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- W1985273624 abstract "▼It is important for the recent experimental strategies of the molecular biology that gene expression profiles can be detected at the translational level. An antibody that is produced against a recombinant protein is a powerful tool for detecting the gene product. The recombinant protein is usually expressed as a fusion protein that carries a protein tag such as T7, His, maltose-binding protein or glutathione-S-transferase. Antisera or monoclonal antibodies are then raised against the gene product using the fusion protein as an immunogen. However, unfortunately, it is difficult to produce good antibodies that can be used for both immunocytochemistry and western blotting. Much effort has been made to improve the detection of antigens that are difficult to detect on histological sections (Ref. 1), because most antibodies are originally screened by western blotting. However, little is known about how to improve the detection of antigens with western blotting. During the course of producing antisera and monoclonal antibodies against several recombinant proteins, we found that some antibodies recognize the native form of the recombinant proteins by dot-blotting even though they do not recognize the protein bands on western blotting. In this report, we describe an effective and convenient method for restoring their antigenicities on western-blotting membranes. Moreover, we show that, when analysing antibodies, screening only with the usual western blotting can fail to detect some good antibodies that can recognize the native form of the gene product. The method described here will help to increase the efficiency of antibody production." @default.
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- W1985273624 date "2001-01-01" @default.
- W1985273624 modified "2023-09-23" @default.
- W1985273624 title "Improved antigen detection on western blots" @default.
- W1985273624 cites W2020957025 @default.
- W1985273624 cites W2140564918 @default.
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- W1985273624 doi "https://doi.org/10.1016/s1366-2120(08)70163-6" @default.
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