Recombinant Human C-Reactive Protein/CRP Protein

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C-reactive protein (CRP) also known as CRP protein is an acute-phase protein with a molecular mass of approximately 25 kDa. It is primarily synthesized in the liver in response to cytokines. This protein appears in the blood where it binds to phosphocholine expressed on the surface of dead or dying cells. CRP is often used as a biomarker for inflammation in the body and its levels in human and canine (anti CRP used) blood samples are measured using assays like the CRP ELISA test or CRP ELISA kit.

Biological function summary

CRP plays a significant role in the innate immune system by recognizing foreign pathogens and damaged cells. It does not form part of a larger complex but itself can bind to specific ligands initiating the complement cascade. This activation enhances phagocytosis by macrophages contributing to the clearance of necrotic and apoptotic cells. The CRP protein therefore acts as a fast responder in the presence of inflammation making it a useful indicator for monitoring inflammatory diseases.

Pathways

CRP operates predominantly within the acute-phase response pathway. Its production is upregulated by cytokines such as IL-6 which connects it to inflammation-signaling pathways. CRP also interacts with the complement system bridging innate and adaptive immunity. Besides CRP could indirectly influence pathways involving other inflammatory proteins like serum amyloid A and haptoglobin creating a network of responses important for managing inflammation.

Elevated CRP levels are commonly associated with cardiovascular diseases and rheumatoid arthritis. In cardiovascular diseases CRP acts as a marker for atherosclerosis where the protein levels correlate with disease severity. It connects with other proteins involved in inflammatory processes such as fibrinogen to contribute to disease pathology. In rheumatoid arthritis CRP provides insights into disease activity helping in the assessment of treatment responses.