CRP Human Recombinant

CRP is composed of 206 amino acids and has a predicted molecular mass of 23 kDa. Due to glycosylation, the apparent molecular mass of CRP is approximately 26 kDa in SDS-PAGE under reducing conditions . Structurally, CRP is a homopentamer, meaning it consists of five identical subunits arranged in a circular fashion .

The primary function of CRP is to bind to phosphocholine expressed on the surface of dead or dying cells and some types of bacteria. This binding activates the complement system, promoting phagocytosis by macrophages, which helps in clearing the pathogens and damaged cells from the body .

CRP is synthesized by hepatocytes (liver cells) in response to cytokines such as interleukin-6 (IL-6), interleukin-1 (IL-1), and glucocorticoids. These cytokines are released during infection, inflammation, or tissue damage. The level of CRP in human serum can increase up to 1,000-fold within 24-48 hours of an inflammatory stimulus . Once the inflammatory response subsides, CRP levels quickly return to baseline levels, typically less than 1 μg/mL .

CRP is widely used as a biomarker to detect and monitor various inflammatory conditions, including infections, autoimmune diseases, and cardiovascular diseases. Elevated levels of CRP are associated with an increased risk of cardiovascular events, making it a valuable tool in assessing cardiovascular health .

Recombinant human CRP is produced using recombinant DNA technology, where the DNA sequence encoding human CRP is inserted into an expression vector and introduced into host cells, such as HEK293 cells or mouse myeloma cells. These host cells then produce the CRP protein, which is subsequently purified for use in research and clinical applications .

Recombinant CRP is often used in laboratory research to study its structure, function, and role in various diseases. It is also used in the development of diagnostic assays and therapeutic interventions targeting inflammatory conditions .