AI Article Synopsis
- The study explores an alternative method for producing dimeric TGF-beta proteins by using a baculovirus expression system in insect larvae instead of costly eukaryotic cell systems like CHO cells.
- Recombinant human activin C protein was successfully expressed in Noctuidae larvae, showing a size of approximately 15 kD under reducing conditions and 20 kD under non-reducing conditions, indicating it forms dimers through disulfide bridges.
- This insect-based expression method is faster and more cost-effective than traditional eukaryotic cell culture, eliminating the need for expensive equipment and large-scale tissue culture processes.
Article Abstract
In order to generate dimeric recombinant transforming growth factor-beta (TGF-beta) proteins, expensive eucaryotic cell systems, such as CHO cells, are usually used. An alternative represents the expression of such proteins in insects using a baculovirus expression system. In this study, recombinant human activin C protein was expressed in Noctuidae larvae. On SDS-PAGE, the expressed protein has a size of about 15 kD under reducing conditions and of about 20 kD under non-reducing conditions. This suggests that activin C is expressed as a dimer and disulfide bridges can be formed. Compared with expression in eucaryotic cell culture systems, expression in insect larvae presents a rapid and low cost method, without the need for expensive tissue culture scale-ups or special equipment.
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| http://dx.doi.org/10.1016/s0166-0934(97)00215-2 | DOI Listing |
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