Streptavidin-Aequorin Fusion Protein for Bioluminescent Immunoassay | Zendy

S Inouye | Zendy; Junichi Sato | Zendy; Satoko Sasaki | Zendy; Yuiko Sahara | Zendy

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Streptavidin-Aequorin Fusion Protein for Bioluminescent Immunoassay

Author(s) -

S Inouye,

Junichi Sato,

Satoko Sasaki,

Yuiko Sahara

Publication year - 2011

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.100798

Subject(s) - biotinylation , immunoassay , streptavidin , chemistry , microbiology and biotechnology , fusion protein , analyte , bioluminescence , chromatography , antibody , biotin , biology , biochemistry , recombinant dna , immunology , gene

The fusion protein of streptavidin to aequorin (STA-AQ) was highly purified from inclusion bodies in Escherichia coli cells and applied to a bioluminescent sandwich immunoassay. α-Fetoprotein (AFP), which is a serological marker of liver cancer, was used as a model analyte to test STA-AQ in an immunoassay. The measurable range of AFP by the sandwich immunoassay, using the complex of STA-AQ and the biotinylated anti-AFP antibody, was 0.02-200 ng/mL with an average coefficient of variation of 4.9%. The detection sensitivity with the complex of STA-AQ and the biotinylated anti-AFP antibody was similar to that with the complex of biotinylated aequorin, streptavidin and the biotinylated anti-AFP antibody. STA-AQ would be a useful reporter protein for immunoassays.

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