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mouse anti c4d detection antibody  (Quidel)


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    Structured Review

    Quidel mouse anti c4d detection antibody
    A scheme of the complement system. Complement can be activated via three different routes. The classical and lectin pathways have their own specific pattern recognition molecules (PRMs), whereas the alternative pathway is activated by a spontaneous tick-over of C3 and deposition of C3b molecules onto permissive surfaces, which is facilitated by properdin (P). All pathways converge at the stage of C3 convertases, which catalyse breakdown of C3 into C3a and C3b molecules. When C3b molecules bind to the convertase complex, it gives rise to the C5 convertase. Except for the triggers indicated for each pathway in the scheme, apoptotic and necrotic cellular debris as well as degradative protein fragments from the extracellular matrix can also trigger all three pathways [ , ]. In red and boldface type are the markers of complement activation analysed in our study: <t>C4d,</t> the end degradation product of C4b; C3bBbP, a soluble form of alternative C3 convertase including properdin; and sTCC, soluble terminal complement complex (a soluble form of C5b-9). Factor D Serine protease that cleaves factor B, Igs Immunoglobulins, MASP Mannose-binding lectin-associated serine protease, MBL Mannose-binding lectin
    Mouse Anti C4d Detection Antibody, supplied by Quidel, used in various techniques. Bioz Stars score: 95/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/mouse+anti+c4d+antibody+a253/pmc05052889-85-15-20?v=Quidel
    Average 95 stars, based on 6 article reviews
    mouse anti c4d detection antibody - by Bioz Stars, 2026-07
    95/100 stars

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    1) Product Images from "The complement system is activated in synovial fluid from subjects with knee injury and from patients with osteoarthritis"

    Article Title: The complement system is activated in synovial fluid from subjects with knee injury and from patients with osteoarthritis

    Journal: Arthritis Research & Therapy

    doi: 10.1186/s13075-016-1123-x

    A scheme of the complement system. Complement can be activated via three different routes. The classical and lectin pathways have their own specific pattern recognition molecules (PRMs), whereas the alternative pathway is activated by a spontaneous tick-over of C3 and deposition of C3b molecules onto permissive surfaces, which is facilitated by properdin (P). All pathways converge at the stage of C3 convertases, which catalyse breakdown of C3 into C3a and C3b molecules. When C3b molecules bind to the convertase complex, it gives rise to the C5 convertase. Except for the triggers indicated for each pathway in the scheme, apoptotic and necrotic cellular debris as well as degradative protein fragments from the extracellular matrix can also trigger all three pathways [ , ]. In red and boldface type are the markers of complement activation analysed in our study: C4d, the end degradation product of C4b; C3bBbP, a soluble form of alternative C3 convertase including properdin; and sTCC, soluble terminal complement complex (a soluble form of C5b-9). Factor D Serine protease that cleaves factor B, Igs Immunoglobulins, MASP Mannose-binding lectin-associated serine protease, MBL Mannose-binding lectin
    Figure Legend Snippet: A scheme of the complement system. Complement can be activated via three different routes. The classical and lectin pathways have their own specific pattern recognition molecules (PRMs), whereas the alternative pathway is activated by a spontaneous tick-over of C3 and deposition of C3b molecules onto permissive surfaces, which is facilitated by properdin (P). All pathways converge at the stage of C3 convertases, which catalyse breakdown of C3 into C3a and C3b molecules. When C3b molecules bind to the convertase complex, it gives rise to the C5 convertase. Except for the triggers indicated for each pathway in the scheme, apoptotic and necrotic cellular debris as well as degradative protein fragments from the extracellular matrix can also trigger all three pathways [ , ]. In red and boldface type are the markers of complement activation analysed in our study: C4d, the end degradation product of C4b; C3bBbP, a soluble form of alternative C3 convertase including properdin; and sTCC, soluble terminal complement complex (a soluble form of C5b-9). Factor D Serine protease that cleaves factor B, Igs Immunoglobulins, MASP Mannose-binding lectin-associated serine protease, MBL Mannose-binding lectin

