Expression and Purification of Recombinant Human Endostatin / 中国肿瘤生物治疗杂志

ABSTRACT

Objective: To highly express rh-Endostatin from Pichia pastoris and purify it to homogeneity. Methods: Constructed Pichia pastoris X33/pLW202 was amplified and inoculated to ferment media. The supernatant of the strain was collected after induction. Through ultrafiltration, affinity and gel chromatography, rh-Endostatin with high purication was obtained. Results: 60mg/L rh-Endostatin was obstained from supernatant. HPLC showed its purity was above 98%. Conclusion: High level expression of secreted rh-Endostatin has been successfully achieved in Pichia pastoris expression system.