C2 is central to the activation of both the classical and the lectin pathways of complement. It forms the proteolytic subunit of the C3 and C5 convertase of both pathways. Initiation of each pathway generates proteolytic enzyme complexes which are bound to the target surface (C1q/C1r/C1s in the classical pathway and MBL/ Ficolin/ MASPs in the lectin pathway). C1s and MASP in these complexes activate both C4 and C2. They cleave a peptide bond in C4 depositing C4b on the surface. They also cleave C2 into two fragments. The larger fragment (C2a) binds to C4b and forms the C3/C5 convertase enzyme complex C4b,C2a. C2 and factor B are the two most heat sensitive complement components. Both may be largely inactivated by a 6 minute incubation at 56 °C. Care must be taken not to inactivate the many other heat sensitive complement components and it should be noted that heat inactivation only reduces the concentration of active C2, it does not completely inactivate it or remove the C2 protein.
Size
50 μg
Concentration
0.1 ml of approximately 0.5 mg/ml purified natural human C2 isolated from healthy blood donors, in Phosphate buffered saline, pH 6.0. The blood donors have been tested and found negative for various viruses (see table: Human blood test results). The exact protein concentration and functional activity is indicated on the label.