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Related Experiment Videos

[Human interleukin-13 cDNA cloning and expression].

Z Sun1, J Si, S Liu

  • 1Institute of Basic Medical Sciences, CAMS and PUMC, Beijing 100005.

Zhongguo Yi Xue Ke Xue Yuan Xue Bao. Acta Academiae Medicinae Sinicae
|November 23, 2001
PubMed
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Researchers developed an efficient prokaryotic expression system for Human Interleukin-13 (HIL-13). This system successfully produced HIL-13 cDNA and expressed it as a fusion protein, achieving a 37% expression rate.

Area of Science:

  • Molecular Biology
  • Biotechnology
  • Immunology

Background:

  • Human Interleukin-13 (HIL-13) plays a crucial role in immune responses.
  • Efficient production of recombinant HIL-13 is essential for research and therapeutic applications.

Purpose of the Study:

  • To establish a robust and efficient prokaryotic expression system for Human Interleukin-13 (HIL-13).
  • To facilitate the large-scale production and study of HIL-13.

Main Methods:

  • Reverse Transcription Polymerase Chain Reaction (RT-PCR) was used to amplify HIL-13 cDNA.
  • The amplified cDNA was cloned into the pGEX-2T prokaryotic expression vector.
  • Expression was induced and the resulting fusion protein was analyzed.

Main Results:

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  • HIL-13 cDNA was successfully obtained and confirmed via sequencing.
  • A recombinant plasmid, pGEX-2T HIL-13, was constructed.
  • HIL-13 was expressed as a glutathione-s-transferase (GST-HIL-13) fusion protein with an approximate molecular weight of 39,000 Da.

Conclusions:

  • HIL-13 cDNA was successfully isolated from T lymphocytes.
  • The developed prokaryotic expression system achieved an approximate HIL-13 expression rate of 37%.