Single chain antibody fragments

K. Grennan, G. Strachan, A.J. Porter, A.J. Killard, and M.R. Smyth, Atrazine analysis using an amperometric immunosensor based on single-chain antibody fragments and regeneration-free multi-calibrant measurement. Anal Chim. Acta 500, 287-298 (2003). 

An alternative approach to RNA suppression for controlled reduction of flavonoid enzyme activity is the expression of single-chain antibody fragments targeted to a key enzyme or TF. Early attempts with enzymes such as DFR have been inconclusive as to the effectiveness of the technology. 

Willems, P.M., Hoet, R.M., Huys, E.L., Raats, J.M., Mensink, E.J., Raymakers, R.A. (1998). Specific detection of myeloma plasma cells using anti-idiotypic single chain antibody fragments selected from a phage display library. Leukemia, 12, 1295-1302. 

Longstaff, M., C. Newell, B. Boonstra, G. Strachan, D. Learmonth, W. Harris, A. Porter, and W. Hamilton (1998). Expression and characterization of single-chain antibody fragments produced in transgenic plants against the organic herbicides atrazine and paraquat. Biochim. Biophys. Acta, 1381 147-160. 

In an attempt to increase efficacy in therapy, the production of bivalent or multivalent species by linking subunits (non-covalently, covalently, or by disulfide bonds) has been proposed. For example, a bispecific single-chain antibody fragment has been investigated for malaria therapy. This is a combination of two scFv, one directed against the CD3 molecule on human T lymphocytes, and the other against an epitope of a surface protein of Plasmodium falciparum, the parasite which causes malaria [8]. 

Huhalov A, Chester KA (2004), Engineered single chain antibody fragments for radioimmunotherapy, Q. J. Nucl. Med. Mol. Imag. 48 279-88. 

Di Paolo C, Willuda J, Kubetzko S, Lauffer I, Tschudi D, Waibel R, Pluckthun A, Stahel RA, Zangemeister-Wittke U. A recombinant immunotoxin derived from a humanized epithelial cell adhesion molecule-specific single-chain antibody fragment has potent and selective antitumor activity. Clin Cancer Res 2003 9 2837-48. 

Organometallic compounds appear to be a serious alternative to state-of-the-art labeling techniques as shown in the ongoing preclinical and clinical studies with organometallic-labeled tumor affine peptides and single-chain antibody fragments. ... 

Emadi S, Liu R, Yuan B, Schulz P, McAllister C, Lyubchenko Y, Messer A, Sierks MR (2004) Inhibiting aggregation of alpha-synuclein with human single chain antibody fragments. Biochemistry 43 2871-2878. 

Emadi S, Barkhordarian H, Wang MS, Schulz P, Sierks MR (2007) Isolation of a human single chain antibody fragment against oligomeric alpha-synuclein that inhibits aggregation and prevents alpha-synuclein-induced toxicity. J Mol Biol 368 1132-1144. 

Mouse recombinant Single chain antibody Fragment variable (ScFv) produced in E.Coli RPAS Purification Module 17-1362-01 HiTrap Anti-E column, accessories, pre-made buffers for 20 purifications 0.17 mg ScFv/5 ml... 

Ramirez N, Lorenzo D, Palenzuela D, Herrera L, Ayala M, Puentes A, Perez M, Gavilondo J, Dramas P (2000) Single-chain antibody fragments specific to the hepatitis B surface antigen, produced in recombinant tobacco cell cultures. Biotechnol Lett 22 1233-1236. 

Fischer, R., Drossard, J., Emans, N., Comman-deur, U., Hellwig, S.,Towards molecular farming in the future Pichia pastoris-hased production of single-chain antibody fragments. Biotechnol. Appl. Biochem. 1999, 30, 117-120. 

Zahnd, C., Spinelli, S., Luginbuhl, B., Am-stutz, P., Cambillau, C., Pluckthun, A. Directed in vitro evolution and crystallographic analysis of a peptide-binding single chain antibody fragment (scFv) with low picomolar affinity. J. Biol. Chem. 2004, 279, 18870-18877. 

Duggan J M, Coates D M, Ulaeto D O (2001). Isolation of single-chain antibody fragments against Venezuelan equine encephalomyelitis virus from two different immune sources. Viral Immunol. 14 263-273. 

Devaux C, Moreau E, Goyffon M, et al. (2001). Construction and functional evaluation of a single-chain antibody fragment that neutralizes toxin Aahl from the venom of the scorpion Androctonus australis hector. Eur. J. Biochem. 268 694-702. 

Yoshida S, Matsuoka H, Luo E, et al. (1999). A single-chain antibody fragment specific for the Plasmodium berghei ookinete protein Pbs21 confers transmission blockade in the mosquito midgut. Mol. Biochem. Parasitol. 104 195-204. 

Reinikainen, T. et al.. Comparison of the adsorption properties of a single-chain antibody fragment fused to a fungal or bacterial cellulose-binding domain. Enzyme Microb. Technol., 20, 143,1997. 

Wu, S.C. et al. (2002) Functional production and characterization of a fibrin-specific single-chain antibody fragment from Bacillus subtilis. effects of molecular chaperones and a wall-bound protease on antibody fragment production. Appl. Enviran. Microbiol, 68 (7), 3261-3269. 

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