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Antikörper

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Book cover Der Experimentator: Proteinbiochemie/Proteomics

Part of the book series: Experimentator ((EXPERIMENTATOR))

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Zusammenfassung

Es ist immer eine gute Idee, Antikörper gegen ein gereinigtes Protein herzustellen. Antikörper ermöglichen Immunoaffi nitätssäulen, immunologische Nachweistests, histologische Untersuchungen an Schnitten und das Screenen von Expressionsbanken. Antikörper gegen Peptidsequenzen eines Transmembranproteins informieren über seine Lage in der Membran, Antikörper gegen einzelne Untereinheiten oligomerer Proteine geben Auskunft über deren Zusammensetzung und Stöchiometrie.

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Literatur

  1. Griffiths, A. et al. (1993): Human antiself antibodies with high specificity from phage display libraries. EMBO J. 12, 725–734

    CAS  PubMed  Google Scholar 

  2. Marks, J. et al. (1992): Molecular evolution of proteins on flamentous phage. J. Biol. Chem. 267, 16007–16010

    CAS  PubMed  Google Scholar 

  3. Nissim, A. et al. (1994): Antibody fragments from a single pot phage display library as immunochemical reagents. EMBO J. 13, 692–698

    CAS  PubMed  Google Scholar 

  4. Verwandlung kleiner Moleküle in Antigene

    Google Scholar 

  5. Posnett, D. et al. (1988): A novel method for producing antipeptide antibodies. J. Biol. Chem. 263, 1719–1725

    CAS  PubMed  Google Scholar 

  6. Seguela, P. et al. (1984): Antibodies against γ-aminobutyric acid: specificity studies and immunocytochemical results. Proc. Natl. Acad. Sci. USA 81, 3888–3892

    Article  CAS  PubMed  Google Scholar 

  7. Wang, J. (1988): Antibodies for phosphotyrosine: analytical and preparative tool for tyrosylphosphorylated proteins. Anal. Biochem. 172, 1–7

    Article  CAS  PubMed  Google Scholar 

Antigenizität von Peptidsequenzen

  1. Parker, J. et al. (1986): New hydrophilicity scale derived from HPLC peptide retention data: correlation of predicted surface residues with antigenicity and X-ray derived accessible sites. Biochemistry 25, 5425–5432

    Article  CAS  PubMed  Google Scholar 

  2. Chiles, T. et al. (1987): Production of monoclonal antibodies to a low-abundance hepatic membrane protein using nitrocellulose immobilized protein as antigen. Anal. Biochem. 163, 136–142

    Article  CAS  PubMed  Google Scholar 

  3. Diano, M. et al. (1987): A method for the production of highly specific antibodies. Anal. Biochem. 166, 224–229

    Article  CAS  PubMed  Google Scholar 

  4. Hirokawa, N. (1978): Characterization of various nervous tissues of the chick embryos through responses to chronic application and immunocytochemistry of β -bungarotoxin. J. Comp. Neurol. 180, 449–466

    Article  CAS  PubMed  Google Scholar 

  5. Hem, A. et al. (1998): Saphenous Vein puncture for blood sampling of the mouse, rat, hamster, gerbil, guinea pig, ferret and mink. Laboratory Animals 32, 364–368.

    Article  CAS  PubMed  Google Scholar 

  6. Klundt, E. (2001): Tipps für Blutsauger. Laborjournal 11/2001, S61

    Google Scholar 

  7. Bukovsky, J. & Kennet, R. (1987): Simple and rapid purification of monoclonal antibodies from cell culture supernatants and ascites fluids by hydroxyl apatite chromatography on analytical and preparative scales. Hybridoma 6, 219–228

    Article  CAS  PubMed  Google Scholar 

  8. Dunbar, B. & Schwoebel, E. (1990): Preparation of polyclonal antibodies. Methods Enzymol. 182, 663–670

    Article  CAS  PubMed  Google Scholar 

  9. Ey, P. et al. (1978): Isolation of pure IgG1, IgG2a- and IgG2b-immunoglobulins from mouse serum using protein Asepharose. Immunochemistry 15, 429–436

