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Creative Biolabs can provide high-quality Mempro™ rabbit reticulocyte lysate-based cell-free protein production services.
Cell-free protein production based on crude rabbit reticulocyte lysate (RRL) was originally applied for deciphering the genetic code. Nowadays, RRL has been used widely to explicate the mechanisms of translation, post‑translational modifications, and cotranslational modifications of mammalian proteins. RRL can be used for producing membrane proteins to perform interaction, evolution and protein selection studies from DNA or mRNA libraries either in microarray, display or in vitro expression cloning (IVEC) technologies (Figure 1). Thus, the cell-free protein production in rabbit reticulocyte lysate is an attractive tool for structural biology, functional genomics, drug screening, and vaccine production.
Figure 1. The strategy of in vitro expression cloning using RRL. (Cell-Free Expression, 2007)
Creative Biolabs can provide protein research using Mempro™ cell-free protein production in rabbit reticulocyte lysate. Recent advances in cell-free protein production have significantly extended their application, specifically for large-scale protein production, overcoming many obstacles associated with protein production in mammalian cell culture. Mempro™ cell-free protein production in rabbit reticulocyte lysate allows the production of toxic proteins, membrane proteins with low solubility, incorporation of unnatural or stable isotope-labeled amino acids, on-chip protein synthesis, and synthesis of pharmaceutical polypeptides. In addition, we can provide custom serivces for protein folding and post-translational studies using Mempro™ cell-free protein production in rabbit reticulocyte lysate.
Mempro™ cell-free protein production in rabbit reticulocyte lysate has several significant advantages, including：
However, there are some disadvantages of Mempro™ protein production in rabbit reticulocyte lysate: 1).
However, one of the limitations of this system is its low protein yield. Possible ways to enhance protein production in this system include the addition of factors that up-regulate translation.
Inclusion of recombinant virus proteins and specific viral structures on target mRNA could enhance protein production in RRL. It has been reported that simultaneous addition of influenza A virus NS1 protein and inclusion of the encephalomyocarditis virus (EMCV) internal ribosome entry site (IRES) in the target mRNA facilitate translation initiation and increase protein yield over 10-fold, improving the translation capacity of RRL.
M. Arduengo, et al. (2007). The role of cell‑free rabbit reticulocyte expression systems in functional proteomics. Cell.
M. Anastasina, et al. (2014). A technique to increase protein yield in a rabbit reticulocyte lysate translation system. Biotechniques, 56(1): 36-39
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