    Techniques Used: Activation Assay, Binding Assay

    Synovial fluid concentrations of C4d, C3bBbP and soluble terminal complement complex (sTCC). a Box plots with subjects ordered by the diagnostic groups: reference, osteoarthritis (OA), rheumatoid arthritis (RA), pyrophosphate arthritis (PPA), and knee injuries split into recent injury and old injury. b Knee injury samples ordered by days after injury in subgroups of 24–46 subjects (Table ), showing recent injury and old injury groups. Boxes show the quartiles (median, 25th and 75th percentiles) with error bars and whiskers for the 10th and 90th percentiles. The quartiles of the reference group are extended as thin horizontal lines in both panels for comparison. Statistically significant group differences, determined by Mann-Whitney U test, versus the reference group are indicated by asterisks (*) and are presented in Additional file : Table S1. CAU Complement activation units
    Figure Legend Snippet: Synovial fluid concentrations of C4d, C3bBbP and soluble terminal complement complex (sTCC). a Box plots with subjects ordered by the diagnostic groups: reference, osteoarthritis (OA), rheumatoid arthritis (RA), pyrophosphate arthritis (PPA), and knee injuries split into recent injury and old injury. b Knee injury samples ordered by days after injury in subgroups of 24–46 subjects (Table ), showing recent injury and old injury groups. Boxes show the quartiles (median, 25th and 75th percentiles) with error bars and whiskers for the 10th and 90th percentiles. The quartiles of the reference group are extended as thin horizontal lines in both panels for comparison. Statistically significant group differences, determined by Mann-Whitney U test, versus the reference group are indicated by asterisks (*) and are presented in Additional file : Table S1. CAU Complement activation units

    Techniques Used: Diagnostic Assay, Comparison, MANN-WHITNEY, Activation Assay

    Correlation between  C4d,  C3bBbP and sTCC in reference and patient groups
    Figure Legend Snippet: Correlation between C4d, C3bBbP and sTCC in reference and patient groups

    Techniques Used:

    Correlation between  C4d,  C3bBbP, sTCC and other biomarkers in the recent injury group
    Figure Legend Snippet: Correlation between C4d, C3bBbP, sTCC and other biomarkers in the recent injury group

    Techniques Used:

     C4d,  C3bBbP, sTCC concentrations in the recent injury group in relation to structural features
    Figure Legend Snippet: C4d, C3bBbP, sTCC concentrations in the recent injury group in relation to structural features

    Techniques Used:



