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S5512

Sigma-Aldrich

Streptavidin−Peroxidase from Streptomyces avidinii

lyophilized powder

Synonym(s):

Streptavidin−HRP from Streptomyces avidinii

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About This Item

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

conjugate

peroxidase conjugate

Quality Level

form

lyophilized powder

composition

Protein, ≥70% E1%/280

technique(s)

direct ELISA: 1:50,000

storage temp.

−20°C

General description

Steptavidin is coupled to horseradish peroxidase (HRP) using citrate buffer, pH 6.0, and a modified published procedure to form a 1:1 conjugate. HRP has a molecular mass of ~44kDa and steptavidin has a molecular mass of ~60kDa.
Streptavidin derives its name from its bacterial source Streptomyces avidinii and from the hen egg-white protein, avidin, which has high affinity to biotin. Its homologous core shares 33% sequence similarity with avidin, as well as sharing a common tetrameric structure. It is a crystalline tetrameric protein, with a molecular weight of 4*15000Da. It binds four molecules of biotin. Streptavidin lacks carbohydrate and sulfur-containing amino acids.
Streptavidin is considered as a high-affinity biotin-binding agent, which shows resistance to extreme pH, detergents temperature, denaturants and enzymes, hence it is used in molecular biology and bionanotechnology.

Application

Streptavidin- Peroxidase from Streptomyces avidinii has been used for ELISA (enzyme linked immunosorbent assay) and Enzyme-Linked ImmunoSpot (ELISPOT).
Streptavidin-Peroxidase from Streptomyces avidinii has used as a secondary reagent for detection of biotinylated antibodies in standard ELISA, immunoblotting, and immunocytochemistry procedures.

Biochem/physiol Actions

Streptavidin is an antibiotic that functions by binding to and depleting the essential vitamin biotin from the surrounding environment. Because of its unique properties, streptavidin has found various applications in biological studies, including immunotherapy, immunoassays, hybridization assays, lymphocyte activation, antigen localization, and affinity chromatography.

Packaging

Package size based on protein content

Physical form

Lyophilized powder containing citrate buffer salts.

Preparation Note

Labeled with Type VI peroxidase by a modification of the method of O′Sullivan, M.J., et al., FEBS Lett., 95, 311 (1978).
Purified by affinity chromatography.

Analysis Note

The optimal working dilution should be determined empirically using a range of dilutions from a 1 mg/mL stock in buffer.

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.

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Joana M D Portela et al.
Journal of clinical medicine, 9(1) (2020-01-18)
Cancer therapy and conditioning treatments of non-malignant diseases affect spermatogonial function and may lead to male infertility. Data on the molecular properties of spermatogonia and the influence of disease and/or treatment on spermatogonial subpopulations remain limited. Here, we assessed if
K G Welinder
European journal of biochemistry, 96(3), 483-502 (1979-06-01)
Horseradish peroxidase C dominates quantitatively among the isoperoxidases of horseradish root and has an isoelectric point close to 9. It consists of a hemin prosthetic group, 2 Ca2+ and 308 amino acid residues, including 4 disulfide bridges, in a single
Carmine Giorgio et al.
Biochemical pharmacology, 147, 21-29 (2017-11-14)
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Progress in Molecular Biology and Translational Science, 104, 299-323 (2011)
J S Stanley et al.
European journal of biochemistry, 268(20), 5424-5429 (2001-10-19)
An enzymatic mechanism has been proposed by which biotinidase may catalyze biotinylation of histones. Here, human cells were found to covalently bind biotin to histones H1, H2A, H2B, H3, and H4. Cells respond to proliferation with increased biotinylation of histones;

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