Millipore Sigma Vibrant Logo

69409 pET Expression System 3

Classic T7•Tag® pET vectors

pET Expression System 3: Ficha de datos de seguridad (MSDS o SDS), certificado de análisis y de calidad (CoA y CoQ), expedientes, folletos y otros documentos disponibles.
69409
  
Recuperando precio...
No pudo obtenerse el precio
La cantidad mínima tiene que ser múltiplo de
Maximum Quantity is
Al finalizar el pedido Más información
Ahorró ()
 
—
Solicitar precio
—
Disponibilidad a confirmar Disponibilidad a confirmar
Ingrese cantidad 
Suspendido
Cantidades limitadas disponibles
Debe confirmarse disponibilidad
    El resto: se avisará
      El resto: se avisará
      Se avisará
      Póngase en contacto con el Servicio de Atención al Cliente
      Contact Customer Service

       

      Póngase en contacto con el Servicio de Atención al Cliente

      Descripción

      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 3
      The pET Expression System 3 contains 10 µg each of the four pET-3 vectors (pET-3a–c). The pET-3a–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-23a-d(+) series corresponds to pET-3a–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, TB026VM. 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 Number69409
      Brand Family Novagen®
      References
      Product Information
      •10 µg eachpET-3a-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
      Número de referencia GTIN
      69409 0

