Mouse Anti-DNA Recombinant Antibody (clone 16-13) (CAT#: FAMAB-0075CQ)

Figure 1 Binding interactions of monoclonal autoantibody BV 16–13 with 21, 43, 84, and 114 bp dsDNA fragments.

The percentage of bound radiolabeled dsDNA fragments by BV 16–13 was determined using a double-filter binding assay. The percentages of bound and free were calculated by determining the amount of radiolabeled fragments captured on nitrocellulose relative to the amount of unbound radiolabeled dsDNA fragments that passed through the nitrocellulose and were retained on the DEAE membrane. Error bars represent the standard deviation of triplicate trials.

Workman, C. J., & Voss Jr, E. W. (2000). Interaction of dual-specific autoantibodies with dsDNA and a synthetic dimer peptide simulating the hinge region of IgG2a molecules. Molecular immunology, 37(15), 931-939.

Figure 2 Binding inhibition of the interaction between BV 16–13 and radiolabeled 43 bp dsDNA by the 9-amino acid hinge dimer.

The percentage bound was determined by calculating the amount of radiolabeled 43 bp dsDNA bound with varying concentrations of unlabeled dsDNA fragments present versus the amount of radiolabeled 43 bp dsDNA bound without inhibitor.

Workman, C. J., & Voss Jr, E. W. (2000). Interaction of dual-specific autoantibodies with dsDNA and a synthetic dimer peptide simulating the hinge region of IgG2a molecules. Molecular immunology, 37(15), 931-939.