目的　表达及纯化人分泌型肿瘤坏死因子相关激活诱导因子 (secretedformTNF relatedactivation in ducedcytokine,sTRANCE)蛋白。方法　将sTRANCE结构基因重组到含麦芽糖结合蛋白 (MBP)的融合蛋白原核表达载体 pMAL c2x中 ,在大肠杆菌中进行表达。 结果　经IPTG诱导表达出的MBP sTRANCE融合蛋白相对分子质量约 70 0 0 0 ,并经Westernblot分析证实。用直链淀粉琼脂糖凝胶 (amyloseresin)亲和层析纯化得到电泳均一的融合蛋白。结论　成功地获得sTRANCE蛋白 ,为进一步研究其生物学性能和用于肿瘤生物治疗的可能性打下了基础。 Objective To express and purify human secreted form of TNF related activation in duced cytokine (sTRANCE) protein. Methods The sTRANCE structural gene was recombined into prokaryotic expression vector pMAL c2x of fusion protein containing maltose binding protein (MBP) and expressed in E. coli. Results The relative molecular mass of MBP sTRANCE fusion protein induced by IPTG was about 70 000 and confirmed by Western blot analysis. Purification by amyloseresin affinity chromatography yielded an electrophoretically homogeneous fusion protein. Conclusion The successful obtaining of sTRANCE protein laid the foundation for the further study of its biological properties and possibility for tumor biological treatment.