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. Author manuscript; available in PMC: 2017 Aug 1.
Published in final edited form as: Biochim Biophys Acta. 2016 May 4;1862(8):1433–1442. doi: 10.1016/j.bbadis.2016.05.003

Fig. 6.

Fig. 6

Immunoblot analysis of cysteine protease cleavage activity in the Lop/+ lens (P7). A) Pro-caspase 12 cleavage products were mildly elevated in Lop/+ lenses compared with wild-type. ** denotes suspected partial cleavage products (∼ 48 kDa), * denotes fully cleaved product (42 kDa). The signal intensity of fully cleaved caspase 12 in the Lop/+ lens, normalized to β-actin, was approximately 1.5-fold greater than that of wild-type. B) αII-spectrin cleavage was greatly increased in the Lop/+ lens compared with wild-type consistent with calpain activation. * denotes cleavage products of 150 kDa and 145 kDa. The normalized (β-actin) signal intensities of these αII-spectrin cleavage products in the Lop/+ lens was over 30-fold greater than those of wild-type. M, molecular weight markers.