CRP Mouse

CRP is characterized by a cyclic pentameric structure, containing five identical protomers/subunits . Each subunit exhibits a lectin fold composed of two antiparallel beta-sheets with a flattened jellyroll topology . This structure allows CRP to play a crucial role in the body’s immune response by promoting agglutination, swelling of the bacterial capsule, and phagocytosis . Additionally, CRP can cause complement fixation via a calcium-dependent binding to the molecule phosphorylcholine .

CRP is an important and highly conserved acute-phase protein, synthesized primarily by hepatocytes under the control of the cytokine IL-6 . It serves as a well-established circulating marker of inflammation . In most vertebrates, CRP synthesis increases rapidly within hours after tissue injury or infection . However, in mice, CRP levels do not change appreciably during inflammation, suggesting that mouse CRP is not a typical acute-phase protein . Instead, serum amyloid P component (SAP), a homolog of CRP, is the major acute-phase protein in mice .

Recombinant mouse CRP is produced using various expression systems, including Pichia pastoris and Escherichia coli . The recombinant expression of mouse CRP in E. coli often fails to yield sufficient amounts of native protein due to the importance of post-translational modifications like glycosylation in aiding proper folding . By contrast, sufficient amounts of native mouse CRP can be successfully purified from P. pastoris . The purification process typically involves Nickel Chelating Sepharose Fast-Flow affinity chromatography and p-Aminophenyl Phosphoryl Choline Agarose resin affinity chromatography in tandem .

Recombinant mouse CRP is used in various research applications, including studies on inflammation, immune response, and disease models. It is also utilized in the development of diagnostic assays and therapeutic interventions.