MOESM1 of Novel signal peptides improve the secretion of recombinant Staphylococcus aureus Alpha toxinH35L in Escherichia coli

Additional file 1: Table S1. Identified peptide sequences of secreted ATH35L in culture medium. Figure S1. SDS-PAGE analysis of purified ATH35L protein. Secreted ATH35L by NSP4 in culture medium was purified and used for N-terminal peptide sequencing analysis. Figure S2. The cell growth profiles of NSP4_ATH35L and dsbAss_ATH35L. Recombinant ATH35L gene expression was induced by addition of 0.5 mM IPTG at an optical cell density of 80 (OD600). After induction, cell culture was continued in fed-batch mode at 30 °C for an additional 12 h. Cultured cells were collected at different time points postinduction to determine the profiles of secreted ATH35L protein in culture medium. Figure S3. Western blot analysis of cell lysates and cell culture medium from dsbA_ATH35L and NSP4_ATH35L in a Micro24 fed-batch process. (a) Arrow indicates ATH35L protein in cell crude lysates. (b) Arrow indicates released mature ATH35L protein in cell culture medium. Purified ATH35L protein was used as a reference