Recombinant Vaccinia virus Envelope phospholipase F13 (VACWR052)

The production process of the recombinant vaccinia virus Envelope phospholipase F13 (VACWR052) in the E. coli expression system involves several steps. Initially, the gene fragment encoding the full-length VACWR052 protein (1-372aa) is cloned into a suitable expression vector that incorporates an N-terminal 10xHis-tag and a C-terminal Myc-tag. Following transformation into E. coli host cells and selection, the transformed cells are cultured in a growth medium optimized for recombinant protein expression. Recombinant protein production is induced by the addition of IPTG as an inducer, and the cells are allowed to grow for a specific incubation period. Subsequently, the cells are harvested and lysed to release the intracellular contents containing the expressed recombinant VACWR052 protein. Through a purification process, a highly pure recombinant VACWR052 protein with a purity level of up to 90% is obtained, as confirmed by SDS-PAGE analysis.