Abstract: For therapeutic antibody drugs, half-life is an important pharmacokinetic (PK) parameter and an important factor affecting the feasibility and usefulness of their clinical applications. IgG is the main therapeutic antibody drug commonly used in clinical practice, and research on its half-life modification is also constantly innovating. Currently, strategies to extend the half-life of IgG are mainly focused on crystallizable fragment (Fc) region modification, isoelectric point (pI) modification, glycosylation modification, pH-dependent modification of the antigen binding site and calcium-dependent modification of antigen binding site. In recent years, camel-derived nanobody (Nb) has gradually become a popular area of therapeutic antibody drug research. As a small molecule antibody with great potential, it is important to prolong its half-life, and strategies based on protein fusion, chemical modification, erythrocyte carrier and multivalent Nb have been applied to modify the half-life of Nb. In this paper, some existing strategies and methods for prolonging the half-life of IgG and Nb are introduced, and the application status after halflife modification is briefly described, hoping to provide some reference for more studies on half-life modification of therapeutic antibodies.