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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

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Quantity

Swelling: 1 g swells to approx. 4 ml.

Physical form

Supplied as lyophilized powder stabilized with lactose and dextran.

Application

Protein A-Sepharose was used:
• for immunoprecipitated placentas for protein and RNA analyses using Western blot technique.1
• in chromatin immunoprecipitation to understand the link between Mediator and remodelling of chromatin structure at specific promoters.2
• as lysis buffer to remove endogenous G-type Igs in protein extraction of brain samples from female rats.3
• in immunoprecipitation of [32P] phosphomyristin C of rabbit antiserum, to study the down-regulation of protein kinase C (PKC) and phosphomyristin C (PMC) during T-cell development.4

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.

General description

Protein A-Sepharose when linked with antibody, helps improving antigen binding capacity of IgG crosslinked to column matrices. In this case, binding happens between Protein A and Fc portion of the IgG molecule leaving antigen specific sites free.5

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

Articles

Antibody Basics

Immunoglobulins (Igs) are produced by B lymphocytes and secreted into plasma. The Ig molecule in monomeric form is a glycoprotein with a molecular weight of approximately 150 kDa that is shaped more ...
Keywords: Affinity chromatography, Centrifugation, Chromatography, Digestions, High performance liquid chromatography, Ion Exchange, Microscopy, Precipitation, Purification, Scanning electron microscopy

Related Content

Antibody Explorer - Over 80,000 Products

Monoclonal and polyclonal primary antibodies are focused on cell biology, neurobiology and molecular biology. Secondary antibodies targeting multiple host’s IgG are conjugated to alkaline phosphatase...
Keywords: Buffers, Cancer, Cell biology, Enzyme-linked immunosorbent assay, Immunohistochemistry, Immunoprecipitation, Molecular biology, Neuroscience, Phosphorylations, Purification, Western blot

Peer-Reviewed Papers

References

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1. 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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2. 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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3. Phosphorylation of N-methyl-D-aspartic acid receptor-associated neuronal nitric oxide synthase depends on estrogens and modulates hypothalamic nitric oxide production during the ovarian cycle. Parkash J, d'Anglemont de Tassigny X, Bellefontaine N, et al. Endocrinology 151(6), 2723-35, (2010)

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4. A major myristylated substrate of protein kinase C and protein kinase C itself are differentially regulated during murine B- and T-lymphocyte development and activation. Hornbeck P, Nakabayashi H, Fowlkes BJ, et al. Mol. Cell. Biol. 9(9), 3727-35, (1989)

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5. An improved method for immobilizing IgG antibodies on protein A-agarose. Sisson TH, et al. J. Immunol. Methods 127(2), 215-220, (1990)

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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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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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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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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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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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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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Heparan sulfation is essential for the prevention of cellular senescence. Jung SH, Lee HC, Yu DM, et al. Cell Death Differ., doi:10.1038/cdd.2015.107, (2015)

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

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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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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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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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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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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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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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