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C-Reactive Protein (CRP) consists of five identical, non-covalently associated protomers that are arranged in a symmetrical fashion weighing ~ 23kDa as it participates in the systemic response to inflammation. CRP acts as a recognition molecule such that it binds specifically to certain molecular configurations either during cell death or on the surface of exposed pathogens. After an acute inflammatory stimulus, CRP is synthesized by hepatocytes. CRP sits on the short arm of chromosome 1 (in humans) and it contains only one intron and it is regulated at the transcriptional level by cytokine interleukin-6 (IL-6) and by interleukin-1β (IL-1β). Both IL-6 and IL-1β control expression of many acute phase protein genes through activation of several transcription factors including STAT3, C/EBP family members and Rel proteins (NF-κB).

Some of the biological effects/functions of CRP include: CRP's unique ability to only bind to phosphocholine ligands of either damaged or apoptotic cells. Additionally, CRP can bind to other ligands such as phosphoethanolamine, chromatin, histones, fibronectin, small nuclear ribonucleoproteins, laminin, and polycations. CRP also contains pleiotropic effects which produce both pro and anti-inflammatory responses.