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A7294

Sigma-Aldrich

Avidin–Alkaline Phosphatase

buffered aqueous solution

Synonyme(s) :

Avidin–AP

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.46

Source biologique

avidin from egg white
enzyme from bovine (calf) intestine

Conjugué

alkaline phosphatase conjugate

Forme

buffered aqueous solution

Technique(s)

direct ELISA: 1:70,000
western blot: 1:150,000-1:300,000 using using β-actin in total cell extract of HeLa cells (5-10 μg per lane

Conditions d'expédition

wet ice

Température de stockage

2-8°C

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Description générale

Avidin is homotetrameric protein (66 kDa) obtained from egg whites and binds strongly to biotin. It has four identical subunits of 16,400 Daltons each. It is an attractive adaptor protein, that is resistant to denaturation. This glycoprotein is present in avian, reptilian and amphibian egg white. The product is affinity purified egg white avidin (acitivity 10-15 units/mg protein) conjugated to alkaline phosphatase using a 0.2% glutaraldehyde method.
Avidin-biotin association has been utilized in immunoassays to detect the localization of antigens in tissues. The use of avidin-biotin immunoassay enhances the sensitivity of the technique and facilitates the detection of antigens in low quantities.

Application

Avidin-Alkaline Phosphatase has been used for ELISA. The product can also be used for western blot at 1:150,000-1:300,000 dilutions.
Avidin-Alkaline Phosphatase has been used in enzyme-linked immunosorbent assay (ELISA).
Cytokine ELISA Assays were performed using a biotinylated anti-IL-2 antibody and alkaline phosphatase avidin.

Actions biochimiques/physiologiques

Avidin-biotin association has been utilized in immunoassays to detect the localization of antigens in tissues. The use of avidin-biotin immunoassay enhances the sensitivity of the technique and facilitates the detection of antigens in low quantities. Avidin is a fatty acid biosynthesis regulator. It participates in terminal cell differentiation by weakening the multiplication of cell without affecting the differentiation process.

Forme physique

Solution in 0.05 M Tris buffer, pH 8.0, containing 1% bovine serum albumin, 1 mM MgCl2 and 15 mM sodium azide.

Notes préparatoires

Affinity purified protein conjugated to alkaline phosphatase using 0.2% glutaraldehyde.

Clause de non-responsabilité

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.

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Consulter la Bibliothèque de documents

Ana Maria Marassá et al.
Revista da Sociedade Brasileira de Medicina Tropical, 39(2), 183-186 (2006-05-16)
Lutzomyia longipalpis and Lutzomyia almerioi, phlebotomine species from the fauna of Serra da Bodoquena, in the State of Mato Grosso do Sul, Brazil, have been studied, particularly due to the fact of their abundance and occurrence, the Guaicurus settlement, focus
(Strept)avidin-Biotin Systems
Bioconjugate Techniques, 465-505 (2013)
Kaitlyn Grando et al.
Frontiers in cellular and infection microbiology, 12, 884065-884065 (2022-06-02)
The bacterial amyloid curli, produced by Enterobacteriales including Salmonella species and Escherichia coli, is implicated in the pathogenesis of several complex autoimmune diseases. Curli binds to extracellular DNA, and these complexes drive autoimmunity via production of anti-double-stranded DNA autoantibodies. Here
Avidin expression during chick chondrocyte and myoblast development in vitro and in vivo: regulation of cell proliferation
Zerega B, et al.
Journal of Cell Science, 114(8), 1473-1482 (2001)
Observations on the feeding habits of Lutzomyia longipalpis (Lutz \& Neiva, 1912)(Diptera: Psychodidae: Phlebotominae) in Campo Grande, an endemic area of visceral leishmaniasis in Mato Grosso do Sul, Brazil
de Oliveira AG, et al.
Acta Tropica, 107(3), 238-241 (2008)

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