Complement factor B (CFB) is a critical serine protease in the alternative pathway of the complement system, an essential component of innate immunity. It circulates as a proenzyme and binds to activated C3b, forming the C3 convertase (C3bB), which is stabilized by properdin. Upon cleavage by factor D, CFB generates the active fragments Ba and Bb, with Bb retaining enzymatic activity to drive downstream complement activation, including the formation of the membrane attack complex (MAC) and amplification of inflammatory responses.
Antibodies targeting CFB are vital tools for studying its role in complement-mediated diseases, such as age-related macular degeneration (AMD), autoimmune disorders, and inflammatory conditions. These antibodies enable detection of CFB in various biological samples (e.g., plasma, tissues) using techniques like ELISA, Western blotting, and immunohistochemistry. Researchers also utilize CFB antibodies to investigate its interaction with other complement components, assess its activation status, or evaluate therapeutic interventions targeting the alternative pathway.
Dysregulation of CFB is linked to pathological inflammation and tissue damage, making it a potential biomarker or therapeutic target. Inhibitors of CFB, including monoclonal antibodies, are under exploration for conditions like paroxysmal nocturnal hemoglobinuria (PNH) and autoimmune kidney diseases. CFB-specific antibodies thus serve both diagnostic and research purposes, bridging mechanistic studies and clinical applications in complement-related disorders.