Single chain variable fragments

De Jaeger, G. et al.. High level accumulation of single-chain variable fragments in the cytosol of transgenic Petunia hybrida. Eur. J. Biochem., 259, 426, 1999. 

Haidaris, C. G., Malone, J., Sherrill, L. A., Bliss, J. M., Gaspari, A. A., Insel, R. A., et al. (2001) Recombinant human antibody single chain variable fragments reactive with Candida albicans surface antigens. J. Immunol. Meth. 257, 185-202. 

Fu Y, Shearing LN, Haynes S, Crewther P, Tilley L, Anders RF, Foley M, Isolation from phage display libraries of single chain variable fragment antibodies that recognize conformational epitopes in the malaria vaccine candidate, apical membrane antigen-1, J. Biol. Chem., 272(41) 25678-25684, 1997. 

Liu R, Yuan B, Emadi S, Zameer A, Schulz P, McAllister C, Lyub-chenko Y, Goud G, Sierks MR (2004) Single chain variable fragments against beta-amyloid (Abeta) can inhibit Abeta aggregation and prevent abeta-induced neurotoxicity. Biochemistry 43 6959-6967. 

RPPs have been designed to capture proteins from cellular or tissue lysate samples or present in the serum or plasma onto surfaces (12), which are further identified by an affinity reagent such as antibody, single-chain variable fragments, and aptamers, among others. Thus, the signal could be related to specific protein detection and it could be affected by antibody affinity and... 

Levy-Mintz, P., Duan, L. X., Zhang, H. Z., Hu, B. C., Domadula, G., Zhu, M. H Kulkosky, J., Bizub-Bender, D., Skalka, A. M., and Pomerantz, R. J. (1996) Intracellular expression of single-chain variable fragments to inhibit early stages of the viral life cycle by targeting human immunodeficiency virus type 1 integrase. J. Virol. 70, 8821-8832. 

SJ Deng, CR MacKenzie, J Sadowska, et al. Selection of antibody single-chain variable fragments with improved carbohydrate binding by phage display. J Biol Chem 269 9533-9538, 1994. 

Rippmann J F, Klein M, Floischen C, Brocks B, Rettig W J, Gumpert J, Pfizenmaier K, Mattes R, Moosmayer D (1998). Procaryotic expression of single-chain variable-fragment (scFv) antibodies Secretion in L-form cells of Proteus mirabilis leads to active product and overcomes the limitations of periplasmic expression in Escherichia coli. Appl. Environ. Microbiol. 64 4862-4869. 

Olea-Popelka F, McLean M D, Horsman J, et al. (2005). Increasing expression of an anti-picloram single-chain variable fragment (ScFv) antibody and resistance to piclo-ram in transgenic tobacco (Nicotiana tabacum). J. Agric. Food Chem. 53 6683-6690. 

Deng X K, Nesbit L A, Morrow K J, Jr (2003). Recombinant single-chain variable fragment antibodies directed against Clostridium difficile toxin B produced by use of an optimized phage display system. Clin. Diagn. Lab. Immunol. 10 587-595. 

Choi G H, Lee D H, Min W K, et al. (2004). Cloning, expression, and characterization of single-chain variable fragment antibody against mycotoxin deoxynivalenol in recombinant Escherichia coli. Protein Expr. Purif. 35 84-92. 

Shaheen F, Duan L, Zhu M, et al. (1996). Targeting human immunodeficiency virus type 1 reverse transcriptase by intracellular expression of single-chain variable fragments to inhibit early stages of the viral life cycle. /. Virol. 70 3392-3400. 

Rousselet, N. et al. Inhibition of tumorigenicity and metastasis of human melanoma cells by anti-cathepsin L single chain variable fragment. Cancer Res. 2004, 64, 146-151. 

The MALDI-MS spot-on-a-chip sample preparation platform has been applied to protein array experiments, by microdispensing of a recombinant single-chain variable fragment (scFv) antibody specific for choleratoxin onto a nitrocellulose-coated nanovial array chip (Figure 49.12). This concept has later been considerably expanded by use of porous silicon as an arraying substrate by Ressine et The implementation of microfluidic array-based antibody assays to MALDI-MS... 

PHB biobeads displaying the ZZ domain of Protein A from Staphylococcus aureus as the result of N-terminal fusion to PhaC were found to be suitable to purify IgG from serum samples and culture supernatant with high binding capacity and purification power [20, 68]. Other binding domains were successfully displayed such as scFv (single-chain variable fragment) or streptavidin and enabled application of the respective beads as affinity purification resin [69,70). 

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