Biotinylated Human Complement C5 Protein, His,Avitag™ (MALS verified)

Protein

RT

73.9 kDa (β chain) & 116.1 kDa (α chain)

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.

Complement C5

This protein carries a polyhistidine tag at the C-terminus, followed by an Avi tag (Avitag™). 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 116.1 kDa (α chain). The protein migrates as 75 kDa, 120 kDa and 200 kDa under reducing (R) condition, and 200 kDa under non-reducing (NR) condition (SDS-PAGE) due to glycosylation.

PBS, pH7.4

trehalose