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    Quidel mouse anti c4d detection antibody
    A scheme of the complement system. Complement can be activated via three different routes. The classical and lectin pathways have their own specific pattern recognition molecules (PRMs), whereas the alternative pathway is activated by a spontaneous tick-over of C3 and deposition of C3b molecules onto permissive surfaces, which is facilitated by properdin (P). All pathways converge at the stage of C3 convertases, which catalyse breakdown of C3 into C3a and C3b molecules. When C3b molecules bind to the convertase complex, it gives rise to the C5 convertase. Except for the triggers indicated for each pathway in the scheme, apoptotic and necrotic cellular debris as well as degradative protein fragments from the extracellular matrix can also trigger all three pathways [ , ]. In red and boldface type are the markers of complement activation analysed in our study: <t>C4d,</t> the end degradation product of C4b; C3bBbP, a soluble form of alternative C3 convertase including properdin; and sTCC, soluble terminal complement complex (a soluble form of C5b-9). Factor D Serine protease that cleaves factor B, Igs Immunoglobulins, MASP Mannose-binding lectin-associated serine protease, MBL Mannose-binding lectin
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    https://www.bioz.com/product/mouse+anti+c4d+antibody+a253/pmc05052889-85-15-20?v=Quidel
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    Quidel mouse anti c4d antibody a253
    Mechanism of convertase stabilization by C4NeF isolated from patient seven. a Spontaneous decay of classical C3 convertase assembled from purified components. Sensitized erythrocytes were coated with C1 and C4. Addition of C2 initiated the process of convertase formation. Convertase activity was assessed at indicated time points in the same manner, as described in Figs. and . b The same experiment as in a but with CD55-Fc added together with C2. c Representative blot of the C4b degradation pattern (C4b, factor I, and C4BP present) and comparison to negative control with no factor I added and sample, in which C4b cleavage was inhibited by excessive anti-C4c antibody. d Quantification of <t>C4d</t> produced upon C4b degradation in the presence of Igs isolated from patient seven or from NHS. When anti-C4c antibodies were tested in the same experiments, C4d readout was below the lower level of detection and therefore is not shown. All graphs show data collected from at least 3 independent experiments and statistical significance was assessed with two-way ANOVA assay at * p < 0.05, ** p < 0.0,1 and *** p < 0.001
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    https://www.bioz.com/product/mouse+anti+c4d+antibody+a253/pmc04896984-49-10-18?v=Quidel
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    Quidel mouse anti human c4d antibody
    Mechanism of convertase stabilization by C4NeF isolated from patient seven. a Spontaneous decay of classical C3 convertase assembled from purified components. Sensitized erythrocytes were coated with C1 and C4. Addition of C2 initiated the process of convertase formation. Convertase activity was assessed at indicated time points in the same manner, as described in Figs. and . b The same experiment as in a but with CD55-Fc added together with C2. c Representative blot of the C4b degradation pattern (C4b, factor I, and C4BP present) and comparison to negative control with no factor I added and sample, in which C4b cleavage was inhibited by excessive anti-C4c antibody. d Quantification of <t>C4d</t> produced upon C4b degradation in the presence of Igs isolated from patient seven or from NHS. When anti-C4c antibodies were tested in the same experiments, C4d readout was below the lower level of detection and therefore is not shown. All graphs show data collected from at least 3 independent experiments and statistical significance was assessed with two-way ANOVA assay at * p < 0.05, ** p < 0.0,1 and *** p < 0.001
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    Image Search Results


    A scheme of the complement system. Complement can be activated via three different routes. The classical and lectin pathways have their own specific pattern recognition molecules (PRMs), whereas the alternative pathway is activated by a spontaneous tick-over of C3 and deposition of C3b molecules onto permissive surfaces, which is facilitated by properdin (P). All pathways converge at the stage of C3 convertases, which catalyse breakdown of C3 into C3a and C3b molecules. When C3b molecules bind to the convertase complex, it gives rise to the C5 convertase. Except for the triggers indicated for each pathway in the scheme, apoptotic and necrotic cellular debris as well as degradative protein fragments from the extracellular matrix can also trigger all three pathways [ , ]. In red and boldface type are the markers of complement activation analysed in our study: C4d, the end degradation product of C4b; C3bBbP, a soluble form of alternative C3 convertase including properdin; and sTCC, soluble terminal complement complex (a soluble form of C5b-9). Factor D Serine protease that cleaves factor B, Igs Immunoglobulins, MASP Mannose-binding lectin-associated serine protease, MBL Mannose-binding lectin

    Journal: Arthritis Research & Therapy

    Article Title: The complement system is activated in synovial fluid from subjects with knee injury and from patients with osteoarthritis

    doi: 10.1186/s13075-016-1123-x

    Figure Lengend Snippet: A scheme of the complement system. Complement can be activated via three different routes. The classical and lectin pathways have their own specific pattern recognition molecules (PRMs), whereas the alternative pathway is activated by a spontaneous tick-over of C3 and deposition of C3b molecules onto permissive surfaces, which is facilitated by properdin (P). All pathways converge at the stage of C3 convertases, which catalyse breakdown of C3 into C3a and C3b molecules. When C3b molecules bind to the convertase complex, it gives rise to the C5 convertase. Except for the triggers indicated for each pathway in the scheme, apoptotic and necrotic cellular debris as well as degradative protein fragments from the extracellular matrix can also trigger all three pathways [ , ]. In red and boldface type are the markers of complement activation analysed in our study: C4d, the end degradation product of C4b; C3bBbP, a soluble form of alternative C3 convertase including properdin; and sTCC, soluble terminal complement complex (a soluble form of C5b-9). Factor D Serine protease that cleaves factor B, Igs Immunoglobulins, MASP Mannose-binding lectin-associated serine protease, MBL Mannose-binding lectin

