Secretory expression of synthetic human Fas ligand extracellular domain gene in Pichia pastoris: influences of tag addition and N-glycosylation site deletion, and development of a purification method.

@article{Muraki2006SecretoryEO,
  title={Secretory expression of synthetic human Fas ligand extracellular domain gene in Pichia pastoris: influences of tag addition and N-glycosylation site deletion, and development of a purification method.},
  author={Michiro Muraki},
  journal={Protein expression and purification},
  year={2006},
  volume={50 2},
  pages={137-46}
}
Human Fas ligand is a medically important membrane glycoprotein that induces the apoptosis of harmful cells. A new secretory expression and purification method was devised for the production of a large amount of recombinant human Fas ligand extracellular domain (hFasLECD) by Pichia pastoris. The expression plasmid containing a synthetic hFasLECD gene designed using yeast optimal codons was constructed for the secretion of hFasLECD. The secreted product exhibited the specific binding activity… CONTINUE READING
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