Covalent immobilization of antibodies for the preparation of immunoaffinity chromatographic supports

References

• Fitzgerald, J.; Leonard, P.; Darcy, E.; O’Kennedy, R. (2011). Immunoaffinity chromatography, in D. Walls, S. Loughran (Eds.), Protein Chromatography, Methods and Protocols. Humana Press: New York.
   Google Scholar
• Van Ginkel, L.A. (1991) Immunoaffinity chromatography, its applicability and limitations in multi-residue analysis of anabolizing and doping agents. Journal of Chromatography B: Biomedical Science Application, 564: 363–384.
   Web of Science ®Google Scholar
• Hage D.S.; Anguizola, J.A.; Bi, C., Li, R.; Matsuda, R.; Papastavros, E.; Zheng, X. (2012) Pharmaceutical and biomedical applications of affinity chromatography: Recent trends and developments. Journal of Pharmaceutical and Biomedical Analysis,69: 93–105.
   PubMed Web of Science ®Google Scholar
• Rhemrev-Boom, M.M.; Yates, M.; Rudolph, M.; Raedts, M. (2001) (Immuno)affinity chromatography: a versatile tool for fast and selective purification, concentration, isolation and analysis. Journal of Pharmaceutical and Biomedical Analysis, 24: 825–833.
   PubMed Web of Science ®Google Scholar
• Moser, A.C.; Hage, D.S. (2010) Immunoaffinity chromatography: an introduction to applications and recent developments. Bioanalysis, 2: 769–790.
   PubMed Web of Science ®Google Scholar
• Tamura, T.; Terada, T.; Tanaka, A. (2003) A quantitative analysis and chemical approach for the reduction of nonspecific binding proteins on affinity resins. Bioconjugate Chemistry,14: 1222–1230.
   Google Scholar
• Hage, D.S. (2006) Handbook of Affinity Chromatography, Taylor & Francis: Boca Raton.
   Google Scholar
• Nisnevitch, M.; Firer, M.A. (2001) Review: The solid phase in affinity chromatography: strategies for antibody attachment. Journal of Biochemistry and Biophysics Methods, 49: 467–480.
   PubMedGoogle Scholar
• Hage, D.S. (1998) Review: Survey of recent advances in analytical applications of immunoaffinity chromatography. Journal of Chromatography B: Biomedical Science Application, 715: 3–28.
   PubMed Web of Science ®Google Scholar
• Steen Redeker, E.; Ta, D.T.; Cortens, D.; Billen, B.; Guedens, W.; Adriaensens, P. (2013) Protein engineering for directed immobilization. Bioconjugate Chemistry, 24: 1761–1777.
   PubMed Web of Science ®Google Scholar
• Hanrahan, G.; Lu, K. (2006) Application of factorial and response surface methodology in modern experimental design and optimization. Critical Reviews in Analytical Chemistry, 36: 141–151.
   Web of Science ®Google Scholar
• Wu, Y.; Wu, P.Y. (2009) CD133 as a marker for cancer stem cells: progresses and concerns. Stem Cells and Development,18: 1127–1134.
   Google Scholar
• González-González, M.; Rito-Palomares, M. (2013) Aqueous two-phase systems strategies to establish novel bioprocesses for stem cells recovery. Critical Reviews in Biotechnology,34: 318–327.
   Google Scholar
• GenScript. (2015) THE PEG Antibody (Mouse). http://www.genscript.com/peg_antibody_mab.html.
   Google Scholar
• Rao, S.V.; Anderson, K.W.; Bachas, L.G. (1998) Oriented immobilization of proteins. Microchimica Acta,128: 127–143.
   Web of Science ®Google Scholar
• Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry, 72: 248–254.
   PubMed Web of Science ®Google Scholar
• Haaland, P.D. (1989) Experimental Design in Biotechnology, CRC Press: New York.
