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complement factor h  (Novus Biologicals)


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    Novus Biologicals complement factor h
    Complement Factor H, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/complement+factor+h/Complement+Factor+H+Antibody+(C18%2F3)+%5BJanelia+Fluor%C2%AE+549%5D/10__1091_slash_mbc__e25___11___0547-128-18-37
    Average 94 stars, based on 1 article reviews
    complement factor h - by Bioz Stars, 2026-10
    94/100 stars

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    Related Articles

    Incubation:

    Article Title: TEP-1, a glial thioester protein is required for cilia organization and intraflagellar transport in ensheathed sensory neurons in <i>C. elegans</i>
    Article Snippet: 1 Department of Pharmacology and Physiology, University of Maryland School of Medicine, University of Maryland, Baltimore, MD 21201; Department of Integrative Biology, University of Wisconsin Madison, Madison, WI 53706; Department of Ophthalmology and Visual Sciences, University of British Columbia, Vancouver, BC V5Z 3N9, Canada; Department of Microbiology and Immunology, University of Maryland School of Medicine, University of Maryland, Baltimore, MD 21201

    Blocking Assay:

    Article Title: TEP-1, a glial thioester protein is required for cilia organization and intraflagellar transport in ensheathed sensory neurons in <i>C. elegans</i>
    Article Snippet: 1 Department of Pharmacology and Physiology, University of Maryland School of Medicine, University of Maryland, Baltimore, MD 21201; Department of Integrative Biology, University of Wisconsin Madison, Madison, WI 53706; Department of Ophthalmology and Visual Sciences, University of British Columbia, Vancouver, BC V5Z 3N9, Canada; Department of Microbiology and Immunology, University of Maryland School of Medicine, University of Maryland, Baltimore, MD 21201



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    Image Search Results


    FHR5 1-9 FH 1-5 binds to C3, destabilizes C3 convertase and acts as a cofactor for factor I. Binding profiles of increasing amounts of FHR5 1-9 FH 1-5 to surface bound C3, C3b, iC3b, C3d and BSA (negative control), detected with both anti-CFHR5 (a) and anti-FH (b) antibodies. Data shown are mean values of triplicate measurements; error bars denote the standard deviation. C3a generated by convertase formation on surface-bound C3b: ELISA plates were coated with purified C3b. Surface C3 convertase was formed by addition of purified factor B (FB), factor D (FD), and properdin (P). Then increasing amounts of either FH (c) or the FHR5 1-9 FH 1-5 (d) were added followed by addition of C3 to enable C3a generation. To investigate factor I (FI) co-factor activity, FI along with increasing amounts of either FH (e) or the FHR5 1-9 FH 1-5 (f) were added prior to the convertase formation step. NC—negative control, no FB, FD, or P added. PC—positive control, no FH, or FHR5 1-9 FH 1-5 added. P values were determined by one-way ANOVA with Dunnett’s multiple comparisons test; **** P < 0.0001. Fluid phase co-factor assay products were visualized by western blotting (g). Cofactor activity was indicated by the cleavage of C3b as determined by the presence of C3 α-chain fragments (arrow). Negative controls: C3, C3b, C3b with FH, C3b with FI, and FHR5 1-9 FH 1-5 alone. Positive control: C3b incubated with FH and FI.

    Journal: Clinical and Experimental Immunology

    Article Title: A novel fusion protein reduces kidney complement in experimental C3 glomerulopathy

    doi: 10.1093/cei/uxag015

    Figure Lengend Snippet: FHR5 1-9 FH 1-5 binds to C3, destabilizes C3 convertase and acts as a cofactor for factor I. Binding profiles of increasing amounts of FHR5 1-9 FH 1-5 to surface bound C3, C3b, iC3b, C3d and BSA (negative control), detected with both anti-CFHR5 (a) and anti-FH (b) antibodies. Data shown are mean values of triplicate measurements; error bars denote the standard deviation. C3a generated by convertase formation on surface-bound C3b: ELISA plates were coated with purified C3b. Surface C3 convertase was formed by addition of purified factor B (FB), factor D (FD), and properdin (P). Then increasing amounts of either FH (c) or the FHR5 1-9 FH 1-5 (d) were added followed by addition of C3 to enable C3a generation. To investigate factor I (FI) co-factor activity, FI along with increasing amounts of either FH (e) or the FHR5 1-9 FH 1-5 (f) were added prior to the convertase formation step. NC—negative control, no FB, FD, or P added. PC—positive control, no FH, or FHR5 1-9 FH 1-5 added. P values were determined by one-way ANOVA with Dunnett’s multiple comparisons test; **** P < 0.0001. Fluid phase co-factor assay products were visualized by western blotting (g). Cofactor activity was indicated by the cleavage of C3b as determined by the presence of C3 α-chain fragments (arrow). Negative controls: C3, C3b, C3b with FH, C3b with FI, and FHR5 1-9 FH 1-5 alone. Positive control: C3b incubated with FH and FI.

    Article Snippet: After incubation and washing, bound FHR5 1-9 FH 1-5 was detected using goat polyclonal anti-CFHR5 antibody (R&D systems), followed by mouse anti-goat/sheep IgG-HRP (Sigma) and finally TMB substrate (BD).

    Techniques: Binding Assay, Negative Control, Standard Deviation, Generated, Enzyme-linked Immunosorbent Assay, Purification, Activity Assay, Positive Control, Western Blot, Incubation