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The membrane attack complex of complement. Assembly, structure and cytotoxic activity.

Toxicology (1994-02-28)
A F Esser
RESUMEN

The membrane attack complex of complement is formed by the molecular fusion of the five terminal complement proteins, C5, C6, C7, C8, and C9. While the assembly process on a target membrane and its modulation by restriction factors present on host cells is now quite well understood the molecular details of the architecture of the complex still need much further clarification. This is especially true for the interaction of the last acting protein C9, which provides the cytotoxic action of the complex, with the precursor C5b-8 complex. Because of this lack of structural details the molecular mechanisms that lead to complement-mediated cell death remain cryptic, however, it is hoped that recent advances in controlling the assembly process and in site-specific modification of the terminal complement proteins by recombinant DNA techniques should change this predicament quickly.

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Sigma-Aldrich
Complement C7 from human serum, ≥85% (SDS-PAGE), ≥150,000 C7H50 units/mg protein