Recombinant antibody fragments

Hayhurst A., Happe S., Mabry R., Koch Z., Iverson B.L., Georgiou G., Isolation and expression of recombinant antibody fragments to the biological warfare pathogen Brucella melitensis, J. Immunol. Meth. 2003 276 185-196. 

In mice with human breast carcinoma xenografts, a humanized IgG anti-HER-2 MAb eradicated well-established tumours [58]. In addition, a humanized version of an IgG anti-CD33 MAb (HuM 195) mediated ADCC in vitro [59] and had an 8.6-fold higher avidity than the parent murine Mab. Recombinant antibody fragments may have valnable properties as discnssed above, bnt their biophysical behavionr, prodnction yield and low thermostability leaves mnch to be desired and thereby limits their nsefnlness for in-vivo applications so far [60]. One possibility to improve these characteristics of scFv fragments with snboptimal stability and/or folding yield, is the grafting of their CDRs onto the framework of a different, more stable scFv [61,62]. 

Brinkmann, U., Recombinant antibody fragments and immunotoxin fusions for cancer therapy. In Vivo, 2000.14(1) 21-7. 

De Wildt, R.M.T., Ruytenbeek, R., van Venrooij, W.J., Hoet. R.M.A. (1997b). Heavy chain CDR3 optimization of a germline encoded recombinant antibody fragment predisposed to bind to the U1A protein. Protein Eng., 10, 835-843. 

Nen, D., Petrul, H., Winter, G., Light, Y, Marais, R, Britton, K E., and Creighton, A M. (1996) Radioactive labeling of recombinant antibody fragments by phosphorylation using casein kinase II and [y-32P]-ATP Nature Biotechnol. 114,485-490. 

Neri D, Carnemolla B, Nissim A, Leprini A, Querze G, Balza E, Pini A, Tarli L, Elalin C, Neri P, Zandi L, Winter G, Targeting by affinity-matured recombinant antibody fragments of an angiogenesis associated fibronectin isoform, Nat. Biotechnol., 15 1271-1275, 1997. 

Knappik A, Pluckthun A, An improved affinity tax based on the FLAG peptide for the detection and purification of recombinant antibody fragments,... 

Pennell CA, Eldin P. In vitro production of recombinant antibody fragments in Pichia pastoris. Res Immunol 1998 149(6) 599—603. 

Seeing better through a MIST evaluation of monoclonal recombinant antibody fragments on microarrays. 

Maynard, J.A., Maassen, C.B., Leppla, S.H., Brasky, K., Patterson, J.L., Iverson, B.L., Georgiou, G. (2002). Protection against anthrax toxin by recombinant antibody fragments correlates with antigen affinity. Nat. Biotechnol. 20 597-601. 

Borrebaeck, C. A. Ekstrom, S. Hager, A. C. Nilsson, J. Laurell, T. Marko-Varga, G., Protein chips based on recombinant antibody fragments A highly sensitive approach as detected by mass spectrometry, Biotechniques 2001, 30, 1126-1132... 

Angenendt, P. Wilde, J. Kijanka, G. Baars, S. Cahill, D. J. Kreutzberger, J. Lehrach, H. Konthur, Z. Glokler, J., Seeing better through a mist Evaluation of monoclonal recombinant antibody fragments on microarrays, Anal. Chem. 2004, 76, 2916-2921... 

PEREZ, L., et al., A multivalent recombinant antibody fragment specific for carcinoembryonic antigen, Biotechnol. Appl. Biochem. 43 (2006) 39-48. 

King D J, Turner A, Farnsworth A P, et al. (1994). Improved tumor targeting with chemically cross-linked recombinant antibody fragments. Cancer Res. 54 6176-6185. 

Li L, Olafsen T, Anderson A L, et al. (2002). Reduction of kidney uptake in radiometal labeled peptide linkers conjugated to recombinant antibody fragments. Site-specific conjugation of DOTA-peptides to a Cys-diabody. Bioconjug. Chem. 13 985-995. 

A novel quartz crystal microbalance method has been described, which measures the concentration of the antibiotic chloramphenicol, via antichloramphenicol antibodies, which were covalently coupled to the monolayer on a gold surface [44], While this approach shows some promise, the system described was of low sensitivity, detecting only in the pM range. The development of highly sensitive recombinant antibody fragments to atrazine [45] and their potential for expression in multiple different structural formats [46] will greatly aid the development of rapid biosensors for environmental contaminants in the future. 

Steinhauer C., Wingren C., Hager A. C., and Borrebaeck C. A., Single framework recombinant antibody fragments designed for protein chip applications. Biotechniques., Suppl 38-45, 2002. 

Blank K., Lindner R, Diefenbach B., and Rluckthun A., Self-immobilizing recombinant antibody fragments for immunoaffinity chromatography generic, parallel, and scalable protein purification. Protein Expr Purif, 24(2), 313-322, 2002. 

Other antibody-conjugated PET imaging agents include Cu-labeled monoclonal antibody 1A3, Y-labeled anti-Lewis Y monoclonal antibodies, Br-labeled human recombinant antibody fragment to the ED-B domain of fibro-nectin, and a review on isp 293-296 antigranulocyte... 

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