Cathepsin B (Mouse)

Cathepsin B is the first described member of the family of lysosomal cysteine proteases. Cathepsin B possesses both endopeptidase and exopeptidase activities, in the latter case acting as a peptidyl-dipeptidase. It is known to process a number of proteins, including pro and active caspases, prorenin and SLPI. Cathepsin B is synthesized as a preproenzyme. Following removal of the signal peptide, the inactive proenzyme undergoes further modifications including removal of the pro region to result in the active enzyme.

Image: Cells were scratch-wounded and stained against cathepsin B and annexin-II heterotetramer subunit p11 after 1 (a), 8 (b) and 24 (c) hours. Fixation was performed with both -20^oC cold methanol and acetone for 8 minutes each. Cathepsin B is shown in red, p11 is shown in green.

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