Preparation and epitope characterization of monoclonal antibodies against firefly luciferase

Science in China. Series C, Life Sciences
Q XuG Xu

Abstract

The 6-His tagged firefly luciferase was highly expressed inE. coli and purified to homogeneity by affinity chromatography and gel filtration. After immunizing Balb/c mice with the antigen, 6 hybridomas clones were found to secrete monoclonal antibodies (mAbs) and the mAbs were also purified separately. The competitive binding experiments show that 2 mAbs can bind heat-denatured antigen or its proteolytic fragments but not the native luciferase, suggesting that their epitopes might be accommodated in the internal segments of the protein. On the other hand, the other 4 mAbs are capable of binding both native and denatured antigens. It infers that their epitopes locate in the segments on the protein surface. The results also suggest that the six mAbs are all sequence-specific.

References

Oct 1, 1991·Trends in Biochemical Sciences·M E Goldberg

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Citations

Jun 25, 2004·Protein Science : a Publication of the Protein Society·Qin XuGenjun Xu
Dec 25, 2008·The Journal of Comparative Neurology·Heike Diekmann, Claudia A O Stuermer
Aug 20, 2011·PLoS Genetics·Alaron LewisSusan E Brockerhoff
Dec 4, 2012·Viruses·Jiri SochorRene Kizek

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