Half-Life Assessment: The Crucial Role of FcRn

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Antibody half-life is a vital parameter in therapeutic antibody development, directly influencing both efficacy and the frequency of administration. A key determinant of antibody half-life is the interaction between the Fc region and the neonatal Fc receptor (FcRn). FcRn plays a critical role in regulating the recycling of antibodies within the body, thereby prolonging their half-life.

IgGs experience high serum half-life due to the protective FcRn recycling pathway. Adapted from Roopenian et al., 2007.

To evaluate this interaction, we offer a range of FcRn-related products and services, including For the screening and validation of antibody drugs, we have developed a series of Fc receptor-related products, including:

 FcRn Proteins: high homogeneity and purity, verified by SEC-MALS

 FcRn Binding Kits (TR-FRET): No washing steps & Results in just 1 hour.

 FcRn Stable Cell Lines: Stable passage over 20 generations

Verification Data

FcRn High Homogeneity Structure Verified by SEC-MALS

The purity of Biotinylated Canine FCGRT&B2M Heterodimer Protein, His,Avitag&Tag Free (Cat. No. FCM-C82W9) is more than 95% and the molecular weight of this protein is around 43-53 kDa verified by SEC-MALS.

FcRn Binding Affinity Verification for Herceptin®

Immobilized Biotinylated Human FCGRT&B2M Heterodimer Protein, His,Avitag (Cat. No. FCM-H82W7) on SA Chip can bind Herceptin® with an affinity constant of 0.267 μM

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FcRn binding kit: Application of antibody drug Half-Life Assessment

The half-lives of these 3 monoclonal antibodies currently in clinical use generally correlate with the binding affinity to FcRn. The kit has been used to detect 3 FDA approved antibody drugs of different binding affinity to FcRn, and the IC50 trends are consistent with affinity constant from SPR as well as the actual in vivo half-life published.

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