Complement Factor D/Adipsin Protein, Rhesus macaque (HEK293, His)

Complement factor D (CFD), also known as Adipsin, is a member of the S1, or chymotrypsin, family of serine peptidases. CFD is expressed by adipose cells, plays an important role in both physiology and pathophysiology, where it plays a regulatory role in the complement system. The complement system is activated as the first-line of defense against invading pathogens but is also involved in systemic inflammation, thrombosis and even autoimmune diseases. CFD plays a crucial role in the alternate pathway of the complement system by cleaving Factor B when it is complexed with Factor C3b. This cleavage activates the C3bbb complex, transforming it into the C3 convertase of the alternate pathway. In a process homologous to C1s in the classical pathway, CFD orchestrates the activation of the complement cascade, contributing to immune responses and host defense mechanisms. The specificity of its cleavage activity and its involvement in the formation of key complement complexes highlight the pivotal role of CFD in the regulation and amplification of the immune response against pathogens. In addition, CFD regulates collagen type I expression and fibroblast migration to enhance human tendon repair and healing outcomes^[1][2].