Related Experiment Video
Updated: May 4, 2026
Efficient Purification of Elastin-Like Polypeptides (ELPs) from E. coli Using an Organic Solvent-based Extraction and Precipitation Method
Published on: January 9, 2026
Expression and purification of soluble human APRIL in Escherichia coli using ELP-SUMO tag
Jie Zhang1, Lei Ma2, Shuang Quan Zhang2
1Jiangsu Institute of Hematology, The First Affiliated Hospital of Soochow University, Key Laboratory of Thrombosis and Hemostasis of Ministry of Health, Suzhou, Jiangsu Province, PR China; Jiangsu Province Key Laboratory for Molecular and Medical Biotechnology, Life Science College, Nanjing Normal University, Nanjing 210046, Jiangsu, PR China.
Abstract:
APRIL is a member of the tumor necrosis factor (TNF) family of ligands that mediate tumor cells proliferation as well as survival, depending on the cellular context. In this report, we present a novel method to obtain soluble human APRIL in Escherichia coli using the elastin-like polypeptide and SUMO (ELP-SUMO) tags. The fusion protein with ELP-SUMO tag was expressed in a soluble form at 15°C. After purification based on inverse transition cycling (ITC) method, the purified ELP-SUMO-hAPRIL fusion protein was subsequently cleaved by SUMO protease to release mature hAPRIL. Following affinity chromatography, the target protein was re-purified with high purity. Finally, about 4.8mg recombinant hAPRIL was obtained from 1l bacterial culture with no less than 85% purity. The molecular mass (Mr) of the recombinant hAPRIL was confirmed by MALDI-TOF MS as Mr 16,314. The purified hAPRIL exhibits biological activity on Jurkat cells. It is the first report on soluble production of hAPRIL in E. coli using ELP-SUMO tag.