   Google Scholar
• Cuatrecasas, P.; Parikh, I. (1972) Adsorbents for affinity chromatography. Use of N-hydroxysuccinimide esters of agarose. Biochemistry, 11: 2291–2299.
   PubMed Web of Science ®Google Scholar
• Kalkhof, S.; Sinz, A. (2008) Chances and pitfalls of chemical cross-linking with amine-reactive N-hydroxysuccinimide esters. Analytical and Bioanalytical Chemistry,392: 1–8.
   Google Scholar
• Guo, S.L.; Chen, P.C.; Chen, M.S.; Lin, J.M.; Lee, H.C.; Chen, C.S. (2012) A fast universal immobilization of immunoglobulin G at 4°C for the development of array-based immunoassays. PLoS One, 7 (12): e51370.
   Google Scholar
• Wang, W.; Singh, S.; Zeng, D.L.; King, K.; Nema, S. (2007) Antibody structure, instability, and formulation. Journal of Pharmaceutical Sciences, 96: 1–26.
   PubMed Web of Science ®Google Scholar
• Zheng, J.Y., Janis, L.J. (2006) Influence of pH, buffer species, and storage temperature on physicochemical stability of a humanized monoclonal antibody LA298. International Journal of Pharmaceutics, 308: 46–51.
   PubMed Web of Science ®Google Scholar
• Jiang, K.; Schadler, L.S.; Siegel, R.W.; Zhang, X.; Zhang, H.; Terrones, M. (2004) Protein immobilization on carbon nanotubes via a two-step process of diimide-activated amidation. Journal of Materials Chemistry,14: 37–39.
   Web of Science ®Google Scholar
• Matson, R.S.; Little, M.C. (1988) Strategy for the immobilization of monoclonal antibodies on solid-phase supports. Journal of Chromatography A, 458: 67–77.
   Web of Science ®Google Scholar
• Salvador, J.P.; Sánchez-Baeza, F.; Marco, M.P. (2010) A high-throughput screening (HTS) immunochemical method for the analysis of stanozolol metabolites in cattle urine samples. Journal of Chromatography B, 878: 243–252.
   PubMed Web of Science ®Google Scholar
• Ramya, R.; Rajalakshmi, S.; Subramanian, B.M.; Rao, S.U.; Rao, K.R.S.; Villupanoor, S.A. (2012) Immuno-affinity purification of insect cell expressed rabies virus glycoprotein using a conformational specific monoclonal antibody. Journal of Advanced Veterinary Research, 2: 232–238.
   Google Scholar
• Zandian, M.; Jungbauer, A. (2009) An immunoaffinity column with a monoclonal antibody as ligand for human follicle stimulating hormone. Journal of Separation Science, 32: 1585–1591.
   PubMed Web of Science ®Google Scholar
• Ellison, S.L.R.; Farrant, T.J.; Barwick, V.J. (2009) Practical Statistics for the Analytical Scientist : A Bench Guide, Royal Society of Chemistry: Cambridge.
   Google Scholar
• Czajkowsky, D.M.; Shao, Z. (2009) The human IgM pentamer is a mushroom-shaped molecule with a flexural bias. Proceedings of the National academy of Sciences,106: 14960–14965.
   PubMed Web of Science ®Google Scholar
• Nezlin, R.S. (1998) The Immunoglobulins: Structure and Function, Academic Press: San Diego.
   Google Scholar
• Groopman, J.D.; Trudel, L.J.; Donahue, P.R.; Marshak-Rothstein, A.; Wogan, G.N. (1984) High-affinity monoclonal antibodies for aflatoxins and their application to solid-phase immunoassays. Proceedings of the National academy of Sciences of the United States of America, 81: 7728–7731.
   PubMed Web of Science ®Google Scholar
• Strandh, M.; Ohlson, S.; Ohlin, M.; Borrebaeck, C.A.K. (1998) New approach to steroid separation based on a low affinity IgM antibody. Journal of Immunology, 214: 73–79.
   Google Scholar