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X Ma1, Z Chen, H Zheng

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

Zhongguo Yi Xue Ke Xue Yuan Xue Bao. Acta Academiae Medicinae Sinicae
|May 23, 2001
PubMed
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This study demonstrates successful batch production of recombinant human interleukin-6 (rhIL-6) in E. coli. The high purity and activity of rhIL-6 meet requirements for mid-scale production.

Area of Science:

  • Biotechnology
  • Molecular Biology
  • Protein Expression

Background:

  • Recombinant human interleukin-6 (rhIL-6) is a crucial cytokine with therapeutic potential.
  • Efficient and scalable production methods are essential for its availability.

Purpose of the Study:

  • To investigate the feasibility of batch production for recombinant human interleukin-6 (rhIL-6).
  • To optimize expression and purification protocols for rhIL-6.

Main Methods:

  • Utilizing a pET30a vector with T7 promoter for rhIL-6 gene expression in E. coli.
  • Employing standard biochemical assays to determine protein characteristics and activity.

Main Results:

  • Achieved over 50% expression of recombinant protein relative to total cell protein.

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  • Characterized rhIL-6 with a molecular weight of 21,000 and an isoelectric point of 6.7.
  • Demonstrated high purity (>95%) and potent biological activity (0.35 ng/ml) using cell-based assays.

    • Conclusions:

    • The established batch production method yields high-quality rhIL-6 suitable for mid-scale applications.
    • The results confirm the potential of E. coli expression systems for producing functional rhIL-6.