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Protein G Sepharose Bead

IP, Purif Protein G Sepharose beads 90 µm
Pubmed (7)
Catalog No. ABIN412450
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  • Target
    Immunoprecipitation (IP), Purification (Purif)
    Protein G Sepharose for affinity purification of antibodies.
    High binding capacity = Binding of IgG >20 mg human or rabbit IgG/ml Protein G-Sepharose.
    Minimal Leaching of the Ligand
    Flow Rate Tested* = 2.07 ml/min.
    *Test condition: = Calculations based on the time required to pass 18 ml of water through 2 ml settled beads (column diameter 1.5 cm).
    Usage = Reusable for up to 10 times without significant loss of binding capacity.
    Protein G-Sepharose beads are prepared by covalently coupling recombinant Protein G to 6% cross-linked Sepharose beads. Protein G (Cat. # ABIN412519) is a genetically engineered protein containing three IgG-binding regions of native Protein G. The cell wall binding region, albumin binding region and other non-specific regions have been eliminated from the recombinant Protein G to ensure the maximum specific IgG binding. The coupling technique is optimized to give a higher binding capacity for IgG & minimum leaching of recombinant Protein G. The IgG binding capacity of Protein G-Sepharose is >20 mg of human or rabbit IgG per ml of wet beads. Protein G-Sepharose beads display high chemical & physical stability as well as high flow rate, hydrophilicity & high gel strength. It can be used for IgG purification and immunoprecipitation.
    Bead Ligand
    Protein G
    Bead Matrix
    Sepharose beads
    Bead Size
    90 µm
  • Target
  • Application Notes
    - Purification of monoclonal and polyclonal antibodies from culture media, serum, ascites fluid or hybridoma supernatants.
    - Isolation of antibody/antigen complexes in immunoprecipitation experiments, since only the Fc region is involved in antibody binding and the Fab region is available for binding antigen.
    For Research Use only
  • Format
    Supplied as 50% slurry in 20 % Ethanol/H2O. 
    Handling Advice
    Do not freeze!
    4 °C
    Expiry Date
    12 months
  • Jia, Schulte, Loukas, Pickering, Pearson, Mobli, Jones, Rosengren, Daly, Gobert, Jones, Craik, Mulvenna: "Solution structure, membrane interactions, and protein binding partners of the tetraspanin Sm-TSP-2, a vaccine antigen from the human blood fluke Schistosoma mansoni." in: The Journal of biological chemistry, Vol. 289, Issue 10, pp. 7151-63, 2014 (PubMed).

    Price, Beauchamp, Rahir, Zhao, Rieger, Lau-Kilby, Tarbell: "CD8+ dendritic cell-mediated tolerance of autoreactive CD4+ T cells is deficient in NOD mice and can be corrected by blocking CD40L." in: Journal of leukocyte biology, Vol. 95, Issue 2, pp. 325-36, 2014 (PubMed).

    Wicht, Burkard, de Haan, van Kuppeveld, Rottier, Bosch: "Identification and characterization of a proteolytically primed form of the murine coronavirus spike proteins after fusion with the target cell." in: Journal of virology, Vol. 88, Issue 9, pp. 4943-52, 2014 (PubMed).

    Giacani, Denisenko, Tompa, Centurion-Lara: "Identification of the Treponema pallidum subsp. pallidum TP0092 (RpoE) regulon and its implications for pathogen persistence in the host and syphilis pathogenesis." in: Journal of bacteriology, Vol. 195, Issue 4, pp. 896-907, 2013 (PubMed).

    Samanta, Pursell, Mercurio: "IMP3 protein promotes chemoresistance in breast cancer cells by regulating breast cancer resistance protein (ABCG2) expression." in: The Journal of biological chemistry, Vol. 288, Issue 18, pp. 12569-73, 2013 (PubMed).

    He, Kermode: "Programmed cell death of the megagametophyte during post-germinative growth of white spruce (Picea glauca) seeds is regulated by reactive oxygen species and the ubiquitin-mediated proteolytic system." in: Plant & cell physiology, Vol. 51, Issue 10, pp. 1707-20, 2010 (PubMed).

    Tang, Rosen: "Functional consequences of the subdomain organization of the sulfs." in: The Journal of biological chemistry, Vol. 284, Issue 32, pp. 21505-14, 2009 (PubMed).

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