Recombinant Human cytomegalovirus Large structural phosphoprotein (UL32), partial,Biotinylated

The generation process of the biotinylated recombinant human cytomegalovirus Large structural phosphoprotein (UL32) in the E. coli expression system involves several steps. Firstly, the desired gene fragment coding for the 1-285 amino acids of the human UL32 protein is cloned into a suitable expression vector, which incorporates an N-terminal MBP-tag and a C-terminal 6xHis-Avi-tag for efficient purification and biotinylation. The recombinant vector is co-transfected into E.coli cells with the pBirA Cm^r plasmid. After transformation into E. coli host cells and selection, the transformed cells are cultured in a growth medium optimized for protein expression. Subsequently, the cells are harvested and lysed to release the intracellular contents containing the expressed recombinant UL32 protein. Biotinylation is then performed using biotin ligase enzyme-mediated site-specific biotinylation. The purified biotinylated recombinant UL32 protein demonstrates a high purity level of up to 90% as determined by SDS-PAGE analysis.