11/29/2023 0 Comments Permuted![]() ![]() To make the platform fusion protein process even more general such that any protein with an authentic N-terminus can be produced with high efficiency, the bacterial selection system PROFICS (PRotease Optimization via Fusion-Inhibited Carbamoyltransferase-based Selection) was used to evolve cpCasp2 into a variant with a catalytic turnover two orders of magnitude higher and the ability to cleave before any amino acid. While cleavage with cpCasp2 is possible before all 20 proteinogenic amino acids, cleavage before valine, leucine, isoleucine, aspartate and glutamate suffers from slow, and before proline extremely slow, turnover. The circularly permuted caspase-2 (cpCasp2) with its specific cleavage site, efficiently generates the untagged protein. Electronic address: protein technologies improve the expression and purification of recombinant proteins, but the removal of the tags involved requires specific proteases. ![]() 6 Austrian Centre of Industrial Biotechnology, Muthgasse 18, Vienna, Austria Department of Biotechnology, University of Natural Resources and Life Sciences, Vienna (BOKU), Muthgasse 18, Vienna, Austria.5 Biopharma Austria, Process Science, Boehringer Ingelheim Regional Center Vienna GmbH & Co KG, Vienna, Austria.4 Austrian Centre of Industrial Biotechnology, Muthgasse 18, Vienna, Austria. ![]()
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