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Related Experiment Videos

Optimal expression condition of recombinant RAP.

Jie Zhang1, Hong Zhang, Hao Bi

  • 1Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, China. tjzj121@sina.com

Journal of Huazhong University of Science and Technology. Medical Sciences = Hua Zhong Ke Ji Da Xue Xue Bao. Yi Xue Ying De Wen Ban = Huazhong Keji Daxue Xuebao. Yixue Yingdewen Ban
|March 30, 2007
PubMed
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Researchers optimized the expression of human Receptor Associated Protein (RAP) using prokaryotic systems. The study successfully produced functional RAP, suitable for further use as a research tool.

Area of Science:

  • Molecular Biology
  • Protein Expression
  • Biochemistry

Background:

  • Receptor Associated Protein (RAP) plays a crucial role in the low-density lipoprotein receptor (LDLR) family.
  • Efficient production of functional RAP is essential for its use as a research tool.

Purpose of the Study:

  • To construct and optimize the expression of recombinant human Receptor Associated Protein (RAP).
  • To compare the efficiency of different prokaryotic expression systems and induction conditions.
  • To verify the functionality of the purified recombinant RAP.

Main Methods:

  • Construction of recombinant plasmids using pT7-PL and pET-28a(+) vectors.
  • Expression in E. coli BL21 strains (BL21 (DE3) and BL21 (DE3, plysS)).
  • Optimization of induction conditions and purification using Ni(+)-NTA affinity chromatography.

Related Experiment Videos

  • Assessment of binding affinity with RAW264.7 cells.

    • Main Results:

    • Both pT7-PL and pET-28a(+) vectors yielded high expression of RAP.
    • The pT7-PL-RAP plasmid in the BL21 (DE3, plysS) strain showed significantly higher expression levels.
    • Expression was enhanced in the presence of chloramphenicol, with most RAP being soluble.
    • Purified RAP demonstrated strong binding to RAW264.7 cells.

    Conclusions:

    • Optimized expression conditions for recombinant human RAP were established.
    • Functional recombinant RAP was successfully produced and purified.
    • This provides a foundation for the development of RAP as a valuable research tool.