FcRn Affinity Column Gen2

prepacked column for affinity chromatography

custombiotech
fcrn gen2

Enhanced analysis of antibody half-life


The FcRn Affinity Column Gen 2 accelerates and standardizes antibody half-life analysis, so you can develop a meaningful lead candidate more quickly.  

The easy-to-use column works on your HPLC and allows you to:

  • monitor antibody behavior at multiple pH values, visualizing even minor differences in antibody and its half-life
  • automate antibody processing
  • eliminate potentially inconsistent coating densities for truly standardized analyses

     
With FcRn Affinity Column Gen 2 you can characterize and distinguish:
 
  • IgG variants with different Fab fragments
  • oxidized and native IgG
  • aggregated and monomeric IgG
  • wild-type and engineered IgG
  • antibody isotypes
  • aggregates and unbound serum albumin

  1. Alt, N., et al. (2016) Determination of critical quality attributes for monoclonal antibodies  using quality by design principles, Biologicals 44(5), 291 – 305  
  2. Cymer, F., et al. (2017) Evaluation of an FcRn affinity chromatographic method for IgG1- type antibodies and evaluation of IgG variants, Bioanalysis 9(17), 1305 – 1317 
  3. Datta-Mannan, A., et al. (2014) Application of FcRn binding assays to guide mAb  development, Drug Metab Dispos 42(11), 1867 – 1872
  4. Dostalek, M., et al. (2017) Pharmacokinetic de-risking tools for selection of monoclonal  antibody lead candidates, MAbs 9(5), 756 – 766  
  5. Edelmann, M. R., et al. (2019) Radiolabeled IgG antibodies: Impact of various labels on  neonatal Fc receptor binding, J Labelled Comp Radiopharm 62(11), 751 - 757  
  6. Edelmann, M. R., et al. (2021) Functional in vitro assessment of modified antibodies:  Impact of label on protein properties, PLoS One 16(9), e0257342 
  7. Gahoual, R., et al. (2017) Detailed Characterization of Monoclonal Antibody Receptor  Interaction Using Affinity Liquid Chromatography Hyphenated to Native Mass  Spectrometry, Anal Chem 89(10), 5404 – 5412 
  8. Haberger, M., et al. (2015) Functional assessment of antibody oxidation by native mass  spectrometry, MAbs 7(5), 891 – 900  
  9. Jensen, F. P., et al. (2017) A Two-pronged Binding Mechanism of IgG to the Neonatal  Fc Receptor Controls Complex Stability and IgG Serum Half-life, Mol Cell Proteomics  16(3), 451 – 456  
  10. Jensen, P. F., et al. (2015) Investigating the interaction between the neonatal Fc  receptor and monoclonal antibody variants by hydrogen/deuterium exchange mass  spectrometry, Mol Cell Proteomics 14(1), 148 – 161  
  11. Neuber, T., et al. (2014) Characterization and screening of IgG binding to the neonatal  Fc receptor, MAbs 6(4), 928 – 942  
  12. Piche-Nicolas, N. M., et al. (2018) Changes in complementarity-determining regions  significantly alter IgG binding to the neonatal Fc receptor (FcRn) and pharmacokinetics,  MAbs 10(1), 81 – 94  
  13. Pyzik, M., et al. (2019) The Neonatal Fc Receptor (FcRn): A Misnomer?, Front Immunol  10, 1540  
  14. Robbie G. J., et al. (2013) A novel investigational Fc-modified humanized monoclonal  antibody, motavizumab-YTE, has an extended half-life in healthy adults, Antimicrob  Agents Chemother 57(12), 6147 – 6153  
  15. Roopenian, D. C., et al. (2007) FcRn: the neonatal Fc receptor comes of age, Nature  Rev Immunol 7(9), 715 – 725  
  16. Schlothauer, T., et al. (2013) Analytical FcRn affinity chromatography for functional  characterization of monoclonal antibodies, MAbs 5(4), 576 – 586 
  17. Schoch, A., et al. (2015) Charge-mediated influence of the antibody variable domain on  FcRn-dependent pharmacokinetics, Proc Natl Acad Sci USA 112(19), 5997 – 6002  
  18. Sounders, C. A., et al. (2015) A novel in vitro assay to predict neonatal Fc receptor mediated human IgG half-life, MAbs 7(5), 912 – 921  
  19. Stracke, J., et al. (2014) A novel approach to investigate the effect of methionine  oxidation on pharmacokinetic properties of therapeutic antibodies, MAbs 6(5), 1229 –  1242  
  20. Suzuki, T., et al. (2010) Importance of neonatal FcR in regulating the serum half-life of therapeutic proteins containing the Fc domain of human IgG1: a comparative study of the  affinity of monoclonal antibodies and Fc-fusion proteins to human neonatal FcR, J  Immunol 184(4), 1968 – 1976  
  21. Walters, B. T., et al. (2016) Conformational Destabilization of Immunoglobulin G  Increases the Low pH Binding Affinity with the Neonatal Fc Receptor, J Biol Chem  291(4), 1817 – 1825  
  22. Wang, W., et al. (2011) Impact of methionine oxidation in human IgG1 Fc on serum half life of monoclonal antibodies, Mol Immunol 48(6-7), 860 – 866  
  23. Wang, W., et al. (2011) Monoclonal antibodies with identical Fc sequences can bind to  FcRn differentially with pharmacokinetic consequences, Drug Metab Dispos 39(9), 1469  – 1477  
  24. Wang, X., et al. (2017) Impact of SPR biosensor assay configuration on antibody:  Neonatal Fc receptor binding data, MAbs 9(2), 319 – 332  
  25. Wang, Y., et al. (2014) Neonatal Fc receptor (FcRn): a novel target for therapeutic  antibodies and antibody engineering, L Drug Target 22(4), 269 – 278

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