In vitro protein expression is a technique that enables researchers to express and reproduce recombinant proteins more quickly than is possible using traditional protein expression methods, because there is no need to transform, transfect, or culture cells in order to analyze proteins of interest.
We have optimized several cell-free expression systems for the rapid synthesis of recombinant proteins, utilizing bacterial, rabbit reticulocyte, and human derived lysate systems. The bacterial systems are ideal for producing high protein yield, while the mammalian-based systems are more likely to produce proteins with native posttranslational modifications. The human derived proteins are typically full-length and functionally active, with higher yield than is obtained using rabbit reticulocyte lysates. For membrane-bound proteins, we include a lipid bilayer with protein scaffolding for expression with our MembraneMax Protein Expression System.
Comparison of cell-free protein expression systems
| E. coli | Rabbit reticulocyte | HeLa | |
|---|---|---|---|
| Yield | High | Low | Medium-high |
| Protein modifications | None | Limited glycosylation | Glycosylation and phosphorylation |
| Recommended for high MW proteins | No | No | Yes |
| Produces functional proteins | Possible | Possible | Yes |
| Comments | Robust system | Flexible system | Higher protein yield per reaction |
| Learn more | Learn more | Learn more |
Featured cell-free protein expression products
Efficiently translate in vitro-synthesized transcripts, poly(A) RNA, and total RNA, including difficult-to-translate RNAs with high protein yield, biological activity, and consistent performance.
For Research Use Only. Not for use in diagnostic procedures.