Your browser doesn't support javascript.
loading
Express the recombinant protein PD-L1 in prokaryotic and analyze its biological activity / 中华实验和临床病毒学杂志
Chinese Journal of Experimental and Clinical Virology ; (6): 5-7, 2009.
Article in Chinese | WPRIM | ID: wpr-332447
ABSTRACT
<p><b>OBJECTIVE</b>To 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.</p><p><b>METHODS</b>The 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.</p><p><b>RESULTS</b>The 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.</p><p><b>CONCLUSION</b>We 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.</p>
Subject(s)
Full text: Available Index: WPRIM (Western Pacific) Main subject: Recombinant Fusion Proteins / Antigens, CD / Gene Expression / Chemistry / Cloning, Molecular / Escherichia coli / B7-H1 Antigen / Genetics / Metabolism / Molecular Weight Limits: Humans Language: Chinese Journal: Chinese Journal of Experimental and Clinical Virology Year: 2009 Type: Article

Similar

MEDLINE

...
LILACS

LIS

Full text: Available Index: WPRIM (Western Pacific) Main subject: Recombinant Fusion Proteins / Antigens, CD / Gene Expression / Chemistry / Cloning, Molecular / Escherichia coli / B7-H1 Antigen / Genetics / Metabolism / Molecular Weight Limits: Humans Language: Chinese Journal: Chinese Journal of Experimental and Clinical Virology Year: 2009 Type: Article