CRP is a pentameric protein found in the blood plasma, and it plays a pivotal role in the body’s immune response. It is produced by the liver in response to inflammation. The protein binds to phosphocholine expressed on the surface of dead or dying cells (and some types of bacteria) to activate the complement system via the C1Q complex. This process promotes phagocytosis by macrophages, thereby aiding in the clearance of necrotic and apoptotic cells.
The recombinant form of CRP, covering amino acids 19 to 224, is expressed in Escherichia coli and is a non-glycosylated polypeptide chain. This segment of CRP retains the biological activity of the full-length protein, making it suitable for various research applications. The recombinant protein is purified using advanced chromatographic techniques to ensure high purity and functionality .
Recombinant CRP is widely used in:
The preparation of recombinant CRP involves cloning the CRP gene into an expression vector, transforming E. coli cells, and inducing protein expression. The protein is then purified through a series of chromatographic steps, including ion exchange and size exclusion chromatography. The final product is typically greater than 95% pure, as confirmed by SDS-PAGE and HPLC analysis .
The availability of high-quality recombinant CRP has significantly advanced our understanding of inflammation and its role in various diseases. It has enabled detailed studies on the protein’s interaction with other molecules, its role in the immune response, and its potential as a therapeutic target.