Download Single Domain Antibodies: Methods and Protocols by Dirk Saerens, Serge Muyldermans PDF

By Dirk Saerens, Serge Muyldermans

The improvement of the hybridoma expertise created the chance to acquire limitless quantities of monoclonal antibodies (mAb) with excessive specificity and affinity for any objective and to introduce mAbs in a variety of functions; even if, the cumbersome measurement of mAbs, high priced construction, and bulky engineering hampered usually their streamlined improvement in a few applications.  In unmarried area Antibodies: equipment and Protocols, professional researchers research unmarried variable area antibody fragments, known as VH, VL, VHH or VNAR. those fragments are the smallest intact antigen-binding fragments that may be produced recombinantly at low cost.  Written within the hugely winning tools in Molecular Biology™ sequence layout, chapters contain introductions to their respective subject matters, lists of the required fabrics and reagents, step by step, easily reproducible laboratory protocols, and pointers on troubleshooting and keeping off recognized pitfalls

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J Mol Biol 367: 358–372 27. Henderson KA et al (2007) Structure of an IgNAR-AMA1 complex: targeting a conserved hydrophobic cleft broadens malarial strain recognition. Structure 15:1452–1466 28. Engberg J et al (1995) Phage-display libraries of murine and human antibody Fab fragments. Methods Mol Biol 51:355–376 29. Nuttall SD et al (2002) A naturally occurring NAR variable domain binds the Kgp protease from Porphyromonas gingivalis. FEBS Lett 516: 80–86 30. Coia G, Hudson PJ, Lilley GG (1996) Construction of recombinant extended singlechain antibody peptide conjugates for use in the diagnosis of HIV-1 and HIV-2.

J Mol Biol 300:83–91 Conrath KE, Wernery U, Muyldermans S, Nguyen VK (2003) Emergence and evolution of functional heavy-chain antibodies in Camelidae. Dev Comp Immunol 27:87–103 Spinelli S, Frenken LG, Hermans P, Verrips T, Brown K, Tegoni M, Cambillau C (2000) Camelid heavy-chain variable domains provide efficient combining sites to haptens. Biochemistry 39:1217–1222 Lauwereys M, Arbabi GM, Desmyter A, Kinne J, Holzer W, De Genst E, Wyns L, Muyldermans S (1998) Potent enzyme inhibitors derived from dromedary heavy-chain antibodies.

The CH1, which functions as an anchor for the light chain in conventional antibodies is encoded in the gene of the heavy chain isotype for the HCAb but is removed during mRNA splicing, due to a point mutation in the splice signal at the 3¢ end of the CH1 exon (13, 14). Hence, the variable domain is joined directly to the hinge region in HCAbs. The removal of the CH1 domain is critical for the secretion of the HCAbs, since intact heavy chains are retained in the endoplasmic reticulum by specific chaperones interacting with the CH1 domain, and it is the displacement of these chaperones by the light chain that allows secretion of classic antibodies (15).

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