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P3838

Sigma-Aldrich

Protein A from Staphylococcus aureus

Soluble, Cowan Strain, essentially salt-free, lyophilized powder

Synonym(s):

Protein A, Staphylococcus aureus Protein A

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.46

conjugate

unconjugated

Quality Level

form

essentially salt-free, lyophilized powder

technique(s)

ELISA: suitable
immunohistochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable

capacity

7-14 mg/mg, solid binding capacity (human IgG)

UniProt accession no.

storage temp.

2-8°C

Gene Information

Staphylococcus aureus subsp. aureus NCTC 8325 ... SAOUHSC_00069(3919448)

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Application

Protein A may be conjugated with various reporter molecules including fluorescent dyes (FITC), enzyme markers (peroxidase, β-galactosidase, alkaline phosphatase), biotin, and colloidal gold without affecting the antibody binding site on the molecule. These conjugates are used to detect immunoglobulins in various immunochemical assays including western blotting, immunohistochemistry, and ELISA applications. In addition, protein A may be immobilized on a solid support such as agarose or acrylic beads for the purification of either polyclonal or monoclonal immunoglobulins. It is also routinely used for immunoprecipitation assays.

Biochem/physiol Actions

Protein A is a highly stable cell surface receptor produced by several strains of Staphylococcus aureus. It consists of a single polypeptide chain of molecular weight 42 kDa, containing four repetitive domains rich in aspartic and glutamic acids but devoid of cysteine. It contains little or no carbohydrate and only 4 tyrosine residues and no tryptophans. Protein A is capable of binding to the Fc portion of immunoglobulins, especially IgGs, from a large number of species. One protein A molecule has been shown to bind at least 2 molecules of IgG simultaneously. The IgG binding domain of Protein A consists of three anti-parallel α-helicies, the third of which is disrupted when the protein is complexed with the Fc region of the immunoglobulins. Protein A will bind the Fc portion of human IgG subclasses, IgM, IgA and IgE; and mouse IgG1 (weakly), IgG2a, and IgG2b. Protein A also binds IgGs from other species, including monkey, rabbit, pig, guinea pig, dog, and cat.
Protein A also participates in a number of different protective biological functions including anti-tumor, toxic, and carcinogenic activities. In addition to acting as an immunomodulator, it also has antifungal and antiparasitic properties.

Preparation Note

Purified by affinity chromatography

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


Certificates of Analysis (COA)

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E Mongodin et al.
The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society, 48(4), 523-534 (2000-03-22)
Staphylococcus aureus is a common human pathogen involved in non-bronchial diseases and in genetic and acquired bronchial diseases. In this study, we applied an immunolabeling approach for in vivo and in vitro detection of S. aureus, based on the affinity
Protein A isolated from Staphylococcus aureus after digestion with lysostaphin.
J Sjöquist et al.
European journal of biochemistry, 29(3), 572-578 (1972-09-25)
Emma M Lessieur et al.
Diabetologia, 65(10), 1734-1744 (2022-07-20)
Induction of intercellular adhesion molecule-1 (ICAM-1) has been implicated in the development of macrovascular and microvascular diseases such as diabetic retinopathy. Lesions of diabetic retinopathy are unique to the retina but the reason for this is unclear, as all tissues
Stéphane Gilbert et al.
Journal of cell science, 129(17), 3262-3273 (2016-07-17)
Keratins are epithelial cell intermediate filament (IF) proteins that are expressed as pairs in a cell-differentiation-regulated manner. Hepatocytes express the keratin 8 and 18 pair (denoted K8/K18) of IFs, and a loss of K8 or K18, as in K8-null mice
Regina Stoltenburg et al.
International journal of molecular sciences, 19(2) (2018-03-03)
New, as yet undiscovered aptamers for Protein A were identified by applying next generation sequencing (NGS) to a previously selected aptamer pool. This pool was obtained in a classical SELEX (Systematic Evolution of Ligands by EXponential enrichment) experiment using the

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