Recombinant Human C-Reactive Protein/CRP Protein, CF Summary
Details of Functionality
Measured by its binding ability in a functional ELISA. Immobilized recombinant human (rh) Fc gamma RIIA at 2 µg/mL (100 µL/well) can bind rhCRP with a linear range of 0.15-10 µg/mL.
Source
Mouse myeloma cell line, NS0-derived human C-Reactive Protein/CRP protein Phe17-Pro224
>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Binding Activity
Theoretical MW
23 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
26 kDa, reducing conditions
Publications
Read Publications using 1707-CR/CF in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in Tris-HCl, NaCl and CaCl2.
Purity
>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 200 μg/mL in sterile 20 mM Tris-HCl, pH 8.0.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human C-Reactive Protein/CRP Protein, CF
C-Reactive Protein
C-reactive protein, pentraxin-related
CRP
MGC88244
pentraxin 1
PTX1MGC149895
Background
CRP is a member of the pentraxin family of proteins that are characterized by a cyclic pentameric structure. Human CRP gene encodes a 224 amino acids precursor. The mature human CRP protein has 206 amino acids that are non-covalently linked to form the pentameter. Human CRP shares 71% and 64% amino acid sequence homology with mouse and rat respectively.
CRP, synthesized by hepatocytes, is a major acute phase serum protein in human. IL-6, IL-1 and glucocorticoids are the major inducer of the CRP gene. In response to infection, inflammation or tissue damage, the level of CRP in human serum can increase 1,000-fold within 24-48 hours. It will come back to base level of less than 1 μg/mL very fast. Human CRP is an acute-phase serum protein that plays a role in the first line in host innate host defense. Like other pentraxins, CRP exhibits Ca++‑dependent binding to ligands. Phosphocholine (PCh), a constituent of many bacterial and fungal walls, is a principal ligand of CRP. CRP also binds to the membrane of injured cells, membrane and nuclear components of necrotic and apoptotic cells. Upon binding with the ligands, CRP is recognized by C1q and initiates the activation of complement cascade. Ligand bound CRP also binds to Fc gamma RI and Fc gamma RIIa on phagocytes and activates phogocytotic responses. In addition to phogocytosis, CRP also can induce production of hydrogen peroxide and inflammatory cytokines, such as IL-1, IL-6 and TNF‑ alpha by monocytes. With these functions, human CRP is an important serum protein for anti-bacterial pathogen and clearance of damaged and apoptotic cells. However, in mouse, CRP is expressed at very low level and is not an acute phase reactant. Serum amyloid P component (SAP), another pentraxin, is the major acute phase serum protein in mice. It has been shown that high levels of CRP in humans is associated with an increased risk of cardiovascular diseases.
Gotschlich, E.C. and G.M. Edelman (1965) Proc. Natl. Acad. Sci. USA 54:558.
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