Anti-Human EGFR VHH Single Domain Antibody is a recombinant protein produced in E. coli.
Figure 1 Functional characterization of purified EgA1 ATTACK.
Biolayer interferometry (BLI)-derived sensorgrams (in black) for the interaction between immobilized EGFR-Fc and EgA1-based antibodies.
Harwood, S. L., Alvarez-Cienfuegos, A., Nuñez-Prado, N., Compte, M., Hernández-Pérez, S., Merino, N., ... & Mikkelsen, K. (2018). ATTACK, a novel bispecific T cell-recruiting antibody with trivalent EGFR binding and monovalent CD3 binding for cancer immunotherapy. Oncoimmunology, 7(1), e1377874.
Figure 2 Functional characterization of purified EgA1 ATTACK.
The binding to EGFR on the cell surface of HeLa cells by cetuximab- and EgA1-based antibodies at 0.1, 0.32, 1, and 10 nM, measured by FACS and normalized to the binding at 10 nM.
Harwood, S. L., Alvarez-Cienfuegos, A., Nuñez-Prado, N., Compte, M., Hernández-Pérez, S., Merino, N., ... & Mikkelsen, K. (2018). ATTACK, a novel bispecific T cell-recruiting antibody with trivalent EGFR binding and monovalent CD3 binding for cancer immunotherapy. Oncoimmunology, 7(1), e1377874.
Figure 3 Functional characterization of purified EgA1 ATTACK.
The binding to CD3 on the cell surface of Jurkat cells by OKT3- and EgA1-based antibodies at 0.1, 1, 3.2, and 10 nM, measured by FACS and normalized to the binding at 10 nM.
Harwood, S. L., Alvarez-Cienfuegos, A., Nuñez-Prado, N., Compte, M., Hernández-Pérez, S., Merino, N., ... & Mikkelsen, K. (2018). ATTACK, a novel bispecific T cell-recruiting antibody with trivalent EGFR binding and monovalent CD3 binding for cancer immunotherapy. Oncoimmunology, 7(1), e1377874.
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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