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Protein G Magnetic Beads Bead

IP, AC, Purif Protein G Magnetic particles 40 µm
Pubmed (9)
Catalog No. ABIN400576
$148.50
Plus shipping costs $45.00
2 mL
local_shipping Shipping to: United States
Delivery in 4 to 6 Business Days
  • Target
    Reactivity
    Streptococcus
    Application
    Immunoprecipitation (IP), Affinity Chromatography (AC), Purification (Purif)
    Purpose
     Protein G MagBeads are ideal for small-scale antibody purification and immunoprecipitation of proteins, protein complexes or other antigens.
    Brand
    MagBeads
    Characteristics
    Protein G MagBeads are superparamagnetic beads of average 40 μm in diameter, covalently coated with recombinant The Protein G MagBeads have a binding capacity of more than 10 mg Goat IgG per 1 ml settled beads (e.g. 4 ml 25% slurry).
    Bead Ligand
    Protein G
    Bead Matrix
    Magnetic particles
    Bead Size
    40 µm
  • Target
    Background
    Protein G, a bacterial cell wall protein isolated from group G Streptococci, binds to mammalian IgGs mainly through Fc regions. Native Protein G has three IgG binding domains and also the sites for albumin and cell-surface binding. Albumin and cell-surface binding domains have been eliminated from recombinant Protein G to reduce nonspecific binding. Protein G has greater affinity than Protein A for most mammalian IgGs, especially for certain subclasses including human IgG3, mouse IgG1 and rat IgG2a. Unlike Protein A, Protein G does not bind to human IgM, IgD and IgA.
  • Restrictions
    For Research Use only
  • Format
    Liquid
    Buffer
    The beads are supplied as 25% slurry in phosphate buffered saline (PBS), pH 7.4, containing 20% ethanol.  0.5 ml settled Beads (2 ml 25% slurry)
    Storage
    4 °C
    Storage Comment
    Store at 4°C, do NOT freeze.
    Expiry Date
    12 months
  • Patel, Baranwal, Love, Patel, Grossman, Patel: "Inhibition of C-terminal binding protein attenuates transcription factor 4 signaling to selectively target colon cancer stem cells." in: Cell cycle (Georgetown, Tex.), Vol. 13, Issue 22, pp. 3506-18, 2015 (PubMed).

    Youker, Assad-Kottner, Cordero-Reyes, Trevino, Flores-Arredondo, Barrios, Fernandez-Sada, Estep, Bhimaraj, Torre-Amione et al.: "High proportion of patients with end-stage heart failure regardless of aetiology demonstrates anti-cardiac antibody deposition in failing myocardium: humoral activation, a potential contributor of ..." in: European heart journal, Vol. 35, Issue 16, pp. 1061-8, 2014 (PubMed).

    Xu, Yang, Zhao, Wu, Qi: "AKAP3 synthesis is mediated by RNA binding proteins and PKA signaling during mouse spermiogenesis." in: Biology of reproduction, Vol. 90, Issue 6, pp. 119, 2014 (PubMed).

    Evnouchidou, Weimershaus, Saveanu, van Endert: "ERAP1-ERAP2 dimerization increases peptide-trimming efficiency." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 193, Issue 2, pp. 901-8, 2014 (PubMed).

    Kuroda, Hamaguchi, Moriyama, Tanimoto, Haginaka: "Improved capillary electrophoresis method for the analysis of carbohydrate-deficient transferrin in human serum, avoiding interference by complement C3." in: Journal of pharmaceutical and biomedical analysis, Vol. 76, pp. 81-6, 2013 (PubMed).

    Kapadia, Viswakarma, Parsa, Kain, Behera, Suraj, Babu, Kar, Panda, Zhu, Jia, Thimmapaya, Reddy, Misra: "ERK2-mediated phosphorylation of transcriptional coactivator binding protein PIMT/NCoA6IP at Ser298 augments hepatic gluconeogenesis." in: PLoS ONE, Vol. 8, Issue 12, pp. e83787, 2013 (PubMed).

    Bilichak, Ilnystkyy, Hollunder, Kovalchuk: "The progeny of Arabidopsis thaliana plants exposed to salt exhibit changes in DNA methylation, histone modifications and gene expression." in: PLoS ONE, Vol. 7, Issue 1, pp. e30515, 2012 (PubMed).

    Dai, Santagata, Tang, Shi, Cao, Kwon, Bronson, Whitesell, Lindquist: "Loss of tumor suppressor NF1 activates HSF1 to promote carcinogenesis." in: The Journal of clinical investigation, Vol. 122, Issue 10, pp. 3742-54, 2012 (PubMed).

    Morales, Wu, Yang, Hao, Li: "Drosophila glycoprotein 93 Is an ortholog of mammalian heat shock protein gp96 (grp94, HSP90b1, HSPC4) and retains disulfide bond-independent chaperone function for TLRs and integrins." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 183, Issue 8, pp. 5121-8, 2009 (PubMed).

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