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P8651

Sigma-Aldrich

Protein A–Peroxidase from Staphylococcus aureus/horseradish

lyophilized powder

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Synonym(s):
Peroxidase–Protein A
MDL number:
NACRES:
NA.46

conjugate

peroxidase conjugate

Quality Level

100
200

form

lyophilized powder

technique(s)

direct ELISA: 1:80,000 using human IgG

storage temp.

−20°C

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This Item
P8170P2165P8375
Peroxidase from horseradish Type VI, essentially salt-free, lyophilized powder, ≥250 units/mg solid (using pyrogallol)

P8375

Peroxidase from horseradish

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

essentially salt-free, lyophilized powder

storage temp.

−20°C

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

2-8°C

Quality Level

100, 200

Quality Level

-

Quality Level

300

Quality Level

300

conjugate

peroxidase conjugate

conjugate

peroxidase conjugate

conjugate

biotin conjugate

conjugate

-

General description

Protein A is a cell wall constituent of Staphylococcus aureus, with a molecular weight of 56kDa. It possesses five binding domains which interact with heavy chains of immunoglobulins at the Fc or Fab fragment. In response to protein A, the complement system, interferon production, hypersensitivity reactions and cell-mediated cytotoxicity get activated. Horseradish peroxidase is a heme-containing enzyme. In the presence of hydrogen peroxide, the enzyme catalyzes the oxidation of luminol.

Specificity

Binds IgG only from most mammals, except rat, goat, sheep.

Application

Protein A–Peroxidase from Staphylococcus aureus/horseradish has been used in enzyme-linked immunosorbent assay (ELISA).

Packaging

Package size based on protein content.

Physical form

Lyophilized powder containing sodium citrate buffer salt. Protein determined by A205.

Preparation Note

Protein A, extracellular, coupled to Peroxidase, Type VI, by a modification of the procedure of O′Sullivan, M.J., et al., FEBS Lett., 95, 311 (1978), which favors low molecular weight conjugates.

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.

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Katharina Mayer et al.
International journal of molecular sciences, 22(16) (2021-08-28)
Within-host adaptation is a typical feature of chronic, persistent Staphylococcus aureus infections. Research projects addressing adaptive changes due to bacterial in-host evolution increase our understanding of the pathogen's strategies to survive and persist for a long time in various hosts
Staphylococcal protein A consists of five IgG-binding domains
Tomas MOKS
European Journal of Biochemistry (1986)
Monica L Mazuz et al.
International journal for parasitology. Parasites and wildlife, 7(3), 317-321 (2018-09-04)
Neosporosis and besnoitiosis, caused by cyst-forming protozoa Neospora caninum and Besnoitia besnoiti, respectively, are parasitic infestations of livestock in Israel. These parasites cause significant economic losses in cattle due to reproductive and productive disorders. Both parasites have been detected in
Maria Fort et al.
Veterinary microbiology, 125(3-4), 244-255 (2007-07-06)
The notion that postweaning multisystemic wasting syndrome (PMWS)-affected pigs develop an impaired humoral response against porcine circovirus type 2 (PCV2) has been reported in several studies. However, little information is available regarding the presence of neutralizing antibodies (NA) in PCV2-infected
Gaetana Lanzi et al.
Journal of virology, 80(10), 4998-5009 (2006-04-28)
Deformed wing virus (DWV) of honeybees (Apis mellifera) is closely associated with characteristic wing deformities, abdominal bloating, paralysis, and rapid mortality of emerging adult bees. The virus was purified from diseased insects, and its genome was cloned and sequenced. The

Protocols

To standardize a procedure for the assay of Peroxidase using 2,2'-Azino-bis(3-Ethylbenzthiazoline-6-Sulfonic Acid) as a substrate.

This procedure is for the determination of Peroxidase enzymatic activity using Pyrogallol as the substrate.

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

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