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Abstract
AI239 and RB95 antibodies against the Glutathione S-transferase (GST) protein recognize a GST-tagged human TAC protein by immunofluorescence in paraformaldehyde-fixed HeLa cells; AF209, AF212 and RB94 do not.
Highlights
Glutathione S-transferase (GST) (Uniprot #P08515) is a large (~215 aa) protein tag, from Schistosoma japonicum, used to affinity-purify GST-fused proteins, given its ability to bind its glutathione substrate with high affinity (Smith and Johnson, 1988)
After 3 washes (10 min) with PBS + 0.2% (w/v) BSA (PBS-BSA), cells were incubated for 30 min in PBS-BSA with secondary goat anti-mouse IgG conjugated to AlexaFluor-647 (1:300, Molecular Probes, #A21235) and, when AJ519 was used for co-localization, goat anti-rabbit IgG conjugated to AlexaFluor-488 (1:300, Molecular Probes #A11034)
AI239 and MRB95 antibodies detected a signal at the plasma membrane in cells transfected with the GST-tagged TAC protein (Fig. 1A)
Summary
Glutathione S-transferase (GST) (Uniprot #P08515) is a large (~215 aa) protein tag, from Schistosoma japonicum, used to affinity-purify GST-fused proteins, given its ability to bind its glutathione substrate with high affinity (Smith and Johnson, 1988). We show that the AI239 and RB95 recombinant antibodies detect a GST-tagged human TAC protein by immunofluorescence in HeLa cells. Facility (www.unige.ch/medecine/antibodies/) as miniantibodies with the antigen-binding scFv fused to a mouse
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