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69026 | T7•Tag® Antibody Agarose

69026
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      Overview

      Replacement Information

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      Catalog NumberAvailability Packaging Qty/Pack Price Quantity
      69026-3
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          Glass bottle 2 ml
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          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
          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

          Documentation

          SDS

          Title

          Safety Data Sheet (SDS) 

          Certificates of Analysis

          TitleLot Number
          69026

          Brochure

          Title
          Protein Purification and Preparation

          Citations

          Title
        • 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.
        • User Protocols

          Title
          TB125 T7•Tag<sup>®</sup> Affinity Purification Kit