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69026 T7•Tag® Antibody Agarose

T7•Tag® Antibody Agarose : FDS (Fiches de données de sécurité), certificats d’analyse (CoA) et de qualité (CoQ), dossiers, brochures et autres documents disponibles.
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69026
  
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      Aperçu

      Replacement Information
      Description
      OverviewThe T7•Tag® Antibody Agarose is designed for rapid immunoaffinity purification of target proteins that carry the T7•Tag sequence (i.e., the amino terminal 11 aa of the T7 gene 10 protein). Purification is based on binding target proteins to T7•Tag monoclonal antibody that is covalently coupled to cross-linked agarose beads, washing away unbound proteins, and eluting at pH 2.2. Capacity will vary somewhat between different target proteins, but the beads are standardized to bind a minimum of 300 µg T7•Tag β-galactosidase per milliliter of settled resin. The beads can be used in either batch or column methods and can be recycled a minimum of five times without loss of binding activity.
      Catalogue Number69026
      Brand Family Novagen®
      References
      Product Information
      Quality LevelMQ400
      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 Blue Ice Only
      Toxicity Standard Handling
      Storage +2°C to +8°C
      Do not freeze Yes
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Référence GTIN
      69026 0

      Documentation

      T7•Tag® Antibody Agarose FDS

      Titre

      Fiche de données de sécurité des matériaux (FDS) 

      T7•Tag® Antibody Agarose Certificats d'analyse

      TitreNuméro de lot
      69026

      Citations

      Titre
    • Hiroko Hayakawa, et al. (2007) Soluble ST2 blocks interleukin-33 signaling in allergic airway inflammation. Journal of Biological Chemistry 282, 26369-26380.
    • Neelima Sukumar, et al. (2007) Differential Bvg phase-dependent regulation and combinatorial role in pathogenesis of two Bordetella paralogs, BipA and BcfA. Journal of Bacteriology 189, 3695-3704.
    • Andrew J. Leger, et al. (2006) Blocking the protease-activated receptor 1-4 heterodimer in platelet-mediated thrombosis. Circulation 113, 1244-1254.
    • Peter T. Beernink, et al. (2005) Specificity of protein interactions mediated by BRCT domains of the XRCC1 DNA repair protein. Journal of Biological Chemistry 280, 30206-30213.
    • Steven A. Jacobs, et al. (2005) Soluble domains of telomerase reverse transcriptase identified by high-throughput screening. Protein Science 14, 2051-2058.
    • Arlene E. Kray, et al. (2005) Positive regulation of IB kinase signaling by protein serine/threonine phosphatase 2A. Journal of Biological Chemistry 280, 35974-35982.
    • Taruho S. Kuroda and Mitsunori Fukuda. (2005) Functional analysis of Slac2-c/MyRIP as a linker protein between melanosomes and myosin VIIa. Journal of Biological Chemistry 280, 28015-28022.
    • Takamasa Suzuki, et al. (2005) An Arabidopsis protein with a novel calcium-binding repeat sequence interacts with TONSOKU/MGOUN3/BRUSHY1 involved in meristem maintenance. Plant and Cell Physiology 46, 1452-1461.
    • Robert L. Del Vecchio and Nicholas K. Tonks. (2005) The conserved immunoglobulin domain controls the subcellular localization of the homophilic adhesion receptor protein-tyrosine phosphataseμ. Journal of Biological Chemistry 280, 1603-1612.
    • Wolf Wente, et al. (2005) Interactions with PDZ domain proteins PIST/GOPC and PDZK1 regulate intracellular sorting of the somatostatin receptor subtype 5. Journal of Biological Chemistry 280, 32419-32425.
    • Jennifer R. Ball, Christian Dimaano and Katharine S. Ullman. (2004) The RNA binding domain within the nucleoporin Nup153 associates preferentially with single-stranded RNA. RNA 10, 19-27.
    • Mitsunori Fukuda and Taruho S. Kuroda. (2004) Missense mutations in the globular tail of myosin-Va in dilute mice partially impair binding of Slac2-a/melanophilin. Journal of Cell Science 117, 583-591.
    • Michael H. Kagey, Tiffany A. Melhuish and David Wotton. (2003) The polycomb protein Pc2 is a SUMO E3. Cell 113, 127-137.
    • Taruho S. Kuroda, Hiroyoshi Ariga and Mitsunori Fukuda. (2003) The actin-binding domain of Slac2-a/melanophilin is required for melanosome distribution in melanocytes. Molecular and Cellular Biology 23, 5245-5255.
    • Emily Bernstein, et al. (2001) Role for bidentate ribonuclease in the initiation step of RNA interference. 409, 363-366.
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      Protocoles Utilisateur

      Titre
      TB125 T7•Tag® Affinity Purification Kit