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  pTriEx™-1.1 DNA
Cat. No. 70840  
All Categories » Novagen » Protein Expression, Purification, and Detection » Protein Expression » Multisystem Expression » pTriEx™ Multisystem Expression Vectors
pTriEx™ Multisystem Expression Vectors
One construct for efficient expression in bacterial, insect and mammalian systems
 

Target genes are often expressed in more than one system for various purposes. For example, a bacterial system may be used for initial studies to ascertain solubility or activity, or to produce large amounts of protein for structural studies or antibody production. The same gene may need to be expressed in insect and/or mammalian cells, to obtain higher activity or eukaryotic post-translational modifications. Although Novagen bacterial and baculovirus expression vectors offer compatible cloning strategies and restriction sites to make the cloning process more convenient, the entire process can be streamlined by using a single vector to reliably express target genes in the three major expression systems. The benefits of such a multisystem vector are enhanced when performing high-throughput (HT) gene analysis, which currently require a significant effort to construct and manage all of the multiple recombinants used for different expression systems.

To address this need, Novagen developed the pTriEx™ System, a novel expression vector platform that enables optimal protein expression in bacterial, insect, and mammalian cells from a single plasmid. 

 
Product Description

The pTriEx™-1.1 vector1 is uniquely designed to allow rapid characterization of target genes in multiple expression systems. With this vector a single recombinant plasmid can be used to test expression in E. coli, insect and vertebrate cells. Transient vertebrate expression is mediated by a hybrid promoter composed of the CMV immediate early enhancer fused to the chicken b-actin promoter. For expression in insect cells, pTriEx-1.1 contains flanking baculovirus sequences to permit the generation of recombinant baculoviruses using the BacVector™ System. In baculovirus-infected insect cells, expression is driven by the very late p10 promoter. Expression in E. coli is regulated by the tightly controlled T7lac promoter. Expression can be induced in hosts such as NovaBlue by infecting with lCE6, a phage that constitutively expresses T7 RNA polymerase from the lpL and l>pI promoters. Alternatively, pTriEx recombinant plasmids can be transferred into a (DE3)pLacI host that allows IPTG based induction.
1 patent pending
Note- this product is not available in Japan  

Need additional information about this product? Email our Technical Service department at: novatech@novagen.com

 Related information for this product is available:

EMD Chemicals Inc. list price is displayed (pricing with local distributors may vary). NOTE: In Stock status is based on item availability worldwide.

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70840-320 µgYN/A

EMD Chemicals Inc. list price is displayed (pricing with local distributors may vary). NOTE: In Stock status is based on item availability worldwide.

Product Name
Cat. No.
Size
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pTriEx™-3 DNA70823-320 µgYN/A
pTriEx™-4 DNA70824-320 µgYN/A
pTriEx™-2 DNA70826-320 µgYN/A

Available Separately:
69825: NovaBlue Competent Cells
70526: Clonables™ Ligation/Transformation Kit
70846: TriEx™UP Primer
70847: TriEx™DOWN Primer

Related Literature:

Insect Cell Expression

Material Safety Data Sheets:
70840: pTriEx™-1.1 DNA - English
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Related Categories:
All Categories » Novagen » Protein Expression, Purification, and Detection » Protein Expression » Multisystem Expression » pTriEx™ Multisystem Expression Vectors
All Categories » Novagen » Protein Expression, Purification, and Detection » Protein Expression » Insect Cell Expression » Baculovirus Transfer Plasmids
All Categories » Novagen » Protein Expression, Purification, and Detection » Protein Expression » Multisystem Expression » pTriEx™ Multisystem Expression Vectors » pTriEx™ Multisystem Expression Vectors
All Categories » Novagen » Vectors » Plasmid » pTriEx

Selected Citations:
  1. Ying Cao, et al. (2008) The osterix transcription factor down-regulates interleukin-1α expression in mouse osteosarcoma cells. Molecular Cancer Research 6, 119-126.
  2. Caterina Grillo, et al. (2007) DNA-binding activity of the ERp57 C-terminal domain is related to a redox-dependent conformational change. Journal of Biological Chemistry 282, 10299-10310.
  3. Costin I. Popescu, et al. (2006) Productive folding of tyrosinase ectodomain is controlled by the transmembrane anchor. Journal of Biological Chemistry 281, 21682-21689.
  4. Ying Cao, et al. (2005) Osterix, a transcription factor for osteoblast differentiation, mediates antitumor activity in murine osteosarcoma. Cancer Research 65, 1124-1128.
  5. Costin I. Popescu, et al. (2005) Soluble tyrosinase is an ER- associated degradation substrate retained in the ER by calreticulin and BIP and not calnexin. Journal of Biological Chemistry 280, 13833-13840.
  6. Norica Branza-Nichita, et al. (2004) Role of N-glycan trimming in the folding and secretion of the pestivirus protein erns. Biochemical and Biophysical Research Communications 319, 655–662.
  7. Torsten Wurm, et al. (2001) Localization to the nucleolus Is a common feature of coronavirus nucleoproteins, and the protein may disrupt host cell division. Journal of Virology 75, 9345-9356.