Objective  To construct a recombinant vector containing TAT-p38αG fusion gene HIV transcription factor TAT and a docking motif of p38α MAP kinase and investigate the transduction capability of the expressed TATp38αG fusion protein into endothelial cells.   Methods The p38αG fragment was amplified by PCR

cloned into pMD18-T vector

and then subcloned into pTAT-HA vector. The constructed vector pTAT-p38αG was further transfected into E. coli DH5α

and then into BL21 after sequencing. The expression of TAT-p38αG protein was induced by IPTG. After purification by Ni-NTA column and ultrafiltration

the fusion protein was labeled by FITC

and cocultured with endothelial cell line EVC304. The transduction capability of TAT-p38αG into EVC304 cell was then determined.   Results  The recombinant vector containing TAT-p38αG was constructed and TATp38αG protein was expressed successfully. FITC labeled TAT-p38αG protein was able to be transducted into EVC304 cells in a dose-dependent manner.   Conclusion  TAT-p38αG protein shows a high capability of transduction into endothelial cells

which enable us to further investigate its possible inhibitory role in p38α kinase activity.