VHH antibodies: Emerging reagents for the analysis of ...
www.ncbi.nlm.nih.gov › pmc › articlesVHH had superior temperature stability and could bind antigen well at elevated temperature and higher concentrations of the chaotrope ammonium thiocyanate compared to mAbs. Both mAbs and VHHs showed no change in binding in the presence of up to 50% ethanol . Further examination of the crystal structure of a VHH revealed that although VHH lack the hydrophobic cleft typically formed by VL and VH chains, the CDRs of VHH are adaptable and binding may occur in any number of ways.