Prokaryotic high-level expression and activity assay of extracellular domain of B7-2 (CD86) in vitro

Xiaocai Yan, Lüsheng Si*, Yili Wang, Baochang Lai, Yiping Geng

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


Objective: To clone, express and investigate the costimulatory activity of B7-2(IgV + C), extracellular domain of B7-2(CD86). Methods: B7-2(IgV + C) gene was amplified from B7-2 cDNA by PCR and then cloned into an prokaryotic expression vector pGEX-4T-3. The engineered E. coli were used to express protein. After denaturation and renaturation, the protein was used to stimulate human T lymphocytes cooperated with anti-CD3 in vitro. 3 H-TdR incorporation was used to detect the activation of T cells. Results: The plasmid pGEX-4T-3/hB7-2(IgV + C) was reconstructed and expressed a M, 55 × 103 fusion protein in E. coli at a level of 33% of the total cellular protein. The experiment in vitro suggested that the fusion protein activated human T lymphocyte. Conclusion: With the first signal, the recombinant protein B7-2(IgV + C) had costimulatory avtivity to activate T cells.

Original languageEnglish (US)
Pages (from-to)131-133
Number of pages3
JournalChinese Journal of Microbiology and Immunology
Issue number2
StatePublished - Mar 2002
Externally publishedYes


  • B7-2(CD86)
  • Costimulation
  • Fusion protein
  • Gene expression

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Virology


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