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70564 pET GST Fusion System 42

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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 Expression System 42
      The pET-41a-c(+) and pET-42a-c(+) vectors incorporate the schistosomal glutathione-S-transferase (GST; GST•Tag) coding sequence as a fusion partner. The GST•Tag sequence has been reported to enhance the production and in some cases the solubility of its fusion partners (Smith 1998). When expressed in a soluble, properly folded form, GST•Tag fusion proteins can be purified with immobilized glutathione. Gentle elution is achieved with buffers containing reduced glutathione. Quantification of soluble GST fusions is also possible by assaying the transferase activity. The pET-41 and -42 series feature the powerful T7lac promoter, and encode the GST•Tag (220 aa) sequence, proteolytic sites, His•Tag (6 aa) sequence, and S•Tag (15 aa) sequence.

      In contrast to other commercially available GST-fusion vectors, the Xa (IleGluGlyArg, pET-42 series) and enterokinase (AspAspAspAspLys, pET-41 series) proteolytic cleavage sites have been engineered to allow removal of 100% of the vector-encoded sequences and the generation of native proteins with their authentic N-terminal residues. Unfused proteins can be produced by using the Nde I cloning site. A version of pET-41 is available as a linearized vector prepared for ligation-independent cloning (LIC) of PCR products.

      Another pET vector with the GST•Tag sequence is pET-49b(+). Please see the website description for more information. The His•Tag and S•Tag sequences enable alternative protein detection and purification procedures to be performed. For example, when enhancing purity with a separate purification method, or when purifying under denaturing conditions.

      Commercial use of this Product requires a commercial license from EMD Millipore Corporation. Commercial use shall include but not be limited to (1) use of the Product or its components in manufacturing; (2) use of the Product or its components to provide a service, information, or data to others in exchange for consideration; (3) use of the Product or its components (or any derivatives thereof) for therapeutic, diagnostic or prophylactic purposes (including as part of a device, chip, assay or other product); or (4) resale of the Product or its components, whether or not such Product or its components are resold for use in research. Nothing contained herein shall be deemed to represent or warrant that additional third party rights are not required for use of this Product.
      Catalogue Number70564
      Brand Family Novagen®

      Smith, D.B. and Johnson, K.S. 1988. Gene 67, 31.

      Product Information
      Fusion tagHis•Tag, GST•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
      Avoid freeze/thaw Avoid freeze/thaw
      Do not freeze Ok to freeze
      Packaging Information
      Transport Information
      Supplemental Information


      pET GST Fusion System 42 Certificates of Analysis

      TitleLot Number


      Reference overview

      Smith, D.B. and Johnson, K.S. 1988. Gene 67, 31.


    • F. Allemand, et al. (2007) Escherichia coli ribosomal protein L20 binds as a single monomer to its own mRNA bearing two potential binding sites. Nucleic Acids Research 35, 3016-3031.
    • Rutilio A. Fratti, et al. (2007) Stringent 3Q·1R composition of the SNARE 0-layer can be bypassed for fusion by compensatory SNARE mutation or by lipid bilayer modification. Journal of Biological Chemistry 282, 14861-14867.
    • Jeffrey G. Gardner, et al. (2006) Control of acetyl-coenzyme A synthetase (acsA) activity by acetylation/deacetylation without NAD+ involvement in Bacillus subtilis. Journal of Bacteriology 188, 5460-5468.
    • Ganna Panasyuk, et al. (2006) Nuclear export of S6K1 II is regulated by protein kinase CK2 phosphorylation at ser 17. Journal of Biological Chemistry 281, 31188-31201.
    • Shawn F. Bairstow, Kun Ling and Richard A. Anderson. (2005) Phosphatidylinositol phosphate kinase type I directly associates with and regulates Shp-1 tyrosine phosphatase. Journal of Biological Chemistry 280, 23884-23891.
    • Jian Cui, et al. (2005) Identification of a specific domain responsible for JNK2α2 autophosphorylation. Journal of Biological Chemistry 280, 9913-9920.
    • Karthikeyan Kandasamy, et al. (2005) Translational control of 2-adrenergic receptor mRNA by T-cell-restricted intracellular antigen-related protein. Journal of Biological Chemistry 280, 1931-1943.
    • M. Teresa Marques Novo, et al. (2005) A complete approach for recombinant protein expression training: from gene cloning to assessment of protein functionality. Biochemical Education 33, 34-40.
    • Ken Okada and Toshiharu Hase. (2005) Cyanobacterial non-mevalonate pathway: (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase interacts with ferredoxin in Thermosynechococcus elongatus BP-1. Journal of Biological Chemistry 280, 60672-20679.
    • Irene Soderhall, et al. (2005) An ancient role for a prokineticin domain in invertebrate hematopoiesis. journal of Immunology 174, 6153-6160.
    • Shuo Wei, et al. (2005) Reactive site mutations in tissue inhibitor of metalloproteinase-3 disrupt inhibition of matrix metalloproteinases but not TNF-α-converting enzyme. Journal of Biological Chemistry 280, 32877-32882.
    • Junji Yamauchi, et al. (2005) The neurotrophin-3 receptor TrkC directly phosphorylates and activates the nucleotide exchange factor Dbs to enhance Schwann cell migration. Proceedings of the National Academy of Sciences (USA) 102, 5198-5203.
    • Brian A. Zabel, Amanda M. Silverio and Eugene C. Butcher. (2005) Chemokine-like receptor 1 expression and chemerin-directed chemotaxis distinguish plasmacytoid from myeloid dendritic cells in human blood. Journal of Immunology 174, 244-251.
    • Jacob Nielsen, et al. (2004) Sequential dimerization of human zipcode-binding protein IMP1 on RNA: a cooperative mechanism providing RNP stability. Nucleic Acids Research 32, 4368-4376.
    • User Protocols

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

      Vector Map

      TB240VM pET-42a-c(+) Vector Map

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      Life Science Research > Genomic Analysis > Transfection and Protein Expression > Bacterial Expression > Bacterial Expression Vectors