Recombinant Human Antibody binds selectively to Human HCV NS.
Figure 1 Characterization of the specificity of binding of MAb ZX10 to rNS3 and 16-amino-acid synthetic peptides with a 6-amino-acid overlap by solid-phase EIA.
Zhang, Z. X., Lazdina, U., Chen, M., Peterson, D. L., & Sällberg, M. (2000). Characterization of a monoclonal antibody and its single-chain antibody fragment recognizing the nucleoside Triphosphatase/Helicase domain of the hepatitis C virus nonstructural 3 protein. Clin. Diagn. Lab. Immunol., 7(1), 58-63.
Figure 2 Characterization of the preferred binding of MAb ZX10 by testing serial dilutions of MAb ZX10 with rNS3 (h) and the peptide p1367 to 1382 (Œ) by solid-phase EIA.
Zhang, Z. X., Lazdina, U., Chen, M., Peterson, D. L., & Sällberg, M. (2000). Characterization of a monoclonal antibody and its single-chain antibody fragment recognizing the nucleoside Triphosphatase/Helicase domain of the hepatitis C virus nonstructural 3 protein. Clin. Diagn. Lab. Immunol., 7(1), 58-63.
This is a product of Creative Biolabs' Hi-Affi™ recombinant antibody portfolio, which has several benefits including:
• Increased sensitivity
• Confirmed specificity
• High repeatability
• Excellent batch-to-batch consistency
• Sustainable supply
• Animal-free production
See more details about Hi-Affi™ recombinant antibody benefits.
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