Express the recombinant protein PD-L1 in prokaryotic and analyze its biological activity.
- Author:
Li-Ping SHEN
1
;
Si-Yong CHEN
;
Tao BIAN
;
Yao YI
;
Feng WANG
;
Feng QIU
;
Sheng-Li BI
Author Information
- Publication Type:Journal Article
- MeSH: Antigens, CD; chemistry; genetics; isolation & purification; metabolism; B7-H1 Antigen; Cloning, Molecular; Escherichia coli; genetics; metabolism; Gene Expression; Humans; Molecular Weight; Recombinant Fusion Proteins; chemistry; genetics; isolation & purification; metabolism
- From: Chinese Journal of Experimental and Clinical Virology 2009;23(1):5-7
- CountryChina
- Language:Chinese
-
Abstract:
OBJECTIVETo construct the programmed cell death 1 ligant 1 (PD-L1) recombination expression vector, express the fusion protein in prokaryotic and analyze the biological action of express product.
METHODSThe whole PD-L1 gene sequence was synthesized after codon optimized. Construct the thioredoxin-(PD-L1) recombination expression vector and express the fusion protein in E. coli. Purified the target protein and analyze the conjugated ability of protein by ELISA.
RESULTSThe PD-L1 recombinant expression vector has been constructed correctly. The target protein has been obtained with which expressed in high efficiency and production. The target protein can conjugate specifically with the PD-1, its specific receptor.
CONCLUSIONWe have obtained the PD-L1 recombinant protein success with high biological activity. The result provide the basic condition for further study on antibody and mutually action between PD-L1 and chronic virus infectious.
