Calpain undergoes translocation between cell compartments during the various steps of the cell cycle. It is among the proteases implicated in apoptosis and the proteasome-ubiquitine pathway of protein degradation.
One unit will produce a ΔA280 of 0.5 in 30 min at pH 7.5 at 30 °C, measured as TCA soluble products using N,N-dimethylated casein as substrate. (Final volume = 1.8 mL, light path = 1 cm.) (Modified from Kawashima, S., et al.)
Forme physique
Lyophilized powder containing lactose, dithiothreitol and tris buffer salts.
Journal of biochemistry, 90(1), 233-240 (1981-07-01)
The structure of the calcium-activated neutral proteinase (CANP) from rabbit skeletal muscle was examined. The purified CANP was homogeneous as judged by disc gel electrophoresis, while it showed two bands (M.W.=80,000 (80 K) and 31,000 (30 K) on SDS-gel electrophoresis.
Journal of biochemistry, 95(1), 95-101 (1984-01-01)
Calcium-activated neutral proteases (CANPs) were purified from rabbit skeletal muscle and chicken skeletal muscle, and compared as to their electrophoretic properties, metal requirements, subunit amino acid compositions and immunological cross-reactivities. Two kinds of CANPs (mu CANP and mCANP) were isolated
Proteolysis is a key event in the control of the cell cycle. Most of the proteins which are degraded at specific cycle points, e.g. cyclins A, B, and E, are substrates of the ubiquitin/proteasome pathway. The Ca2+ dependent neutral protease
Cell biology and toxicology, 14(2), 121-132 (1998-04-29)
Proteolytic cleavage of a limited number of cellular proteins is a central biochemical feature of apoptosis. Aspartate-specific cysteine proteases, the so-called 'caspases', are the main enzymes involved in this process. At least ten homologues of interleukin-1 beta converting enzyme (ICE)
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