DOI: 10.5176/2301-3761_CCECP15.60

Authors: Bongmun Kang and Yoiichi Kumada

Abstract:

The PMMA-tag was genetically fused with the C-terminal region of VHH molecules. This antibody, VHH, is known as a single chain domain, which is devoid of light chains. The PMMA-tag, which could affect the isoelectric point (pI) changeable with charge of amino acid in VHHs were closely related to solubility of VHH molecules during refolding. The genetic fusion of PMMA-tag to C-terminal region of VHHs significantly affect the recovery of their soluble protein during refolding by 50 mM TAPS at pH 8.5. It could be refolded with a recovery of more than 95{6e6090cdd558c53a8bc18225ef4499fead9160abd3419ad4f137e902b483c465} by dialysis at pH 8.5. A marked difference in the antigen-binding activities in the adsorption state was significantly high in VHH-PM compared to wild type of VHH. There are approximately 8-fold differences in the antigen-binding activities in the adsorption state between VHH-PM and VHH.

Keywords: ELISA, Immobilization, Isoelectric point, pH, PMMA-tag, Refolding, Solubility, VHH

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