Introduction
The so-called non-cell protein expression system refers to the expression of protein by using in vitro translation system (such as ribosome display technology) to mimic the protein translation system in cell, at the same time using the well-designed liposome membrane to replace the cell membrane, proteins were inserted on it to maintain the maximum natural conformation and natural activity.
In vitro protein expression is the production of recombinant proteins in solution using biomolecular translation machinery extracted from cells. Because protein synthesis occurs in cell lysates rather than within cultured cells, the method is also called cell-free protein expression. Cell-free protein production can be accomplished with several kinds and species of cell extract, and these approaches have several advantages and features that complement traditional in vivo methods.
Introduction to in vitro protein expression
In vitro protein expression (also known as in vitro translation, cell-free protein expression, cell-free translation, or cell-free protein synthesis) is a technique that enables researchers to rapidly express and manufacture small amounts of functional proteins. Compared to in vivo techniques based on bacterial or tissue culture cells, in vitro protein expression is considerably faster because it does not require gene transfection, cell culture or extensive protein purification.
Although in vitro expression is not practical for commercial large-scale recombinant protein production, it has a variety of features that make it considerably more useful and flexible for many research applications.
The diagram provides an example of the application of a cell-free protein expression method combined with protein mass spectrometry (MS).
Production of cell-free membrane proteins
Advantages
Comparison of various cell-free protein expression systems
System |
Advantages |
Disadvantages |
E. coli |
· Very high protein yield · Relatively tolerant of additives |
· Many eukaryotic proteins insoluble upon expression · Eukaryotic co- and post-translational modifications not possible · Codon usage is different from eukaryotes |
Rabbit |
· Mammalian system · Cap independent translation |
· Sensitive to additives · Protein glycosylation not possible · Co-expression of off-target proteins |
Wheat germ |
· Translation of large proteins possible · Devoid of off-target endogenous mammalian proteins · High protein yield |
· Mammalian co- and post-translational modifications are not possible · Premature termination of products |
Insect |
· Translation of large proteins possible · No endogenous mammalian proteins · Certain forms of protein glycosylation possible |
· Non-mammalian |
Human |
· Human system · Co- and post-translational modifications are possible · Synthesis of functional proteins · Possible to make virus-like particles (VPLs) |
· Sensitive to additives · Lower yields than E. coli · New system |
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Why Leading Biology?
At Leading Biology, we custom protein purification design for every single protein to ensure the production and recovery rate as high as possible.
Working with us, you will get stability, and it means a reliable partner to help streamline your R&D process.
Working with us, you will get the guaranteed service to accommodate your requirements.
- Innovative configurations of chromatography columns custom-tailored to each protein
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- Flexible scale-up protein production
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2 | Acetylation | 776 | Leading Biology | 2020-06-23 |
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