Objective:To establish a method of antitumor drug screening model based on recombinant hPPARγ-LBD as a target protein for lipid metabolism. Methods:pReceiver-B01-PPARγ- LBD expression plasmid was constructed and transferred into Escherichia coli BL2(1DE3)competent cells. Growth conditionswere optimized to induce soluble expression of hPPARγ-LBD recombinant protein. Purification was carried out by Nickel affinity chromatography. Ligand binding activity of the recombinant protein was determined by novel size exclusion chromatography and high performance liquid chromatography(SEC-HPLC)method with rosiglitazone as reference ligand and GW9662 as antagonist. Results:Under optimal conditions (16℃

0.6 mmol/L IPTG and induction time 20 h)

the soluble recombinant protein was expressed successfully. After one-step purification with Nickel affinity chromatography

41 mg of recombinant protein with more than 95% purity could be obtained from per liter Luria-Bertani(LB)medium. The Kd and percentage ofspecific bindingofrosiglitazone and tetrazanbigen tohPPARγ-LBDare 625 nmol/L

65% and 1 000 nmol/L

60%

respectively.Conclusion:In this study

a fast

stable and simple method could be used successfully to screen antitumor drug.