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Protein A Resin

Purif, AC Protein A Agarose beads 90 µm
Produktnummer ABIN1536564
  • Target Alle Protein A Produkte
    Protein A
    Reaktivität
    Staphylococcus aureus
    Applikation
    Purification (Purif), Affinity Chromatography (AC)
    Verwendungszweck
    Protein A Resin is an affinity chromatography medium designed for easy, one-step purification of classes, subclasses and fragments of immunoglobulins from biological fluids and from cell culture media.
    Produktmerkmale
    Protein A Resin can also be used for immunoprecipitation of proteins,protein complexes or antigens. The recombinant protein A ligand is coupled to 4% agarose. The coupling is optimized to give high binding capacity for immunoglobulins. The static binding capacity of Protein A Resin is greater than 20 mg rabbit IgG/ml settled resin. The dynamic binding capacity will vary depending on several factors such as target antibody, flow rate etc.

    Ligand: Recombinant Streptococcal protein A expressed in E. coli
    Number of IgG binding sites per ligand: 5
    MW of ligand: Approximately 34 kDa
    PI of ligand: 5.17
    Degree of substitution: Approximately 2 mg protein A/ml settled resin
    Static binding capacity: >20 mg rabbit IgG/ml settled resin
    Matrix: spherical agarose, 4%
    Average particle size: 90 μm (45-165 μm)
    Bead Ligand
    Protein A
    Bead Matrix
    Agarose beads
    Bead Size
    90 µm
  • Kommentare

    High temperature heating is not recommended. The agarose melts above 65°C.

    Beschränkungen
    Nur für Forschungszwecke einsetzbar
  • Format
    Liquid
    Buffer
    1X PBS containing 20% ethanol
    Lagerung
    4 °C
    Informationen zur Lagerung
    Store regenerated Protein A Resin in Binding/Wash Buffer containing 20% ethanol at 2°C to 8°C. Do not freeze.
    Haltbarkeit
    18 months
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    Cheung, Zhu, Lui, Dimitrov, Baron: "Human monoclonal antibody fragments targeting matrilin-3 in growth plate cartilage." in: Pharmaceutical research, Vol. 32, Issue 7, pp. 2439-49, (2015) (PubMed).

    Mui, Zhou, Blanchette, Chughtai, Knight, Gruosso, Papadakis, Huang, Park, Gingras, Branton: "The Human Adenovirus Type 5 E4orf4 Protein Targets Two Phosphatase Regulators of the Hippo Signaling Pathway." in: Journal of virology, Vol. 89, Issue 17, pp. 8855-70, (2015) (PubMed).

    Ju, Na, Yu, Kim, Jeong, Jung: "Structural consequences of aglycosylated IgG Fc variants evolved for Fc?RI binding." in: Molecular immunology, Vol. 67, Issue 2 Pt B, pp. 350-6, (2015) (PubMed).

    Asavapanumas, Ratelade, Verkman: "Unique neuromyelitis optica pathology produced in naïve rats by intracerebral administration of NMO-IgG." in: Acta neuropathologica, Vol. 127, Issue 4, pp. 539-51, (2014) (PubMed).

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    Wang, Zhao, Wang: "C-type lectin binds to ?-integrin to promote hemocytic phagocytosis in an invertebrate." in: The Journal of biological chemistry, Vol. 289, Issue 4, pp. 2405-14, (2014) (PubMed).

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    Zhang, Verkman: "Longitudinally extensive NMO spinal cord pathology produced by passive transfer of NMO-IgG in mice lacking complement inhibitor CD59." in: Journal of autoimmunity, Vol. 53, pp. 67-77, (2014) (PubMed).

    Asavapanumas, Verkman: "Neuromyelitis optica pathology in rats following intraperitoneal injection of NMO-IgG and intracerebral needle injury." in: Acta neuropathologica communications, Vol. 2, pp. 48, (2014) (PubMed).

    Payapilly, High: "BAG6 regulates the quality control of a polytopic ERAD substrate." in: Journal of cell science, Vol. 127, Issue Pt 13, pp. 2898-909, (2014) (PubMed).

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    Ratelade, Verkman: "Inhibitor(s) of the classical complement pathway in mouse serum limit the utility of mice as experimental models of neuromyelitis optica." in: Molecular immunology, Vol. 62, Issue 1, pp. 104-13, (2014) (PubMed).

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    Song, Kim, Kim, Lee, Kim, Park: "IGFBP5 mediates high glucose-induced cardiac fibroblast activation." in: Journal of molecular endocrinology, Vol. 50, Issue 3, pp. 291-303, (2013) (PubMed).

  • Target
    Protein A
    Abstract
    Protein A Produkte
    Synonyme
    alpha protein Bead, repB Bead
    Hintergrund
    Protein A, a bacterial cell wall protein isolated from Staphylococcus aureus, binds to mammalian IgGs mainly through Fc regions. Native protein A has five IgG binding domains and many other domains with unknown functions. Recombinant protein A contains five high affinity IgG binding domains with other non-essential domains removed to reduce nonspecific binding. Since only the Fc region is involved in binding, the Fab region is available for binding antigens. 
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