A rapid method for gene expression analysis, PURExpress® is a novel cell-free transcription/translation system reconstituted from the purified components necessary for E. coli translation.
PURExpress® is a registered trademark of New England Biolabs, Inc.
- Protein Synthesis Reaction using PURExpress (E3313)
- Protein Synthesis Reaction using PURExpress (E6800)
- Protein Synthesis Reaction using PURExpress® ∆ (aa, tRNA) Kit (E6840)
- Measurement of 35S-Methionine Incorporation by TCA Precipitation and Yield Determination using PURExpress
- Purification of Synthesized Protein using Reverse His-tag Purification
- PURExpress Disulfide Bond Enhancer (E6820)
- Determination of Protein Synthesis Yield with PURExpress (E6800)
- Determination of Protein Synthesis Yield with PURExpress (E3313)
- Determination of Protein Synthesis Yield with PURExpress (E6840)
- Analysis of Synthesized Protein using PURExpress (E6800)
- Analysis of Synthesized Protein using PURExpress (E3313)
- Analysis of Synthesized Protein using PURExpress (E6840)
- Determination of Protein Synthesis Yield with PURExpress (E6850)
- Analysis of Synthesized Protein using PURExpress (E6850)
- Protein Synthesis Reaction using PURExpress® ∆ RF123 Kit (E6850)
- Protocol for Avoiding Rnase Contamination using Murine Rnase Inhibitor (M0314)
- Poly(A) Tailing of RNA using E. coli Poly(A) Polymerase (NEB# M0276)
- Use of the PURExpress® in vitro Protein Synthesis Kit, Disulfide Bond Enhancer and SHuffle® Competent E. coli for heterologous in vitro and in vivo cellulase expression.
- Using the PURExpress® In Vitro Protein Synthesis Kit for Heterologous In Vitro Expression and Functional Screening of FMN-dependent Oxidoreductase Variants
The Future of Cell-Free Protein Synthesis
Cell-free protein synthesis has the potential to become one of the most important high throughput technologies for functional genomics and proteomics.
Avoid Common Obstacles in Protein Expression
Read how to avoid common obstacles in protein expression that prevent interactions with cellular machinery.
Protein Expression & Purification Brochure
The Protein Expression and Purification brochure provides information on the advanced tools for protein expression and purification offered by NEB.
- Protein Expression and Purification Selection Chart
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- Feng, Z., et al. 2011. Optimization of Medium Composition for Production of Recombinant Calf Chymosin from Kluyveromyces lactis in Submerged Fermentation J. of Northeast Agricultural University. 18, PubMedID: , DOI:
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- Panayiotou, C., Solaroli, N., Xu, Y., Johansson, M. and Karlsson, A. 2011. The characterization of human adenylate kinases 7 and 8 demonstrates differences in kinetic parameters and structural organization among the family of adenylate kinase isoenzymes Biochem J. . 2433 , PubMedID: 21080915, DOI:
- Lamichhane, T.N., Abeydeera, N.D., Duc, A.C., Cunningham, P.R. and Chow, C.S 2011. Selection of peptides targeting helix 31 of bacterial 16S ribosomal RNA by screening M13 phage-display libraries Molecules . 16, PubMedID: 21278676, DOI:
- Rosner, K., Kasprzak, M.F., Horenstein, A.C., Thurston, H.L., Abrams, J., Kerwin, L.Y., Mehregan, D.A. and Mehregan, D.R. 2011. Engineering a waste management enzyme to overcome cancer resistance to apoptosis: adding DNase1 to the anti-cancer toolbox Cancer Gene Ther. . 18, PubMedID: 21233855, DOI:
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- Shimizu, Y. and Ueda, T. 2006. SmpB triggers GTP hydrolysis of elongation factor Tu on ribosome by compensating for the lack of codon-anticodon interaction during trans-translation initiation J. Biol. Chem.. 281, PubMedID: 16601123, DOI:
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- Ying, B.W., Taguchi, H., Kondo, M. and Ueda, T. 2005. Co-translational involvement of the chaperonin GroEL in the folding of newly translated polypeptides J. Biol. Chem.. 280, PubMedID: 15664980, DOI:
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- Theerthagiri, G., Eisenhardt, N., Schwarz, H. and Antonin, W. 2010. The nucleoporin Nup188 controls passage of membrane proteins across the nuclear pore complex J. Cell Biol. . 189, PubMedID: 20566687, DOI:
- Noto, T., Kurth, H., Kataoka, K., Aronica, L., DeSouza, L., Siu, K., Pearlman, R., Gorovsky, M. and Mochizuki, K. 2010. The tetrahymena argonaute-binding protein Giw1p directs a mature argonaute-siRNA complex to the nucleus Cell . 140 , PubMedID: 20211138, DOI:
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- His-Tagged Translation Factors
- Initiation Factors (IF1, IF2, IF3)
- Elongation Factors (EF-Tu, EF-Ts, EF-G)
- Release Factors (RF1, RF2, RF3)
- Ribosome Recycling Factor
- 20 Aminoacyl tRNA synthetases
- Methionyl tRNA formyltransferase
- E. coli Ribosomes
- E. coli tRNAs
- Energy Regeneration System
- NTPs, Amino Acids, Salts, Buffer
In addition, recombinant T7 RNA polymerase is used to couple transcription to translation. The PURE system represents an important step towards a totally defined in vitro transcription/translation system, thus avoiding the “black box” nature of the cell extract-based systems.
While NEB develops and validates its products for various applications, the use of this product may require the buyer to obtain additional third party intellectual property rights for certain applications.
For more information about commercial rights, please contact NEB's Global Business Development team at [email protected].
This product is intended for research purposes only. This product is not intended to be used for therapeutic or diagnostic purposes in humans or animals.
NEB has a long history in recombinant protein expression and has developed a wide array of solutions for proteins that are difficult to express.