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P3391 Sigma

Protein A-Sepharose® from Staphylococcus aureus

lyophilized powder

Synonym: Protein A–Agarose

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Properties

Related Categories Affinity Chromatography, Affinity Resins, Antibodies, Antibody Purification, Antibody Purification and Characterization,
form   lyophilized powder
extent of labeling   3 mg per mL
matrix   Sepharose CL-4B
matrix activation   cyanogen bromide
matrix attachment   amino
matrix spacer   1 atom
capacity   ≥16 mg/mL binding capacity (human IgG)
storage temp.   2-8°C

Description

Frequently Asked Questions

Live Chat and Frequently Asked Questions are available for this Product.

Quantity

Swelling: 1 g swells to approx. 4 ml.

Physical form

Supplied as lyophilized powder stabilized with lactose and dextran.

Application

Protein A-Sepharose® is used for affinity chromatography, antibody purification and characterization, immunoaffinity matrices, protein chromatography, protein A, G and L resins, and recombinant protein expression and analysis. Protein A-Sepharose® has been used to develop strategies for investigating protein interactions, to improve the detection of celiac disease, and to study diabetes in children.

Legal Information

Sepharose is a registered trademark of GE Healthcare

Price and Availability

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Safety & Documentation

Safety Information

WGK Germany 
3

Protocols & Articles

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Peer-Reviewed Papers

References

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Plant Retromer, Localized to the Prevacuolar Compartment and Microvesicles in Arabidopsis, May Interact with Vacuolar Sorting Receptors. Oliviusson, P. et al. Plant Cell 18, 1239-1252, (2006)

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A Phosphorylated Cytoplasmic Autoantigen, GW182, Associates with a Unique Population of Human mRNAs within Novel Cytoplasmic Speckles. Eystathioy, T., et al. Mol. Biol. Cell 13, 1338-1351, (2002)

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Caspase-dependent Cleavage of Signaling Proteins during Apoptosis: A Turn-Off Mechanism for Anti-Apoptotic Signals. Widmann, C., et al. J. Biol. Chem. 273, 7141-7147, (1998)

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Dissecting long-range transcriptional mechanisms by chromatin immunoprecipitation. Johnson, K.D., and Bresnick, E.H. Methods 26, 27-36, (2002)

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Subcellular Distribution and Function of Rab3A, B, C, and D Isoforms in Insulin-Secreting Cells. Iezzi, M., et al. Mol. Endocrinol. 13, 202-212, (1999)

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Proteins from Multiple Metabolic Pathways Associate with Starch Biosynthetic Enzymes in High Molecular Weight Complexes: A Model for Regulation of Carbon Allocation in Maize Amyloplasts. Hennen-Bierwagen, T.A., et al. Plant Physiol. 149, 1541-1559, (2009)

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A novel human-specific soluble vascular endothelial growth factor receptor 1: cell-type-specific splicing and implications to vascular endothelial growth factor homeostasis and preeclampsia. Itin, A., et al. Circ. Res. 102, 1566-1574, (2008)

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Peroxynitrite-Induced Nitrotyrosination of Proteins Is Blocked by Direct 5-Lipoxygenase Inhibitor Zileuton. Coffey, M.J., et al. J. Pharmacol. Exp. Ther. 299, 198-203, (2001)

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A novel triple mix radiobinding assay for the three ZnT8 (ZnT8-RWQ) autoantibody variants in children with newly diagnosed diabetes Vaziri-Sani, F., et al. J. Immunol. Methods 371, 25-37, (2011)

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A Chromatin-remodeling Protein Is a Component of Fission Yeast Mediator. Khorosjutina, O., et al. J. Biol. Chem. 285, 29729-29737, (2010)

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Cloning and characterization of hELD/OSA1, a novel BRG1 interacting protein. Hurlstone, A.F.L., et al. Biochem. J. 364, 255-264, (2002)

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Inhibition of in vitro cotranslational disassembly of tobacco mosaic virus by monoclonal antibodies to the viral coat protein. Saunal, H., et al. J. Gen. Virol. 74, 897-900, (1993)

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A Pore Residue of the KCNQ3 Potassium M-Channel Subunit Controls Surface Expression. Gómez-Posada, J.C., et al. J. Neurosci. 30, 9316-9323, (2010)

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Peblp (Pas7p) Is an Intraperoxisomal Receptor for the NH2-terminal, Type 2, Peroxisomal Targeting Sequence of Thiolase: Peblp Itself Is Targeted to Peroxisomes by an NHE-terminal Peptide. Zhang, J.W., and Lazarow, P.B. J. Cell Biol. 132, 325-334, (1996)

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AKINβγ Contributes to SnRK1 Heterotrimeric Complexes and Interacts with Two Proteins Implicated in Plant Pathogen Resistance through Its KIS/GBD Sequence. Gissot, L., et al. Plant Physiol. 142, 931-944, (2006)

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Theiler's virus L protein is targeted to the mitochondrial outer membrane. Sorgeloos, F., et al. J. Virol. 85, 3690-4, (2011)

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Regulation of LIM-kinase 1 and cofilin in thrombin-stimulated platelets. Pandey, D., et al. Blood 107, 575-583, (2006)

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CCAAT/enhancer-binding protein mRNA is translated into multiple proteins with different transcription activation potentials. Ossipow, V., et al. Proc. Natl. Acad. Sci. U. S. A. 90, 8219-8223, (1993)

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Archaeal RNase P has multiple protein subunits homologous to eukaryotic nuclear RNase P proteins. Hall, T.A., and Brown, J.W. RNA 8, 296-306, (2002)

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The design of protein-imprinted polymers as antibody substitutes for investigating protein-protein interactions Gao, J., et al. Biomaterials 33, 3344-3352, (2012)

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Improved efficacy by using the pTnT-rhtTG plasmid for the detection of celiac disease specific tissue transglutaminase autoantibodies in radioligand binding assays Kjellerås, J., et al. Scand. J. Clin. Lab. Invest. 71, 701-704, (2011)

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N-terminal amino acid sequence identity between a major allergen of Ascaris lumbricoides and Ascaris suum, and MHC-restricted IgE responses to it. Christie, J.F., et al. Immunology 69, 596-602, (1990)

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GRID: A Novel Grb-2-Related Adapter Protein That Interacts with the Activated T Cell Costimulatory Receptor CD28. Ellis, J.H., et al. J. Immunol. 164, 5805-5814, (2000)

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Novel Mitochondrial Substrates of Omi Indicate a New Regulatory Role in Neurodegenerative Disorders. Johnson, F., and Kaplitt, M.G. PLoS ONE 4, e7100, (2009)

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Protocol: methodology for chromatin immunoprecipitation (ChIP) in Chlamydomonas reinhardtii. Strenkert, D., et al. Plant Methods 7, 35, (2011)

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Biochemical Characterization Of Native Usher Protein Complexes From A Vesicular Subfraction Of Tracheal Epithelial Cells. Zallocchi, M., et al. Biochem. Pharmacol. 49, 1236-47, (2010)

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Recovery of an HMWP/hmwBP (pUL48/pUL47) complex from virions of human cytomegalovirus: subunit interactions, oligomer composition, and deubiquitylase activity. Tullman JA, Harmon ME, Delannoy M, et al. J. Virol. 88(15), 8256-67, (2014)

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Enzymatic Digestion of Monoclonal Antibodies. Andrew, S.M. Protein Protocols Handbook, (2002) Part VII, 1047-1052

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