High-affinity LPS binding domain(s) in recombinant factor C of a horseshoe crab neutralizes LPS-induced lethality.

@article{Tan2000HighaffinityLB,
  title={High-affinity LPS binding domain(s) in recombinant factor C of a horseshoe crab neutralizes LPS-induced lethality.},
  author={Nguan Soon Tan and Bow Ho and Jeak Ling Ding},
  journal={FASEB journal : official publication of the Federation of American Societies for Experimental Biology},
  year={2000},
  volume={14 7},
  pages={
          859-70
        }
}
SSCrFCES is a biologically active, recombinant fragment of factor C, which is the endotoxin-sensitive serine protease of the LAL coagulation cascade. The approximately 38 kDa protein represents the LPS binding domain of factor C. A novel secretory signal directs the secretion of SSCrFCES into the culture supernatant of Drosophila cells, and hence it is readily purified. By differential ultrafiltration followed by preparative isoelectric membrane electrophoresis, SSCrFCES was purified as an… CONTINUE READING

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