In previous study, a novel gene, LRRC4, a member of leucine-rich repeat(LRR) superfamily was cloned. Expression analysis indicated that LRR may play an important role in the central nervous system. To investigate the function and the structure-function relationship of LRRC4, full length coding region was amplified and subcloned into pGEM T Easy vector. Further, the recombinant plasmid, pEGFP-C1/LRRC4, was constructed and transfected transiently into U251 cell. Under the fluorescence microscope, the green fluorescence produced by LRRC4 fusion protein was observed on the cytoplasmic membrane. Consistent to prediction by bioinformatics, this result indicated that product of LRRC4 is a membrane protein. In addition, the recombinant of LRRC4，pGEX-4T-2/LRRC4 and truncated LRRC4 recombinant, pGEX-4T-2/mLRRC4, were constructed and transformed into E.coli BL21. Induced by 0.5 mmol/L IPTG, The band corresponding to fusion protein were observed in SDS-PAGE as expected. Together with bioinformatic analysis of LRRC4 protein, these results establish the basis for functional study of LRRC4.