Abstract
Keratinocyte growth factor-2 (KGF-2) is a member of the fibroblast growth factor family. The full-length human KGF-2 coding sequence, gained by synthesizing, was cloned into the pPICZαA vector in frame with the yeast α-factor secretion signal under the transcriptional control of the AOX promoter and integrated into Pichia pastoris strain GS115. In shake-flask culture induced with methanol, the rhKGF-2 content was about 17.5% of the total secreted proteins. Under the optimal conditions, stable production of rhKGF-2 around 1.0 g/l was achieved. The recombinant protein was purified by heparin affinity chromatography. A preliminary biochemical characterization of purified rhKGF-2 was performed both by Western blot analysis and biological activity analysis, and the result demonstrated that the recombinant KGF-2 was expressed successfully.
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