Title: The amino-terminal domain of the lamin B receptor is a nuclear envelope targeting signal Document date: 1993_3_1
ID: 377v2ufn_32
Snippet: In unfixed, digitonin-permeabilized cells that were not exposed to Triton X-100 (lower panels), fluorescence was not observed in any cells. In contrast, ceils transfected with AG-LMBR (Fig. 6 c) showed staining in unfixed, digitoninpermeabilized ceils (lower panel) as well as cells fixed and exposed to Triton X-100 (upper panel). These data suggest that in the digitonin-permeabilized cells, the ot-globin-LBR chimeric protein is accessible to anti.....
Document: In unfixed, digitonin-permeabilized cells that were not exposed to Triton X-100 (lower panels), fluorescence was not observed in any cells. In contrast, ceils transfected with AG-LMBR (Fig. 6 c) showed staining in unfixed, digitoninpermeabilized ceils (lower panel) as well as cells fixed and exposed to Triton X-100 (upper panel). These data suggest that in the digitonin-permeabilized cells, the ot-globin-LBR chimeric protein is accessible to antibodies that can pass through the disrupted plasma membrane. LBR and LBRchicken hepatic lectin are apparently not accessible to antibodies in digitonin-permeabilized cells, consistent with a localization of these polypeptides on the inside of the nuclear envelope in the inner nuclear membrane.
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