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70564 pET GST Fusion System 42

Popular GST fusion tag in advanced pET vectors

pET GST Fusion System 42 MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.
70564
  
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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 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®
References
References

Smith, D.B. and Johnson, K.S. 1988. Gene 67, 31.
Product Information
Components
Fusion tagHis•Tag, GST•Tag, S•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
Katalogové číslo GTIN
70564 0

Documentation

pET GST Fusion System 42 Certificates of Analysis

TitleLot Number
70564

References

Přehled odkazů

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

Citations

Název
  • 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.
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    User Protocols

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

    Vector Map

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