      Documentation

      pET Expression System 3 Certificados de análisis

      CargoNúmero de lote
      69409

      Citas

      Título
    • Mateen A. Khan, et al. (2008) Potyvirus genome-linked protein, VPg, directly affects wheat germ in vitro translation: interactions with translation initiation factors eIF4F and EIFiso4F. Journal of Biological Chemistry 283, 1340-1349.
    • Amanda Nga-Sze Mak, et al. (2007) Structure-function study of maize ribosome-inactivating protein: implications for the internal inactivation region and the sole glutamate in the active site. Nucleic Acids Research 35, 6259-6267.
    • M. Wang and K. A. Hudak. (2006) A novel interaction of pokeweed antiviral protein with translation initiation factors 4G and iso4G: a potential indirect mechanism to access viral RNAs. Nucleic Acids Research 34, 1174-1181.
    • Line Johnsen, et al. (2005) 1.6 Å crystal structure of EntA-Im: A bacterial immunity protein conferring immunity to the antimicrobial activity of the pediocin-like bacteriocin enterocin A. Journal of Biological Chemistry 280, 19045-19050.
    • Taj Kattapuram, et al. (2005) Protein kinase CK1α regulates mRNA binding by hnRNP-C in response to physiologic levels of hydrogen peroxide. Journal of Biological Chemistry 280, 15340-15347.
    • Fabrice A. C. Klein, et al. (2005) Biochemical and NMR mapping of the interface between CREB-binding protein and ligand binding domains of nuclear receptor: beyond the LXXLL motif. Journal of Biological Chemistry 280, 5682-5692.
    • Orbán Komonyi, et al. (2005) DTL, the Drosophila homolog of PIMT/Tgs1 nuclear receptor coactivator interacting protein/RNA methyltransferase, has an essential role in development. Journal of Biological Chemistry 280, 12397-12404.
    • Astrid Krmpotic, et al. (2005) NK cell activation through the NKG2D ligand MULT-1 is selectively prevented by the glycoprotein encoded by mouse cytomegalovirus gene m145. journal of Experimental Medicine 201, 211-220.
    • James T. Macdonald, et al. (2005) Unfolding crystallins: The destabilizing role of a β-hairpin cysteine in βB2-crystallin by simulation and experiment. Protein Science 14, 1282-1292.
    • Takeki Ogata, et al. (2005) Betacellulin-δ4, a novel differentiation factor for pancreatic β-cells, ameliorates glucose intolerance in streptozotocin-treated rats. Endocrinology 146, 4673-4681.
    • Evelyne Raux-Deery, et al. (2005) Identification and characterization of the terminal enzyme of siroheme biosynthesis from Arabidopsis thaliana: a plastid-located sirohydrochlorin ferrochelatase containing a 2Fe-2S center. Journal of Biological Chemistry 280, (4713- 4721).
    • Barbara Zambelli, et al. (2005) UreG, a chaperone in the urease assembly process, is an intrinsically unstructured GTPase that specifically binds Zn2+. Journal of Biological Chemistry 280, 4684-4695.
    • Yinhong Zhao, et al. (2005) CcbP, a calcium-binding protein from Anabaena sp. PCC 7120, provides evidence that calcium ions regulate heterocyst differentiation. Proceedings of the National Academy of Sciences (USA) 102, 5744-5748.
    • Dan Gu, et al. (2004) Identification and characterization of the DNA-binding domain of the multifunctional PutA flavoenzyme. Journal of Biological Chemistry 279, 31171-31176.
    • Liliya A. Yatsunyk, Benjamin E. Ramirez and Amy C. Rosenzweig. (2004) Yeast Cox17 solution structure and copper(I) binding. Journal of Biological Chemistry 279, 53584-53592.
    • F. Castellani, et al. (2002) Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy. 420, 98-102.
    • Claudia Naumann, Thomas Hartmann and Dietrich Ober. (2002) Evolutionary recruitment of a flavin-dependent monooxygenase for the detoxification of host plant-acquired pyrrolizidine alkaloids in the alkaloid-defended arctiid moth Tyria jacobaeae. Procedings of the National Academy of Science 99, 6085-6090.
    • Luca Pellegrini, et al. (2000) Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin. 407, 1029-1034.
    • Zhiguo Zhang, Kei-ichi Shibahara and Bruce Stillman. (2000) PCNA connects DNA replication to epigenetic inheritance in yeast. 408, 221-2225.
    • Joey M. Studts and Brian G, Fox. (1999) Application of fed-batch fermentation to the preparation of isotopically labeled or selenomethionyl- labeled proteins. Protein Expression and Purification 16, 109-119.
    • Kaare Teilum, Lars Ostergaard and Kearen Welinder. (1999) Disulfide bond formation and folding of plant peroxidases expressed as inclusion body proteins in Escherichia coli thioredoxin reductase negative strains. Protein Expression and Purification 15, 77-82.
    • Michael W. West, et al. (1999) De novo amyloid proteins from designed combinatorial libraries. Procedings of the National Academy of Science 96, 1121111216.
    • O. Mayans, et al. (1998) Structural basis for activation of the titin kinase domain during myofibrillogenesis. 395, 863-869.
    • F.-X. Gomis-Ruth, et al. (1997) Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1. 389, 77-81.
    • R. Koljak, et al. (1997) Identification of a naturally occurring peroxidase-lipooxygenase fusion protein. Science 277, 1994-1996.
    • 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.
    • Weibiao Huang and Erik Bateman. (1995) Cloning, expression, and characterization of the TATA-binding protein (TBP) promoter binding factor, a transcription activator of the Acanthamoeba TBP gene. Journal of Biological Chemistry 270, 28839-28847.
    • Michio Yasunami, et al. (1995) Molecular characterization of cDNA encoding a novel protein related to transcriptional enhancer factor-1 from neural precursor cells. Journal of Biological Chemistry 270, 18649-18654.
    • 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.
    • H. Dorai, et al. (1994) Mammalian cell expression of single-shain Fv (santibody proteins and their C-terminal fusions with interleukin-2 and other effector domains. Bio/Technology 12, 890-897.
    • B.H. Johnson and M.H. Hecht. (1994) Recombinant proteins can be isolated from E. coli cells by repeated cycles of freezing and thawing. Bio/Technology 12, 1357-1360.
    • W. Krek, et al. (1994) Negative regulation of the growth-promoting transcription factor E2F-1 by a stably bound cyclin A-dependent protein kinase. Cell 78, 161-172.
    • P. Neubauer and K. Hofmann. (1994) Efficient use of lactose for the lac promoter-controlled overexpression of the main antigenic protein of the foot and mouth disease virus in Escherichia coli under fed-batch fermentation conditions. FEMS Microbiology Reviews 14, 99-102.
    • P. Neubauer, et al. (1992) Maximizing the expression of a recombinant gene in Escherichia coli by manipulation of induction time using lactose as an inducer. Applied Microbiology and Biotechnology 36, 739-744.
      		•

      Protocolos de usuario

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

      Mapa vectorial

      Cargo
      TB026VM pET-3a-d Vector Map

      Productos y aplicaciones relacionados

      Related Products

      Número de referencia Descripción  
      69405 pET Expression System 11 - Novagen Precios y disponibilidad
      69415 pET Expression System 9 Precios y disponibilidad
      70753 pET Expression System 14b - Novagen Precios y disponibilidad
      70755 pET Expression System 15b - Novagen Precios y disponibilidad
      70757 pET Expression System 16b - Novagen Precios y disponibilidad
      70759 pET Expression System 19b - Novagen Precios y disponibilidad
      70761 pET Expression System 20b - Novagen Precios y disponibilidad
      70763 pET Expression System 21 Precios y disponibilidad
      70765 pET Expression System 22b - Novagen Precios y disponibilidad
      70767 pET Expression System 23 - Novagen Precios y disponibilidad
      Show more

      Productos relacionados por: Application Facete

      Protein Expression

      Categorías

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