Human Complement C5 Protein, His Tag (MALS verified)

Derived from proteolytic degradation of complement C5, C5 anaphylatoxin is a mediator of local inflammatory process. C5 precursor is first processed by the removal of 4 basic residues, forming two chains, beta and alpha, linked by a disulfide bond. C5 convertase activates C5 by cleaving the alpha chain, releasing C5a anaphylatoxin and generating C5b (beta chain + alpha' chain) . Activation of C5 by a C5 convertase initiates the spontaneous assembly of the late complement components, C5-C9, into the membrane attack complex. C5b has a transient binding site for C6. The C5b-C6 complex is the foundation upon which the lytic complex is assembled. The C5a anaphylatoxin interacts with C5AR1 and tick complement inhibitor. C5a is also a potent chemokine which stimulates the locomotion of polymorphonuclear leukocytes and directs their migration toward sites of inflammation.

This protein carries a polyhistidine tag at the C-terminus. The mature form of Complement C5 is a disulfide-linked heterodimer composed of proteolytically cleaved α and β chain. Each α and β chain has a calculated MW of 73.9 kDa (β chain) and 114.4 kDa (α chain) . The protein migrates as 66 kDa, 110 kDa and >180kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition, and >180 kDa under non-reducing (NR) condition (SDS-PAGE) .

● -20°C to -70°C for 12 months in lyophilized state; ● -70°C for 3 months under sterile conditions after reconstitution. For long term storage, the product should be stored at lyophilized state at -20°C or lower.

Immobilized Human Complement C5, His Tag (Cat. No. CO5-H52Ha) at 2 μg/mL (100 μL/well) can bind Anti-C5a (Human IgG1) with a linear range of 0.2-3 ng/mL (QC tested).