Human Complement Component C1s Biotinylated Antibody

The classical complement pathway plays a major role in innate immunity against infection. This pathway is triggered by C1, a multimolecular complex composed of the recognition protein C1q and two serine proteases, C1r and C1s. Following the C1q recognition, C1r is autoactivated, and in turn activates C1s, which cleaves C4 and C2, the C1 substrates (1). Both C1r and C1s activation involve cleavage of a specific Arg-Ile bond, converting single-chain proenzymes into active proteases of disulfide bond-linked chains (A and B) (2). The A chains contain multiple domains in the order of CUB1-EGF-CUB2-CCP1-CCP2-Activation Peptide. The B chains contain the serine protease catalytic domain. The full-length (amino acid residues 1‑688) of human C1s was expressed (3‑5). The purified protein corresponded to the processed active form, with A and B chains starting at residue Glu16 and Ile438, respectively.