Data on enhanced expression and purification of camelid single domain antibodies from Escherichia coli classical inclusion bodies

Maristella Maggi; Claudia Scotti

doi:10.1016/j.dib.2017.03.039

Data on enhanced expression and purification of camelid single domain antibodies from Escherichia coli classical inclusion bodies

Data Brief. 2017 Mar 31:12:132-137. doi: 10.1016/j.dib.2017.03.039. eCollection 2017 Jun.

Authors

Maristella Maggi¹, Claudia Scotti¹

Affiliation

¹ Department of Molecular Medicine, Unit of Immunology and General Pathology, University of Pavia, Via Ferrata, 9, 27100 Pavia, Italy.

Abstract

Heterologous expression of high amounts of recombinant proteins is a milestone for research and industrial purposes. Single domain antibodies (sdAbs) are heavy-chain only antibody fragments with applications in the biotechnological, medical and industrial fields. The simple nature and small size of sdAbs allows for efficient expression of the soluble molecule in different hosts. However, in some cases, it results in low functional protein yield. To overcome this limitation, expression of a 6xHistag sdAb was attempted in different conditions in Escherichia coli BL21(DE3) cells. Data showed that high amount of sdAb can be expressed in E. coli classical inclusion bodies, efficiently extracted by urea in a short-time, and properly purified by metal ion affinity chromatography. These data originate from the research article "Enhanced expression and purification of camelid single domain VHH antibodies from classical inclusion bodies" Maggi and Scotti (2017) [1] (DOI: http://dx.doi.org/10.1016/j.pep.2017.02.007).

Keywords: Arginine extraction; Classical inclusion bodies; Non-classical inclusion bodies; Protein purification; Single domain antibody; Urea extraction; VHH; sdAb.