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69415 pET Expression System 9

69415
  
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Áttekintés

Replacement Information
Description
Overview

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 9
The pET Expression System 9 contains 10 µg each of the four versions of pET-9 (pET-9a–d). The pET-9a–d(+) vectors carry an N-terminal T7•Tag® sequence and BamH I cloning site. These vectors are the precursors to many pET family vectors. Note that the sequence is numbered by the pBR322 convention, so the T7 expression region is reversed on the vector map, TB040VM. 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.
Catalogue Number69415
Brand Family Novagen®
References
References

Studier, F.W., et al. 1990. Meth. Enzymol. 185, 60. Seed, B. 1987. Nature 329, 840.

Product Information
10 µg eachpET-9a-d vector DNA
0.2 mlHost bacterial strains BL21, BL21(DE3), and BL21(DE3)pLysS, glycerol stocks
0.2 mlInduction control clone, glycerol stock
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 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
Specifications
Global Trade Item Number
Katalógusszám GTIN
69415 0

Documentation

pET Expression System 9 Certificates of Analysis

TitleLot Number
69415

References

Hivatkozások áttekintése

Studier, F.W., et al. 1990. Meth. Enzymol. 185, 60. Seed, B. 1987. Nature 329, 840.

Citations

Titulus
  • Susanne Eschenburg, et al. (2005) A novel inhibitor that suspends the induced fit mechanism of UDP-N-acetylglucosamine enolpyruvyl transferase (MurA). Journal of Biological Chemistry 280, 14070-14075.
  • Agnes E. Hamburger, et al. (2005) Steric accessibility of the HIV-1 gp41 N-trimer region. Journal of Biological Chemistry 280, 12567-12572.
  • JuHyun Kim, et al. (2005) Adenylate kinase of Escherichia coli, a component of the phage T4 dNTP synthetase complex. Journal of Biological Chemistry 280, 28221-28229.
  • Rongkun Shen, et al. (2004) Escherichia coli nucleoside diphosphate kinase interactions with T4 phage proteins of deoxyribonucleotide synthesis and possible regulatory functions. Journal of Biological Chemistry 279, 32225-32232.
  • Ken-Shwo Dai and Choong-Chin Liew. (2001) A novel human striated muscle RING zinc finger protein, SMRZ, interacts with SMT3b via Its RING domain. Journal of Biological Chemistry 276, 23992-23999.
  • Maria D. Koffa, et al. (2001) Herpes simplex virus ICP27 protein provides viral mRNAs with access to the cellular mRNA export pathway. European Molecular Biology Organization Journal 20, 5769-5778.
  • Brian J. Hoffman, et al. (1995) Lactose fed-batch overexpression of recombinant metalloproteins in Escherichia coli BL21(DE3): process control yielding high levels of metal-incorportaed, soluble protein. Protein Expression and Purification 6, 646-654.
  • User Protocols

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

    Vector Map

    Title
    TB040VM pET-9a-d Vector Map

    Kapcsolódó termékek és alkalmazások

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    Kategóriák

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