Development of an enabling platform biotechnology for the production of proteins.

Protein-based drugs are a mainstay of modern medicine. In contrast to antibodies, most of these need highly individualized production processes which often limits their development. Here, we develop an immunoglobulin domain tag (i-Tag), which can be fused to any protein of interest. This tag is made of a linear arrangement of antibody light chain constant domains. It enhances expression as well as secretion of the fusion partner and allows for simple purification of several structurally and functionally distinct fusion proteins. Furthermore, it improves the biophysical characteristics of most fusion proteins tested, is inert, and does not compromise the fusion partners' functionality. Taken together, the i-Tag should facilitate the development of biopharmaceuticals and diagnostic proteins otherwise lacking a common structural element.

Aschenbrenner I ，Böckler M ，Franke F ，Liebl K ，Catici DAM ，Brandl M ，Behnke J ，Feige MJ ... -  《-》

Orthogonal protein purification facilitated by a small bispecific affinity tag.

Nilvebrant J ，Alm T ，Hober S 《Jove-Journal of Visualized Experiments》

A novel, cheap and effective fusion expression system for the production of recombinant proteins.

Ding FX ，Yan HL ，Mei Q ，Xue G ，Wang YZ ，Gao YJ ，Sun SH ... -  《APPLIED MICROBIOLOGY AND BIOTECHNOLOGY》

The YoaW signal peptide directs efficient secretion of different heterologous proteins fused to a StrepII-SUMO tag in Bacillus subtilis.

Heinrich J ，Drewniok C ，Neugebauer E ，Kellner H ，Wiegert T ... -  《Microbial Cell Factories》

Expression and purification of soluble monomeric streptavidin in Escherichia coli.

Demonte D ，Dundas CM ，Park S 《-》