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- W2088344513 abstract "Insoluble proteins generally do not adsorb to microtitre wells and, therefore, cannot be used as antigens in enzyme-linked immunosorbent assay (ELISA). However, denaturation and solubilization with 2% sodium dodecyl sulphate (SDS) renders these proteins suitable ligands for ELISA. In quantitative ELISA using polyclonal antibodies as primary antibody, comparable results were obtained with native and SDS-denatured protein ligands. The binding of the antibodies to the SDS-treated ligands was completely inhibited by premixing the primary antibody with the corresponding native antigen. Nonspecific binding of primary and secondary antibodies to SDS-treated ligands was not observed. SDS-treated proteins are able to attach to ELISA microwells, retain their antigenic epitopes and do not engender an elevated background. The concentration of SDS-treated proteins required for coating is the same as that of the native proteins." @default.
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- W2088344513 date "2002-12-01" @default.
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- W2088344513 title "Sodium dodecyl sulphate-treated proteins as ligands in ELISA" @default.
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- W2088344513 doi "https://doi.org/10.1016/s0022-1759(02)00214-4" @default.
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