A7294
Avidin–Alkaline Phosphatase
buffered aqueous solution
Synonym(s):
Avidin–AP
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About This Item
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biological source
avidin from egg white
enzyme from bovine (calf) intestine
conjugate
alkaline phosphatase conjugate
form
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
shipped in
wet ice
storage temp.
2-8°C
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General description
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.
Biochem/physiol Actions
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.
Physical form
Solution in 0.05 M Tris buffer, pH 8.0, containing 1% bovine serum albumin, 1 mM MgCl2 and 15 mM sodium azide.
Preparation Note
Affinity purified protein conjugated to alkaline phosphatase using 0.2% glutaraldehyde.
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.
Storage Class Code
10 - Combustible liquids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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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(Strept)avidin-Biotin Systems
Bioconjugate Techniques, 465-505 (2013)
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
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)
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
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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