    Article  CAS  PubMed  Google Scholar 

  10. Firestone, G. & Winguth, S. (1990): Immunoprecipitation of proteins. Methods Enzymol. 182, 688–700

    Article  CAS  PubMed  Google Scholar 

  11. Doolittle, M. et al. (1991): A two-cycle immunoprecipitation procedure for reducing nonspecific protein contamination. Anal. Biochem. 195, 364–368

    Article  CAS  PubMed  Google Scholar 

  12. Platt, E. et al. (1986): Highly sensitive immunoadsorption procedure for detection of low-abundance proteins. Anal. Biochem. 156, 126–135

    Article  CAS  PubMed  Google Scholar 

  13. Sakamoto, J. & Campbell, K. (1991): A monoclonal antibody to the β -subunit of the skeletal muscle dihydropyridine receptor immunoprecipitates the brain ω-conoto-xin GVIA receptor J. Biol. Chem. 266, 18914–18919

    CAS  PubMed  Google Scholar 

  14. Brymora, A. et al. (2001): Enhanced protein recovery and reproducibility from pulldown assays and immunoprecipitations using spin columns. Anal. Biochem. 295, 119–122c

    Article  CAS  PubMed  Google Scholar 

  15. Grässel, S. et al. (1989): Immunoprecipitation of labeled antigens with eupergit C1Z. Anal. Biochem. 180, 72–78

    Article  PubMed  Google Scholar 

  16. Peltz, G. et al. (1987): Monoclonal antibody immunoprecipitation of cell membrane glycoproteins. Anal. Biochem. 167. 239–244

    Article  CAS  PubMed  Google Scholar 

  17. Schneider, C. et al. (1982): A onestep purification of membrane proteins using a high efficiency immunomatrix. J. Biol. Chem. 257, 10766–10769

    CAS  PubMed  Google Scholar 

  18. Berryman, M. & Bretscher, A. (2001): Immunoblot detection of antigens in immunoprecipitates. BioTechniques 4, 744–746

    Google Scholar 

  19. Leah, J. et al. (1988): Purification of ornithine aminotransferase by immunoadsorption. Anal. Biochem. 170, 495–501

    Article  CAS  PubMed  Google Scholar 

  20. Mc Gillis, J. et al. (1987): Immunoafinity purification of membrane constituents of the IM-9 lymphoblast receptor for substance P. Anal. Biochem. 164, 502–513

    Article  CAS  Google Scholar 

  21. Haasemann, M. et al. (1991): Antiidiotypic antibodies bearing the internal image of a bradykinin epitope. J. Immunol. 147, 3882–3892

    CAS  PubMed  Google Scholar 

  22. Kleyman et al., (1991): Characterization and cellular localization of the epithelial Na+ channel. J. Biol. Chem. 266, 3907–3915

    CAS  PubMed  Google Scholar 

  23. Kussie, P. et al. (1989): Production and characterization of monoclonal idiotypes and antiidiotypes for small ligands. Methods Enzymol. 178, 49–63

    Article  CAS  PubMed  Google Scholar 

  24. Schick, M. & Kennedy, R. (1989): Production and characterization of antiidiotypic antibody reagents. Methods Enzymol. 178, 36–48

    Article  CAS  PubMed  Google Scholar 

  25. Frutos, M. et al. (1996) : Analytical Immunology. Methods Enzymol. 270, 82–101

    Article  PubMed  Google Scholar 

  26. Parker, C. (1990): Immunoassays. Methods Enzymol. 182, 700–718

    Article  CAS  PubMed  Google Scholar 

  27. Becker, C.-M. et al. (1989): Sensitive immunoassay shows selective association of peripheral and integral membrane proteins of the inhibitory glycine receptor complex. J. Neurochem. 53, 124–131

    Article  CAS  PubMed  Google Scholar 

  28. Lui, M. et al. (1996): Methodical analysis of proteinnitrocellulose interactions to design a refined digestion protocol. Anal. Biochem. 241, 156–166

    Article  CAS  PubMed  Google Scholar 

  29. Smith, C. et al. (1989): Sodium dodecyl sulfate enhancement of quantitative immunoenzyme dotblot assays on nitrocellulose. Anal. Biochem. 177, 212–219

    Article  CAS  PubMed  Google Scholar 

  30. Varghese, S. & Christakos, S. (1987): A quantitative immunobindiung assay for vitamin D dependent calcium binding protein (Calbindin-D28K) using nitrocellulose filters. Anal. Biochem. 165, 183–189

