Molecular Mass
Recombinant Human DDR2/Fc is a disulfide-linked homodimeric protein. The reduced monomer consists of 616 amino acids and has a calculated molecular mass of 69.4 kDa. Due to glycosylation, rhDDR2/Fc monomer migRates as an approximately 87 kDa protein in SDS-PAGE under reducing conditions.
Background
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.
Derived from proteolytic degradation of complement C5, C5 anaphylatoxin is a mediator of local inflammatory process. Binding to the receptor C5AR1 induces a variety of responses including intracellular calcium release, contraction of smooth muscle, increased vascular permeability, and histamine release from mast cells and basophilic leukocytes (PubMed:8182049). C5a is also a potent chemokine which stimulates the locomotion of polymorphonuclear leukocytes and directs their migration toward sites of inflammation.