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. 2012 Mar 29;8(3):e1002638. doi: 10.1371/journal.ppat.1002638

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(A) Treatment of stably-transfected HT1080 cells overexpressing HA-tagged rNlrp1 proteins with LT (1 µg/ml) for 5 h followed by lysis and Western blotting with anti-HA and anti-Mek3 antibodies. Full length and cleaved HA-tagged rNlrp1 are shown. The central panel shows full length and cleaved MEK3 (in a reprobing of the same gel). Cleavage of rNlrp1 leads to appearance of the 6-kDa HA-reactive band. Cleavage of endogenous MEK3 leads to a shift in mobility. (B) Sucrose lysates from stably-transfected HT1080 cells overexpressing HA-tagged rNlrp1 proteins were treated with LF (1 or 10 µg/ml) for 3 h, and subjected to Western blotting with anti-HA (top row) or anti-MEK3 antibody (second row). Cleavage of rNlrp1 leads to loss of the N-terminal HA epitope, and cleavage of endogenous MEK3 leads to a shift in mobility. (C) IP (anti-HA pulldown) followed by anti-HA Western blotting of lysates from HT1080 cells expressing HA-tagged rNlrp1 following treatment with LF (10 µg/ml, 3.5 h). Anti-HA reactive cross-reactive bands not marked as HA-Nlrp1 also appear in vector-transfected controls (data not shown).