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Monoclonal antibody epitope mapping

Hoet, R.M.A., Raats, J.M.H., de Wildt, R., et al. (1998). Human monoclonal autoantibody fragments from combinatorial antibody libraries directed to the UlsnRNP associated U1C protein) epitope mapping, immunolocalization and V-gene usage. Mol. Immunol., 35, 1045-1055. [Pg.141]

Subsequent studies using IFN-y synthetic peptides to map the epitope specificity of monoclonal antibodies to murine IFN-y showed that N-terminal specific monoclonal antibodies neutralize IFN-y antiviral activity [29]. In receptor-... [Pg.445]

Johne, B., Gadnell, M., and Hansen, K (1993) Epitope mapping and binding kinetics of monoclonal antibodies studied by real time Biospecific Interaction Analysis using surface plasmon resonance J Immunol Methods 160, 191—198... [Pg.171]

Dixit, V. M., Galvin, N. J., O Rourke, K. M., and Frazier, W. A. 1986. Monoclonal antibodies that recognize calcium-dependent structures of human thrombospondin. Characterization and mapping of their epitopes. J. Biol. Chem. 267 1962-1966. [Pg.314]

Nelson, P. N., Westwood, O. M., Jefferis, R. 1997. Characterization of anti-IgG monoclonal antibody A57H by epitope mapping. Biochem. Soc. Trans. 25 373. [Pg.333]

VojteSek, B., Bartek, J., Midgley, C. A., and Lane, D. P. 1992. An immunohistochemical analysis of human nuclear phosphoprotein p53. New monoclonal antibodies and epitope mapping using recombinant p53. J. Immunol. Methods 757 237-244. [Pg.347]

Furst, D. O., Osborn, M., and Nave, R. (1988). The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy A map of ten nonrepetitive epitopes starting at the Z line extends close to the M line. J. Cell. Biol. 106, 1563-1572. [Pg.115]

Epitope mapping can be used to identify areas of a protein that an antibody recognizes and binds to. Monoclonal antibodies are easier to characterize, but epitope maps can also be produced for polyclonal antisera. [Pg.295]

Luther T, Magdolen V, Albrecht S, Kasper M, Riemer C, Kessler H, et al. Epitope-mapped monoclonal antibodies as tools for functional and morphological analyses of the human urokinase receptor in tumor tissue. Am J Pathol 1997 150(4) 1231-1244. [Pg.94]

B-Cell epitope mapping (foot-and-mouth disease, TMV antigen, shrimp allergen) T-Cell epitope mapping (type 1 diabetes, alloreactive T-cell) protein kinase substrate/inhibitor (protein kinase I) MHC class I molecule binding peptides and epitope mapping for monoclonal and polyclonal antibodies. [Pg.1436]

Monoclonal antibodies (MAbs) are specific immunological tools because they bind to a precise determintint (the epitope) on the surface of a protein. The procedure of identifying the binding site of a MAb is often termed epitope mapping. ... [Pg.105]

Wobus CE, Hugle-Dorr B, Girod A, Petersen G, Hallek M, Kleinschmidt JA. Monoclonal antibodies against the adeno-associated virus type 2 (AAV-2) capsid epitope mapping and identification of capsid domains involved in AAV-2-cell interaction and neutralization of AAV-2 infection. J Virol 2000 74 9281-9293. [Pg.92]

Protein blots can be used (i) to identify various constituents of a mixture and to establish their relationship(s) by EIH (epitope mapping) (ii) to localize these constituents by the sensitive immunostain after their haptenation and subsequent reaction with labeled anti-hapten antibodies and, (iii) to elute antibodies immobilized to a certain protein band ( poor man s monoclonals ). [Pg.444]

Papsidero, F. D., Sheu, M., and Ruscetti, F. W. (1989) HIV-1 neutralizing monoclonal antibodies that react with the pl7 core protein characterization and epitope mapping. J. Virol. 63,267-272. [Pg.209]

Pharmacia claims its BIAcore system can provide information on the affinity, specificity, kinetics, multiple binding patterns, and cooperativity of a biochemical interaction on line without the need of washing, sample dilution or labeling of a secondary interactant. Their scientists have mapped the epitope specificity patterns of thirty monoclonal antibodies (Mabs) against recombinant core HTV-l core protein. [Pg.678]

Ellgaard, L., Holtet, T.L., Moestrup, S.K., Etzerodt, M. and Thogersen, H.C. (1995). Nested sets of protein fragments and their use in epitope mapping characterization of the epitope for the S4D5 monoclonal antibody binding to receptor associated protein. J. Immunol. Meth. 180, 53-61. [Pg.177]

Dias P, Parham DM, Shapiro DN, et al. Monoclonal antibodies to the myogenic regulatory protein MyoDl epitope mapping and diagnostic utility. Cancer Res. 1992 52 6431-6439. [Pg.684]


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