expression and purification of recombinant protein in bacteria
Because of its simplicity and low cost, the Escherichia coli expression system is still used as the most widely used bacterial expression system and as the first choice for laboratory research and initial development of the product in commercial activities.
The overall process of expression and purification of recombinant protein in bacteria
This process includes the following steps, which will be further explained in the next posts for each stage: To generate the recombinant protein, we first clone our desired gene into a vector (plasmid); then, transfer the vector into a host cell. This process is called transformation. After the growth and proliferation of the host cell, the cells should be lysed to extract the cellular proteins. In the next step, we transfer the lysates containing the protein and the recombinant protein to the chromatography column. After several phases of column washing, the excessive proteins are washed and removed from the column, and only the recombinant protein remains attached to the column. In the final step, by the addition of elution buffer, the recombinant protein will be removed from the column.