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Streptavidin−Peroxidase from Streptomyces avidinii

lyophilized powder

Sinônimo(s):

Streptavidin−HRP from Streptomyces avidinii

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R$ 647,00
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0.1 MG
R$ 647,00
0.5 MG
R$ 2.069,00
1 MG
R$ 3.220,00
2 MG
R$ 6.250,00

About This Item

Número MDL:
Código UNSPSC:
12352203
NACRES:
NA.46

R$ 647,00


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conjugado

peroxidase conjugate

Nível de qualidade

Formulário

lyophilized powder

composição

Protein, ≥70% E1%/280

técnica(s)

direct ELISA: 1:50,000

temperatura de armazenamento

−20°C

Descrição geral

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.[1][2][3]
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.[4] It is a crystalline tetrameric protein, with a molecular weight of 4*15000Da. It binds four molecules of biotin.[5][6] Streptavidin lacks carbohydrate and sulfur-containing amino acids.[7]
Streptavidin is considered as a high-affinity biotin-binding agent, which shows resistance to extreme pH, detergents temperature, denaturants and enzymes,[8] hence it is used in molecular biology and bionanotechnology.

Aplicação

Streptavidin- Peroxidase from Streptomyces avidinii has been used for ELISA (enzyme linked immunosorbent assay) [9][10] and Enzyme-Linked ImmunoSpot (ELISPOT).[11]
Streptavidin-Peroxidase from Streptomyces avidinii has used as a secondary reagent for detection of biotinylated antibodies in standard ELISA,[9][12] immunoblotting,[13] and immunocytochemistry[14] procedures.

Ações bioquímicas/fisiológicas

Streptavidin is an antibiotic that functions by binding to and depleting the essential vitamin biotin from the surrounding environment.[5] 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.[7]

Embalagem

Package size based on protein content

forma física

Lyophilized powder containing citrate buffer salts.

Nota de preparo

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.

Nota de análise

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

Exoneração de responsabilidade

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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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;
Carmine Giorgio et al.
Biochemical pharmacology, 147, 21-29 (2017-11-14)
Eph/ephrin system is an emerging target for cancer therapy but the lack of potent, stable and orally bioavailable compounds is impairing the development of the field. Since 2009 our research group has been devoted to the discovery and development of
Polymer nanoparticles
Progress in Molecular Biology and Translational Science, 104, 299-323 (2011)
Onset and duration of fecal shedding, cell-mediated and humoral immune responses in pigs after challenge with a pathogenic isolate or attenuated vaccine strain of Lawsonia intracellularis.
Guedes RM and Gebhart CJ
Veterinary Microbiology, 91(2-3), 135-145 (2003)
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

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