A7294
Avidin–Alkaline Phosphatase
buffered aqueous solution
Sinônimo(s):
Avidin–AP
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1 ML
R$ 4.094,00
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1 ML
R$ 4.094,00
About This Item
Produtos recomendados
fonte biológica
avidin from egg white
enzyme from bovine (calf) intestine
conjugado
alkaline phosphatase conjugate
Formulário
buffered aqueous solution
técnica(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
Condições de expedição
wet ice
temperatura de armazenamento
2-8°C
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Descrição geral
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.[1] It is an attractive adaptor protein, that is resistant to denaturation.[2] This glycoprotein is present in avian, reptilian and amphibian egg white.[3] 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[4]. The use of avidin-biotin immunoassay enhances the sensitivity of the technique and facilitates the detection of antigens in low quantities.
Aplicação
Avidin-Alkaline Phosphatase has been used for ELISA[5][6]. The product can also be used for western blot at 1:150,000-1:300,000 dilutions.
Cytokine ELISA Assays were performed using a biotinylated anti-IL-2 antibody and alkaline phosphatase avidin. [9]
Ações bioquímicas/fisiológicas
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.[3]
forma física
Solution in 0.05 M Tris buffer, pH 8.0, containing 1% bovine serum albumin, 1 mM MgCl2 and 15 mM sodium azide.
Nota de preparo
Affinity purified protein conjugated to alkaline phosphatase using 0.2% glutaraldehyde.
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.
Código de classe de armazenamento
10 - Combustible liquids
Classe de risco de água (WGK)
WGK 3
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
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(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
Françoise Immel et al.
PloS one, 11(5), e0154264-e0154264 (2016-05-24)
The zebra mussel Dreissena polymorpha is a well-established invasive model organism. Although extensively used in environmental sciences, virtually nothing is known of the molecular process of its shell calcification. By describing the microstructure, geochemistry and biochemistry/proteomics of the shell, the
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)
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)
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