Abstract
Ever since the introduction of bacterial derived surface proteins like protein A that demonstrate a natural binding reactivity towards antibodies, affinity chromatography has evolved into a well-established technology for the purification of antibodies and antibody fragments. Although high selectivity is provided by these types of affinity ligands, not all antibodies or antibody fragments are covered, which then forces the use of non-affinity-based processes that are less selective and often result in lower one-step purity and yield. To fill these gaps, we here describe a novel range of CaptureSelect™ affinity resins that enables immunoaffinity chromatography for a much broader range of antibody targets.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Similar content being viewed by others
References
Ettre L (1993) Nomenclature for chromatography (IUPAC recommendations 1993). Pure Appl Chem 65(4):819–872
Hage D (1999) Affinity chromatography: a review of clinical applications. Clin Chem 45(5):593–615
Hjelm H, Hjelm K, Sjöquist J (1972) Protein A from Staphylococcus aureus: its isolation by affinity chromatography and its use as an immunosorbent for isolation of immunoglobulins. FEBS Lett 28(1):73–76
Shukla A et al (2007) Review, downstream processing of monoclonal antibodies: application of platform approaches. J Chromatogr B 848(1):28–39
Hober S, Nord K, Linhult M (2007) Protein A chromatography for antibody purification. J Chromatogr B 848(1):40–47
Grodzki A, Berenstein E (2010) Affinity chromatography: protein A and protein G sepharose. Methods Mol Biol 588:33–41
Nilson B et al (1992) Protein L from Peptostreptococcus magnus binds to the kappa light chain variable domain. J Biol Chem 267(4):2234–2239
Hamers-Casterman C et al (1993) Naturally occurring antibodies devoid of light chains. Nature 363:446–448
Muyldermans S (2001) Single domain antibodies: current status. J Biotechnol 74(4):277–302
van der Linden R et al (1999) Comparison of physical properties of llama VHH antibody fragments and mouse monoclonal antibodies. Biochim Biophys Acta 1431(1):37–46
Frenken L et al (2000) Isolation of antigen specific Llama VHH antibody fragments and their high level secretion by Saccharomyces cerevisiae. J Biotechnol 78(1):11–21
Kuroiwa Y et al (2009) Antigen-specific human polyclonal antibodies from hyperimmunized cattle. Nat Biotechnol 27(2):173–181
Reinhart D, Weik R, Kunert R (2012) Recombinant IgA production: single step affinity purification using camelid ligands and product characterization. J Immunol Methods 378(1–2):95–101
Sun Y et al (2012) Pilot production of recombinant human clotting factor IX from transgenic sow milk. J Chromatogr B 898:78–89
Klooster R et al (2012) Muscle-specific kinase myasthenia gravis IgG4 autoantibodies cause severe neuromuscular junction dysfunction in mice. Brain 135(4):1081–1101
Hermans P et al (2012) Reinventing affinity tags: innovative technology designed for routine purification of C-terminal EPEA-tagged recombinant proteins. Genet Eng Biotechnol News 32(17):48–49
Klooster R et al (2007) Improved anti-IgG and HSA affinity ligands: clinical application of VHH antibody technology. J Immunol Methods 324(1–2):1–12
Beyer T et al (2009) Serum-free production and purification of chimeric IgA antibodies. J Immunol Methods 346:26–27
Aitken R, Hosseini A, MacDuff R (1999) Structure and diversification of the bovine immunoglobulin repertoire. Vet Immunol Immunopathol 72(1–2):21–29
Low D, O’Leary R, Pujar N (2007) Future of antibody purification. J Chromatogr B 848(1):48–63
Liu J et al (2009) Comparison of camelid antibody ligand to protein A for monoclonal antibody purification. Biopharm Int 22(9):35–43
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2014 Springer Science+Business Media, New York
About this protocol
Cite this protocol
Hermans, P., Adams, H., Detmers, F. (2014). Purification of Antibodies and Antibody Fragments Using CaptureSelect™ Affinity Resins. In: Ossipow, V., Fischer, N. (eds) Monoclonal Antibodies. Methods in Molecular Biology, vol 1131. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-992-5_19
Download citation
DOI: https://doi.org/10.1007/978-1-62703-992-5_19
Published:
Publisher Name: Humana Press, Totowa, NJ
Print ISBN: 978-1-62703-991-8
Online ISBN: 978-1-62703-992-5
eBook Packages: Springer Protocols