    Article Snippet: Briefly, for the C4d assay, a capture antibody against a C4d neoepitope, together with a mouse anti-C4d detection antibody (A253; Quidel, San Diego, CA, USA), followed by peroxidase-conjugated goat anti-mouse (P0447; Dako, Carpinteria, CA, USA) were used.

    Techniques: Activation Assay, Binding Assay

    Synovial fluid concentrations of C4d, C3bBbP and soluble terminal complement complex (sTCC). a Box plots with subjects ordered by the diagnostic groups: reference, osteoarthritis (OA), rheumatoid arthritis (RA), pyrophosphate arthritis (PPA), and knee injuries split into recent injury and old injury. b Knee injury samples ordered by days after injury in subgroups of 24–46 subjects (Table ), showing recent injury and old injury groups. Boxes show the quartiles (median, 25th and 75th percentiles) with error bars and whiskers for the 10th and 90th percentiles. The quartiles of the reference group are extended as thin horizontal lines in both panels for comparison. Statistically significant group differences, determined by Mann-Whitney U test, versus the reference group are indicated by asterisks (*) and are presented in Additional file : Table S1. CAU Complement activation units

    Journal: Arthritis Research & Therapy

    Article Title: The complement system is activated in synovial fluid from subjects with knee injury and from patients with osteoarthritis

    doi: 10.1186/s13075-016-1123-x

    Figure Lengend Snippet: Synovial fluid concentrations of C4d, C3bBbP and soluble terminal complement complex (sTCC). a Box plots with subjects ordered by the diagnostic groups: reference, osteoarthritis (OA), rheumatoid arthritis (RA), pyrophosphate arthritis (PPA), and knee injuries split into recent injury and old injury. b Knee injury samples ordered by days after injury in subgroups of 24–46 subjects (Table ), showing recent injury and old injury groups. Boxes show the quartiles (median, 25th and 75th percentiles) with error bars and whiskers for the 10th and 90th percentiles. The quartiles of the reference group are extended as thin horizontal lines in both panels for comparison. Statistically significant group differences, determined by Mann-Whitney U test, versus the reference group are indicated by asterisks (*) and are presented in Additional file : Table S1. CAU Complement activation units

    Article Snippet: Briefly, for the C4d assay, a capture antibody against a C4d neoepitope, together with a mouse anti-C4d detection antibody (A253; Quidel, San Diego, CA, USA), followed by peroxidase-conjugated goat anti-mouse (P0447; Dako, Carpinteria, CA, USA) were used.

    Techniques: Diagnostic Assay, Comparison, MANN-WHITNEY, Activation Assay

    Correlation between  C4d,  C3bBbP and sTCC in reference and patient groups

    Journal: Arthritis Research & Therapy

    Article Title: The complement system is activated in synovial fluid from subjects with knee injury and from patients with osteoarthritis

    doi: 10.1186/s13075-016-1123-x

    Figure Lengend Snippet: Correlation between C4d, C3bBbP and sTCC in reference and patient groups

    Article Snippet: Briefly, for the C4d assay, a capture antibody against a C4d neoepitope, together with a mouse anti-C4d detection antibody (A253; Quidel, San Diego, CA, USA), followed by peroxidase-conjugated goat anti-mouse (P0447; Dako, Carpinteria, CA, USA) were used.

