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Inhibition of apoptosis by recombinant 30K protein originating from silkworm hemolymph
Eun Jeong Kim1, Hye Jung Park, Tai Hyun Park
1School of Chemical Engineering and Institute of Chemical Processes, Seoul National University, Gwanak-Gu Shilim-Dong San 56-1, South Korea.
Abstract:
In a previous study, we reported that silkworm hemolymph inhibits apoptosis and that the anti-apoptotic component in silkworm hemolymph is a 30K protein. In this study, the 30K protein encoded by 30Kc6 was expressed in Escherichia coli. The recombinant 30K protein was expressed as an inclusion body, and the inclusion body was separated and refolded by affinity column chromatography using a 6xHis tag. We demonstrated that apoptosis is inhibited by supplementing the culture medium with this purified recombinant 30K protein. The recombinant 30K protein inhibited the virus- or chemical-induced apoptosis in human cells as well as insect cells. Apoptosis-inhibitory activity of recombinant 30K protein was comparable to that of whole silkworm hemolymph. The recombinant 30K protein can be effectively used to minimize cell death and consequently increase the productivity by extending the production time of host cells in commercial animal cell culture.
Insights
Silkworm hemolymph contains a 30K protein that inhibits apoptosis (programmed cell death). This purified recombinant protein effectively prevents cell death in both human and insect cells, showing potential for commercial cell culture applications.
Area of Science:
- Biochemistry
- Cell Biology
- Molecular Biology
Background:
- Silkworm hemolymph was previously identified to inhibit apoptosis.
- A 30K protein was identified as the anti-apoptotic component in silkworm hemolymph.
Purpose of the Study:
- To express and purify the 30K protein encoded by 30Kc6 in Escherichia coli.
- To evaluate the apoptosis-inhibitory activity of the purified recombinant 30K protein in various cell types.
Main Methods:
- Gene expression of 30Kc6 in E. coli.
- Purification of recombinant 30K protein using affinity chromatography (6xHis tag).
- Assessment of apoptosis inhibition in virus- or chemical-induced apoptosis models in human and insect cells.
Main Results:
- The recombinant 30K protein was successfully expressed and purified.
- The purified recombinant 30K protein demonstrated significant apoptosis-inhibitory activity.
- This activity was comparable to that of whole silkworm hemolymph.
- The protein inhibited apoptosis in both human and insect cells.
Conclusions:
- The purified recombinant 30K protein effectively inhibits apoptosis.
- This protein has potential applications in commercial animal cell culture to minimize cell death and enhance productivity.
