ZX-55114-96 | Human-C-Reactive-Protein-(CRP) ELISA Kit
C-reactive protein (CRP) belongs to the pentraxin family of proteins. It is synthesized by the liver and its level increases in response to inflammation. IL-6 primarily induces the transcription of CRP during the acute phase of an inflammatory/infectious disease. CRP is an acute-phase reactant protein and is widely used as a biomarker for systemic inflammation and tissue injury as its level rises and falls rapidly with the onset and eradication of the inflammatory stimulus, respectively.
CRP specifically binds to phosphocholine (PCh) residues of polysaccharides on many microbial pathogens and on apoptotic/necrotic cell membranes. Being recognized by the C1q complex of the complement system, the PCh-bound CRPs efficiently initiate the activation of the system, leading to the elimination of foreign pathogens. The binding of CRP to PCh on damaged cells facilitates the clearance of apoptotic/necrotic host cells, and contributes to the restoration of normal structure and function of injured tissue. Despite its anti-inflammatory properties, CRP can also exert pro-inflammatory properties when it is activated by autoantibodies, displaying the phosphocholine arm in auto-immune diseases.
The binding of CRP to Fc receptors FcγRI and FcγRIIa mediates the interaction of damaged cells or particles with phagocytic cells leading to phagocytosis of the cells or particles. The function of CRP in eliminating foreign pathogens and damaged cells through recruitment of the complement system and phagocytic cells makes CRP a critical molecule in the frontline of innate host defense. In response to infection, cell damage or tissue injury, the serum CRP concentration may increase by up to 1000 fold. Elevated CRP levels have been reported in patients with infection, chronic inflammatory disorders, myocardial infarction, ischemia/reperfusion injury, atherosclerosis, cancer, pulmonary disorders, metabolic syndrome and depression.
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