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|Title:||Increased yield and activity of soluble single-chain antibody fragments by combining high-level expression and the Skp periplasmic chaperonin|
|Citation:||Protein Expression and Purification, 2001; 23(2):289-295|
|Publisher:||Academic Press Inc|
|Abstract:||The success of recombinant antibody fragments as diagnostic reagents and therapeutic agents depends on the availability of sufficient functional material. We have produced a bacterial expression vector that combines high-level expression driven by a modified Shine-Dalgarno sequence with the periplasmic chaperonin Skp. Using this vector, we are able to obtain higher yields of soluble antibody fragments from cultures without the need for supplementation of the culture medium during expression. The fragments produced in the presence of the Skp show improved antigen binding activity compared to when the chaperonin is absent.|
|Keywords:||Animals; Humans; Mice; Antigens, CD15; Bacterial Proteins; Escherichia coli Proteins; Immunoglobulin Fragments; DNA-Binding Proteins; Chaperonins; Molecular Chaperones; Recombinant Fusion Proteins; Flow Cytometry; Cloning, Molecular; Antigen-Antibody Reactions; Genetic Vectors; Promoter Regions, Genetic|
|Appears in Collections:||Paediatrics publications|
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