    Techniques:

    Correlation between  C4d,  C3bBbP, sTCC and other biomarkers in the recent injury group

    Journal: Arthritis Research & Therapy

    Article Title: The complement system is activated in synovial fluid from subjects with knee injury and from patients with osteoarthritis

    doi: 10.1186/s13075-016-1123-x

    Figure Lengend Snippet: Correlation between C4d, C3bBbP, sTCC and other biomarkers in the recent injury group

    Article Snippet: Briefly, for the C4d assay, a capture antibody against a C4d neoepitope, together with a mouse anti-C4d detection antibody (A253; Quidel, San Diego, CA, USA), followed by peroxidase-conjugated goat anti-mouse (P0447; Dako, Carpinteria, CA, USA) were used.

    Techniques:

     C4d,  C3bBbP, sTCC concentrations in the recent injury group in relation to structural features

    Journal: Arthritis Research & Therapy

    Article Title: The complement system is activated in synovial fluid from subjects with knee injury and from patients with osteoarthritis

    doi: 10.1186/s13075-016-1123-x

    Figure Lengend Snippet: C4d, C3bBbP, sTCC concentrations in the recent injury group in relation to structural features

    Article Snippet: Briefly, for the C4d assay, a capture antibody against a C4d neoepitope, together with a mouse anti-C4d detection antibody (A253; Quidel, San Diego, CA, USA), followed by peroxidase-conjugated goat anti-mouse (P0447; Dako, Carpinteria, CA, USA) were used.

    Techniques:

    Mechanism of convertase stabilization by C4NeF isolated from patient seven. a Spontaneous decay of classical C3 convertase assembled from purified components. Sensitized erythrocytes were coated with C1 and C4. Addition of C2 initiated the process of convertase formation. Convertase activity was assessed at indicated time points in the same manner, as described in Figs. and . b The same experiment as in a but with CD55-Fc added together with C2. c Representative blot of the C4b degradation pattern (C4b, factor I, and C4BP present) and comparison to negative control with no factor I added and sample, in which C4b cleavage was inhibited by excessive anti-C4c antibody. d Quantification of C4d produced upon C4b degradation in the presence of Igs isolated from patient seven or from NHS. When anti-C4c antibodies were tested in the same experiments, C4d readout was below the lower level of detection and therefore is not shown. All graphs show data collected from at least 3 independent experiments and statistical significance was assessed with two-way ANOVA assay at * p < 0.05, ** p < 0.0,1 and *** p < 0.001

    Journal: Journal of Clinical Immunology

    Article Title: Testing the Activity of Complement Convertases in Serum/Plasma for Diagnosis of C4NeF-Mediated C3 Glomerulonephritis

    doi: 10.1007/s10875-016-0290-5

    Figure Lengend Snippet: Mechanism of convertase stabilization by C4NeF isolated from patient seven. a Spontaneous decay of classical C3 convertase assembled from purified components. Sensitized erythrocytes were coated with C1 and C4. Addition of C2 initiated the process of convertase formation. Convertase activity was assessed at indicated time points in the same manner, as described in Figs. and . b The same experiment as in a but with CD55-Fc added together with C2. c Representative blot of the C4b degradation pattern (C4b, factor I, and C4BP present) and comparison to negative control with no factor I added and sample, in which C4b cleavage was inhibited by excessive anti-C4c antibody. d Quantification of C4d produced upon C4b degradation in the presence of Igs isolated from patient seven or from NHS. When anti-C4c antibodies were tested in the same experiments, C4d readout was below the lower level of detection and therefore is not shown. All graphs show data collected from at least 3 independent experiments and statistical significance was assessed with two-way ANOVA assay at * p < 0.05, ** p < 0.0,1 and *** p < 0.001

    Article Snippet: Human sera depleted from C3 and/or C5 as well as mouse anti- C4d antibody (A253) were purchased from Quidel.

    Techniques: Isolation, Purification, Activity Assay, Comparison, Negative Control, Produced