The expression of antibacterial peptide CM4 in Escherichia coli fused with human soluble B lymphocyte stimulator activing factor
抗菌肽CM4与人可溶性B淋巴细胞因子hsBAFF在大肠杆菌中的融合表达

To explore the expression and function of antibacterial peptide CM4, the expression and biological activity of recombinant fusion protein CM4-hsBAFF were studied. The human soluble B lymphocyte stimulator activing factor (hsBAFF) gene was fused to the sequence encoding CM4 to construct an expression vector pET28a (+)/CM4-hsBAFF. The recombinant protein was high expression of soluble recombinant protein in Escherichia coli cells, and existed in the supernatant after sonication. Recombinant fusion protein which was purified through size-exclusion chromatography was identified by SDS-PAGE and Western blot analysis. SDS-PAGE and Western blot indicated that recombinant protein was secreted as a protein of around 22.0 KDa and can be specially recognized anti-hsBAFF antibody. The recombinant protein can be expressed and displays antimicrobial activity.