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 (Western Pacific)
| ID: wpr-332447
Responsible library:
WPRO
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>
Full text:
Available
Health context:
Neglected Diseases
Health problem:
Neglected Diseases
/
Zoonoses
Database:
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
Document type:
Article