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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. |
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| 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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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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