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Protein G Sepharose

based on 7 citations in multiple journalsProtein G Sepharose74.1 4
Reusable Protein G conjugated Sepharose beads with ≥20 mg/ml binding capacity & 2.07 ml/min flow rate for antibody purification from multiple sources
Catalog #: 6511

In stock

SKU-Size Size Price Qty
6511-1 1 ml
$130.00
6511-5 5 ml
$415.00
6511-25 25 ml
$995.00
6511-100 100 ml
$1,995.00
More Sizes Get Quote

Product Details

Highlights • CONTENTS: Supplied as 50% slurry in 20 % Ethanol/H2O.
• FEATURES:
- 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.
• APPLICATIONS
- 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.
Storage Conditions 4°C
Shipping Conditions Gel Pack
USAGE For Research Use Only! Not For Use in Humans.

Details

Protein G-Sepharose beads are prepared by covalently coupling recombinant Protein G to 6% cross-linked Sepharose beads. BioVision Protein G (Cat. # 6510) 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.


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Wicht et al., Identification and Characterization of a Proteolytically Primed Form of the Murine Coronavirus Spike Proteins after Fusion with the Target Cell. J. Virol., May 2014; 88: 4943 - 4952.
Jia et al., Solution Structure, Membrane Interactions, and Protein Binding Partners of the Tetraspanin Sm-TSP-2, a Vaccine Antigen from the Human Blood Fluke Schistosoma mansoni.J. Biol. Chem.,  Mar 2014; 289: 7151 - 7163.
Price et al., CD8+ dendritic cell-mediated tolerance of autoreactive CD4+ T cells is deficient in NOD mice and can be corrected by blocking CD40L. J. Leukoc. Biol., Feb 2014; 95: 325 - 336.
Sanjoy Samanta et al., IMP3 Protein Promotes Chemoresistance in Breast Cancer Cells by Regulating Breast Cancer Resistance Protein (ABCG2) Expression. J. Biol. Chem., May 2013; 288: 12569 - 12573.
Lorenzo Giacani et al., Identification of the Treponema pallidum subsp. pallidum TP0092 (RpoE) Regulon and Its Implications for Pathogen Persistence in the Host and Syphilis Pathogenesis. J. Bacteriol., Feb 2013; 195: 896 - 907.
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