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Expression, purification, and characterization of recombinant human keratinocyte growth factor-2 in Pichia pastoris

Paper ID Volume ID Publish Year Pages File Format Full-Text
25143 43555 2007 5 PDF Available
Title
Expression, purification, and characterization of recombinant human keratinocyte growth factor-2 in Pichia pastoris
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.

Keywords
Heterologous expression; KGF-2; Pichia pastoris
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Expression, purification, and characterization of recombinant human keratinocyte growth factor-2 in Pichia pastoris
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 132, Issue 1, 15 October 2007, Pages 44–48
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
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Full-text PDF Download
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