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CFD Purification Protocol
Factor D is a 24 kDa serine protease comprising 228 amino acids, also known as adipsin. Unlike most proteins of the complement system, which are synthesized by the liver and immune cells, factor D is predominantly produced by and secreted into the bloodstream by adipocytes. Plasma concentration of FD is very low and alternative sources have often been used, notably, urine from patients with renal tubular dysfunction or peritoneal dialysis fluid. The following method has been developed to purify factor D from plasma.
Fig.1 Flow chart of CFD purification protocol. (Creative Biolabs)
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Published Data
Efficient purification of CFD requires meticulous optimization of expression systems and chromatographic techniques. The expression of recombinant CFD in mammalian cells requires extensive deglycosylation with enzyme cocktails to reduce glycan variability while maintaining structural integrity. Size exclusion chromatography and MALS analysis performed after purification demonstrate a monodisperse sample with a polydispersity index under 1.001, which shows exceptional sample homogeneity. Functional assays, including binding kinetics with complement regulators, are critical to verify activity. Notably, deglycosylation reduces molecular mass by ~15–20 kDa, aligning with theoretical glycoprotein profiles. To maintain stability, purified CFD is stored in low-salt buffers at −80°C, with activity confirmed via fluorogenic substrate cleavage assays.
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