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Glutathione MagBeads

Sep Glutathione Magnetic particles 40 µm
Catalog No. ABIN1574295
  • Application
    Separation (Sep)
    Brand
    MagBeads
    Characteristics
    The Glutathione MagBeads are developed for quick and efficient small-scale purification of recombinant glutathione-S-transferase (GST) fusion proteins from bacteria, yeast and mammalian crude cell lysates. The The Glutathione MagBeads are superparamagnetic beads, average 40 µm in diameter, coupled with reduced glutathione (GSH). The beads are supplied as 25% slurry in phosphate buffered saline (PBS), pH 7.4, containing 20% ethanol. The Glutathione MagBeads has a binding capacity of 5 to 10 mg GST protein per 1 ml settled beads (e.g. 4 ml 25% slurry).
    Key Features:
    Quick and convenient separation accomplished by magnetic force
    High binding capacity with 5 - 10 mg of GST/ml settled beads
    Magbeads can be regenerated for multiple uses
    Extremely low nonspecific binding
    Bead Ligand
    Glutathione
    Bead Matrix
    Magnetic particles
    Bead Size
    40 µm
  • Restrictions
    For Research Use only
  • Format
    Liquid
    Buffer
    25% slurry in phosphate buffered saline (PBS), pH 7.4, containing 20% ethanol.
    Storage
    4 °C
    Storage Comment
    Store at 4°C, do NOT freeze.
  • Sun, Zhou, Zhang, Gallick, Kuang: "Unravelling the pivotal role of Alix in MVB sorting and silencing of the activated EGFR." in: The Biochemical journal, Vol. 466, Issue 3, pp. 475-87, (2015) (PubMed).

    Förthmann, Brinkmann, Ratzka, Stachowiak, Grothe, Claus: "Immobile survival of motoneuron (SMN) protein stored in Cajal bodies can be mobilized by protein interactions." in: Cellular and molecular life sciences : CMLS, Vol. 70, Issue 14, pp. 2555-68, (2013) (PubMed).

    Zhang, Petrov, Hyun, Liu, Gerber, Myers: "The Tlo proteins are stoichiometric components of Candida albicans mediator anchored via the Med3 subunit." in: Eukaryotic cell, Vol. 11, Issue 7, pp. 874-84, (2012) (PubMed).

    Liu, Myers: "Med5(Nut1) and Med17(Srb4) are direct targets of mediator histone H4 tail interactions." in: PLoS ONE, Vol. 7, Issue 6, pp. e38416, (2012) (PubMed).

    Yu, Nie, Cao, Jin, Yan, Wang, Liu, Xiao, Liang, Zhang: "Phosphatidic acid mediates salt stress response by regulation of MPK6 in Arabidopsis thaliana." in: The New phytologist, Vol. 188, Issue 3, pp. 762-73, (2010) (PubMed).

    Min, Cho, Zhou, Schroeder, Haroutunian, Seeley, Huang, Shen, Masliah, Mukherjee, Meyers, Cole, Ott, Gan: "Acetylation of tau inhibits its degradation and contributes to tauopathy." in: Neuron, Vol. 67, Issue 6, pp. 953-66, (2010) (PubMed).

    Kieken, Jovi?, Tonelli, Naslavsky, Caplan, Sorgen: "Structural insight into the interaction of proteins containing NPF, DPF, and GPF motifs with the C-terminal EH-domain of EHD1." in: Protein science : a publication of the Protein Society, Vol. 18, Issue 12, pp. 2471-9, (2009) (PubMed).

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