Rapid expression of recombinant proteins

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, CHO, 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- and CHO cell line–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 CHO
Yield High Low Medium-high High
Protein modifications None Limited glycosylation Glycosylation and phosphorylation Glycosylation and phosphorylation
Recommended for high MW proteins No No Yes Yes
Produces functional proteins Possible Possible Yes Yes
Comments Robust system Flexible system Higher protein yield per reaction Most economical cost per milligram produced
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Featured cell-free protein expression products

NEW—Express your gene of interest in a CHO lysate to determine how well the insert will translate in CHO cells.

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.