    Article  CAS  PubMed  Google Scholar 

  31. Wiedenmann, B. et al. (1988): Fractionation of synaptophysincontaining vesicles from rat brain and cultured PC12 pheochromocytoma cells. FEBS lett. 240, 71–779

    Article  CAS  PubMed  Google Scholar 

  32. Gregorius, K. & Theisen, M. (2001): In Situ Deprotection: A method for covalent immobilization of peptides with welldefinded orientation for use in solid phase immunoassays such as enzymelinked immunosorbent assay. Anal. Biochem. 299, 84–91

    Article  CAS  PubMed  Google Scholar 

Elisa mit adsorbiertem Antigen

  1. Kemeny, D. (1994): ELISA – Anwendung des Enzyme Linked Immunosorbent Assay im biologisch/medizinischen Labor. Gustav Fischer Verlag, Stuttgart

    Google Scholar 

  2. Kingan, T. (1989): A competitive enzymelinked immunosorbent assay: application in the assay of peptides, steroids, and cyclic nucleotides. Anal. Biochem. 183, 283–289

    Article  CAS  PubMed  Google Scholar 

  3. Yoshioka, H. et al. (1987): An assay of collagenase activity using enzymelinked immunosorbent assay for mammalian collagenase. Anal. Biochem. 166, 172–177

    Article  CAS  PubMed  Google Scholar 

Elisa mit adsorbiertem Antikörper

  1. Goers, J. et al. (1987): An enzymelinked immunoassay for lipoprotein lipase. Anal. Biochem. 166, 27–35

    Article  CAS  PubMed  Google Scholar 

  2. Kemeny, D. (1994): ELISA – Anwendung des Enzyme Linked Immunosorbent Assay im biologisch/medizinischen Labor. Gustav Fischer Verlag, Stuttgart

    Google Scholar 

  3. Kwan, S. et al. (1987): An enzyme immunoassay for the quantitation of dihydropteridin reductase. Anal. Biochem. 164, 391–396

    Article  CAS  PubMed  Google Scholar 

  4. Zhiri, A. et al. (1987): A new enzyme immunoassay of microsomal rat liver epoxid hydrolase. Anal. Biochem. 163, 298–302

    Article  CAS  PubMed  Google Scholar 

Konjugation von Antikörpern mit Markerenzymen

  1. Jeanson, A. et al. (1988): Preparation of reproducible alkaline phosphataseantibody conjugates for enzyme immunoassay using a heterobifunctional linking agent. Anal. Biochem. 172, 392–396

    Article  CAS  PubMed  Google Scholar 

  2. Tijssen & Kurstak (1984): Highly efficient and simple methods for the preparation of peroxidase and active peroxidaseantibody conjugates for enzyme immunoassays. Anal. Biochem. 136, 451–457

    Article  CAS  PubMed  Google Scholar 

  3. Wolfe, C. & Hage, D. (1995): Studies on the rate and control of antibody oxidation by periodate. Anal. Biochem. 231, 123–130

    Article  CAS  PubMed  Google Scholar 

  4. Chan, C. et al. (2004): Nanocrystal biolabels with releasable fluorophores for immunoassays. Anal. Chem. 76, 3638–3645

    Article  CAS  PubMed  Google Scholar 

  5. Trau, D. et al. (2002): Nanoencapsulated microcrystalline particles for superamplified biochemical Assays. Anal. Chem. 74, 5480–5486

    Article  CAS  PubMed  Google Scholar 

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Author information

Authors and Affiliations

  1. Rathausgasse 20, 79098, Freiburg

    Dr. Hubert Rehm

  2. Competence Pool Weihenstephan (CPW), Technische Universität München, Weihenstephaner Steig 23, 85354, Freising-Weihenstephan

    Dr. Thomas Letzel

Authors
  1. Dr. Hubert Rehm
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  2. Dr. Thomas Letzel
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© 2010 Spektrum Akademischer Verlag Heidelberg

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Rehm, H., Letzel, T. (2010). Antikörper. In: Der Experimentator: Proteinbiochemie/Proteomics. Experimentator. Spektrum Akademischer Verlag. https://doi.org/10.1007/978-3-8274-2313-9_6

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