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70942 pET NusA Fusion System 43.1 - Novagen

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      This product has been discontinued.

      pET Expression Systems and pET
      pET Expression Systems and pET Expression Systems plus Competent Cells provide core reagents needed for target gene cloning and expression.

      Components: pET Expression Systems
      Components for pET Expression Systems are similar for all systems unless otherwise stated with the specific pET Expression System description. pET Expression Systems include:
      • 10 µg pET vector DNA (for each indicated plasmid)
      • 0.2 ml BL21 Glycerol Stock
      • 0.2 ml BL21(DE3) Glycerol Stock
      • 0.2 ml BL21(DE3)pLysS Glycerol Stock
      • 0.2 ml Induction Control Glycerol Stock

      Components: pET Expression Systems plus Competent Cells
      pET Expression Systems plus Competent Cells contain all of the components of the specific pET Expression System, as well as the following additional components, unless otherwise stated with the specific pET Expression System description:
      • 0.2 ml NovaBlue Competent Cells
      • 0.2 ml BL21(DE3) Competent Cells
      • 0.2 ml BL21(DE3)pLysS Competent Cells
      • 2 × 0.2 ml SOC Medium
      • 10 µl Test Plasmid

      These components are sufficient for up to 10 transformations in each host.

      Purification and Detection Reagents
      Purification and detection reagents are available separately. For complete product descriptions and ordering information, refer to the Protein Purification and Antibodies, Conjugates & Detection Tools chapters.

      pET NusA Fusion System 43.1
      The pET NusA Fusion Systems are designed for cloning and high-level expression of polypeptide sequences fused with the 495-aa NusA (Nus•Tag) protein. The NusA protein has been identified as having the highest potential for solubility when a database of more than 4000 E. coli proteins was subjected to solubility modeling (Harrison 2000, Davis 1998). Greater than 85% of the expressed protein was soluble in tests with each of four different NusA fusion proteins (Harrison 2000).

      Another pET vector with the Nus•Tag sequence is pET-50b(+) (Cat. No. 71471-3). The pET-43.1 vectors incorporate the Nus•Tag fusion partner and are also compatible with the trxB/gor mutant Origami, Origami 2, Origami B, Rosetta-gami, Rosetta-gami 2, and Rosetta-gami B strains, which facilitatedisulfide bond formation in the cytoplasm (Davis 1998). Disulfide-bonded proteins maybe obtained by employing the combination of a pET-43.1 or pET-44 vector and these trxB/gor host strains. Unfused proteins can be produced by using the Nde I cloning site.

      This product is covered under license from Brookhaven National Labs. Commercial entities need to obtain a research use license prior to purchase. Please contact your licensing department to confirm that your company already holds a research use license.

      Catalogue Number70942
      Brand Family Novagen®

      Harrison, R.G. 2000. inNovations 11, 4. Davis, G.D., et al. 1999. Biotechnol. Bioeng. 65, 382. Novy, R. and Drott, D. 2002. inNovations 14, 12.

      Product Information
      Fusion tagHis•Tag, HSV•Tag, Nus•Tag, S•Tag
      Biological Information
      Physicochemical Information
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Storage and Shipping Information
      Ship Code Shipped with Blue Ice or with Dry Ice
      Toxicity Standard Handling
      Storage ≤ -70°C
      Do not freeze Ok to freeze
      Packaging Information
      Transport Information
      Supplemental Information


      pET NusA Fusion System 43.1 - Novagen Certificates of Analysis

      TitleLot Number


      Reference overview

      Harrison, R.G. 2000. inNovations 11, 4. Davis, G.D., et al. 1999. Biotechnol. Bioeng. 65, 382. Novy, R. and Drott, D. 2002. inNovations 14, 12.


    • Kenneth Segers, et al. (2007) Design of protein-membrane interaction inhibitors by virtual ligand screening, proof of concept with the C2 domain of factor V. Procedings of the National Academy of Science 104, 12697-12702.
    • Mahmoud Reza Banki, Tillman U. Gerngross and David W. Wood. (2005) Novel and economical purification of recombinant proteins: Intein-mediated protein purification using in vivo polyhydroxybutyrate (PHB) matrix association. Protein Science 14, 1387-1395.
    • Ju-Ock Nam, et al. (2005) Regulation of tumor angiogenesis by fastatin, the fourth FAS1 domain of β-ig-h3, via α-v-β-3 integrin. Cancer Research 65, 4153-4161.
    • Aymeric Goyer, et al. (2004) Characterization and metabolic function of a peroxisomalsarcosine and pipecolate oxidase from Arabidopsis. Journal of Biological Chemistry 279, 16947-16953.
    • Valeria De Marco, et al. (2004) The solubility and stability of recombinant proteins are increased by their fusions to NusA. Biochimica et Biophysica Acta 322, 766-771.
    • Deanne M. Compaan and W. Ross Ellington. (2003) Functional consequences of a gene duplication and fusion event in an arginine kinase. 206, 1545-1556.
    • Ramin Nazarian, Juan M. Falcon-Perez and Esteban C. Dell'Angelica. (2003) Biogenesis of lysozyme-related organelles complex 3 (BLOC-3): a complex containing the Hermansky- Pudlak syndrome (HPS) proteins HPS1 and HPS4. Procedings of the National Academy of Science 100, 8770-8775.
    • Lei Zheng, Ulrich Baumann and Jean-Louis Reymond. (2003) Production of a functional catalytic antibody ScFv-NusA fusion protein in bacterial cytoplasm. Journal of Biochemistry (Tokyo) 133, 577-581.
    • User Protocols

      TB053 Academic and Non-profit Laboratory Assurance Letter
      TB055 pET System Manual

      Vector Map

      TB288VM pET-43.1a-c(+) Vector Map

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