Protein G Sepharose

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Immunoprecipitation (IP), Purification (Purif)
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Purpose Protein G Sepharose for affinity purification of antibodies.
Specificity 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.
Characteristics 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.
ProductDetails: Bead Ligand Protein G
ProductDetails: Bead Matrix Sepharose beads
ProductDetails: Bead Size 90 µm
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.
Restrictions For Research Use only
Format Liquid
Buffer Supplied as 50% slurry in 20 % Ethanol/H2O. 
Handling Advice Do not freeze!
Storage 4 °C
Expiry Date 12 months
Product cited in: 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).