Incubation

    Structural change in CRP after binding to immobilized proteins at acidic pH. Microtiter wells were coated with factor H, oxLDL, C3b, IgG, Aβ, and BSA. CRP (10 μg/ml), diluted in TBS-Ca, pH 7.0–4.6, was then added to the wells and incubated at 37 °C for 2 h. Bound CRP was detected using three different anti-CRP antibodies: a polyclonal anti-CRP antibody, anti-CRP mAb HD2.4, or anti-CRP mAb 3H12. After addition of appropriate HRP-conjugated secondary antibodies, the absorbance of the developed color was read at 405 nm and plotted on the y axis.

    Journal: The Journal of Biological Chemistry

    Article Title: Identification of Acidic pH-dependent Ligands of Pentameric C-reactive Protein *

    doi: 10.1074/jbc.M110.142026

    Figure Lengend Snippet: Structural change in CRP after binding to immobilized proteins at acidic pH. Microtiter wells were coated with factor H, oxLDL, C3b, IgG, Aβ, and BSA. CRP (10 μg/ml), diluted in TBS-Ca, pH 7.0–4.6, was then added to the wells and incubated at 37 °C for 2 h. Bound CRP was detected using three different anti-CRP antibodies: a polyclonal anti-CRP antibody, anti-CRP mAb HD2.4, or anti-CRP mAb 3H12. After addition of appropriate HRP-conjugated secondary antibodies, the absorbance of the developed color was read at 405 nm and plotted on the y axis.

    Article Snippet: Immunoaffinity purified polyclonal rabbit anti-CRP antibody was purified from the rabbit anti-human CRP antiserum (Sigma) by affinity chromatography on a CRP-conjugated agarose column prepared by using the AminoLink Immobilization kit (Pierce), as described previously ( ).

    Techniques: Binding Assay, Incubation