Antigens antigen recognition

Mariuzza, R.A., Phillips, S.E.V., Poljak, R.J. The structural basis of antigen-antibody recognition. Annu. Rev. Biophys. Biophys. Chem. 16 139-159, 1987. 

Delon J, Bercovici N, Liblau R, Trautmann A. Imaging antigen recognition by naive CD4+ T cells compulsory cytoskeletal alterations for the triggering of an intracellular calcium response. Eur J Immunol 1998 28(2) 716-729. 

Roach, T.I.A., Else, K.J., Wakelin, D., McLaren, D.J. and Grencis, R.K. (1991) Trichuris murK. antigen recognition and transfer of immunity in mice by IgA monoclonal antibodies. Parasite Immunology 13, 1-12. 

Citraconic anhydride also has been used to reverse the effects of formalin fixation in tissue sections. Namimatsu et al. (2005) found that heating deparafinized tissue sections in a dilute solution of citraconic anhydride broke the formaldehyde crosslinks and restored antigen recognition of proteins within the samples. 

Varma, M. M. Nolte, D. D. Inerowicz, H. D. Regnier, F. E., Spinning disk self referencing interferometry of antigen antibody recognition, Opt. Lett. 2004, 29, 950 952... 

The Agilent multiple affinity removal system utilizes the specificity of antibody-antigen recognition for 14 highly abundant proteins from human serum samples. The affinity column achieves reproducible and specific depletion from human serum and plasma to eliminate 94% of interfering proteins. It allows identification of proteins down to nanograms per milliliter level as reported by Agilent. 

Steinbacher, S., Miller, S., Baxa, U., Budisa, N., Weintraub, A., Seckler, R., and Huber, R. (1997). Phage P22 tailspike protein Crystal structure of the head-binding domain at 2.3 A, fully refined structure of the endorhamnosidase at 1.56 A resolution, and the molecular basis of O-antigen recognition and cleavage. J. Mol. Biol. 267, 865-880. 

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