69405 pET Expression System 11 - Novagen

69405
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      Overview

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      69405-3
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          Description
          OverviewpET 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 11
          The pET Expression System 11 contains 10 µg each of the four versions of pET-11 (pET-11a–d). The pET-11a-d vectors carry an N-terminal T7•Tag® sequence and BamH I cloning site. These vectors are the precursors to many pET family vectors; the pET-21a-d(+) series corresponds to pET-11a-d but incorporates several additional features. Note that the sequence is numbered by the pBR322 convention, so the T7 expression region is reversed on the vector map, TB042VM. The pET-3, 9, and 11 vector series are original, basic pET plasmids constructed by Studier and colleagues (Studier 1990) and are the precursors of the subsequent pET vectors. These vectors offer a single BamH I cloning site in three reading frames for producing proteins fused with a non-cleavable Nterminal T7•Tag® epitope. Unfused proteins can be produced by using the Nde I cloning site in the "a", "b", and "c" versions, or the Nco I site in the "d" version. The pET-17b vector carries a multiple cloning site in oneframe.






          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.
          This product contains genetically modified organisms (GMO). Within the EU GMOs are regulated by Directives 2001/18/EC and 2009/41/EC of the European Parliament and of the Council and their national implementation in the member States respectively. This legislation obliges MilliporeSigma to request certain information about you and the establishment where the GMOs are being handled. Click here for Enduser Declaration (EUD) Form.
          Catalogue Number69405
          Brand Family Novagen®
          References
          Product Information
          Components
          Fusion tagT7•Tag
          Applications
          Biological Information
          Physicochemical Information
          Dimensions
          Materials Information
          Toxicological Information
          Safety Information according to GHS
          Safety Information
          Product Usage Statements
          Storage and Shipping Information
          Ship Code Dry Ice Only
          Toxicity Standard Handling
          Storage ≤ -70°C
          Avoid freeze/thaw Avoid freeze/thaw
          Do not freeze Ok to freeze
          Packaging Information
          Transport Information
          Supplemental Information
          Specifications

          Documentation

          pET Expression System 11 - Novagen SDS

          Title

          Safety Data Sheet (SDS) 

          pET Expression System 11 - Novagen Certificates of Analysis

          TitleLot Number
          69405

          Citations

          Title
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        • Jessica C. Greene, et al. (2005) Genetic and genomic studies of Drosophila parkin mutants implicate oxidative stress and innate immune responses in pathogenesis. Human Molecular Genetics 14, 799-811.
        • Noriko Handa, et al. (2005) Crystal structure of a novel polyisoprenoid-binding protein from Thermus thermophilus HB8. Protein Science 14, 1004-1010.
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        • Frank Hillger, et al. (2005) Biophysical comparison of BMP-2, ProBMP-2, and the free pro-peptide reveals stabilization of the pro-peptide by the mature growth factor. Journal of Biological Chemistry 280, 14974-14980.
        • Mette Praetorius Ibba, et al. (2005) Association between archaeal prolyl-and leucyl-tRNA synthetases enhances tRNAPro aminoacylation. Journal of Biological Chemistry 280, 26099-26104.
        • Eva Johansson, et al. (2005) Structures of dCTP deaminase from Escherichia coli with bound substrate and product: reaction mechanism and determinants of mono- and bifunctionality for a family of enzymes. Journal of Biological Chemistry 280, 3051-3059.
        • Peter A. Lemaire, Jeffrey Lary and James L. Cole. (2005) Mechanism of PKR activation: dimerization and kinase activation in the absence of double-stranded RNA. Journal of Molecular Biology 345, 81-90.
        • Mette Praetorius-Ibba, et al. (2005) Association between archaeal prolyl- and leucyl-tRNA synthetases enhances tRNApro aminoacylation. Journal of Biological Chemistry 280, 26099-26104.
        • Rongde Qiu, et al. (2005) Identification of the putative staphylococcal AgrB catalytic residues involving in the proteolytic cleavage of AgrD to generate autoinducing peptide. Journal of Biological Chemistry 280, 16695-16704.
        • Ok Hee Ryu, et al. (2005) Proteolysis of MIP-1α isoforms LD78β and LD78α by neutrophil-derived serine proteases. Journal of Biological Chemistry 280, 17415-17421.
        • D. Andrew Skaff, et al. (2005) Glucose 6-phosphate release of wild-type and mutant human brain hexokinases from mitochondria. Journal of Biological Chemistry 280, 38403-38409.
        • Wayne W. Chan, Steven L. Roderick and David E. Cohen. (2002) Human phosphatidylcholine transfer protein: purification, crystallization and preliminary X-ray diffraction data. Biochimica et Biophysica Acta 1596, 1-5.
        • Angelina J. Lay, et al. (2000) Phosphoglycerate kinase acts in tumor angiogenesis as a disulphide reductase. 408, 869-873.
        • Jianyuan Luo, et al. (2000) Deactylation of p53 modul;ates its effect on cell growth and apoptosis. 408, 377-381.
        • G.L. Conn, et al. (1999) Crystal structure of a conserved ribosomal protein-RNA complex. Science 284, 1171-1174.
        • Trudy H. Grossman, et al. (1998) Spontaneous cAMP-dependent derepression of gene expression in stationary phase plays a role in recombinant expression instability. Gene 209, 95-103.
        • C. C. Hu, et al. (1997) Cloning, characterization, and heterologous expression of exon-4-containing amelogenin mRNAs. Journal of Dental Research 76, 641-647.
        • Ren Zhang, JiaJu Zhao and James D. Potter. (1995) Phosphorylation of both serine residues in cardiac troponin I is required to decrease the Ca2+ affinity of cardiac troponin C. Journal of Biological Chemistry 270, 30773-30780.
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        • K.M. Bohren, et al. (1991) Expression of human aldose and aldehyde erductases. Journal of Biological Chemistry 266, 24031-24037.
        • User Protocols

          Title
          TB055 pET System Manual

          Vector Map

          Title
          TB042VM pET-11a-d Vector Map

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