P4533
Calpain II from rabbit skeletal muscle
lyophilized powder, 15-40 units/mg protein
Synonym(s):
Calcium Activated Neutral Protease
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352202
Recommended Products
biological source
rabbit skeletal muscle
Quality Level
form
lyophilized powder
specific activity
15-40 units/mg protein
composition
Protein, 2-10% Lowry
concentration
2-10% protein (Lowry)
UniProt accession no.
storage temp.
−20°C
Gene Information
rabbit ... CAPN2(100009092)
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Biochem/physiol Actions
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.
Other Notes
80K subunit of mCANP
Unit Definition
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.)
Physical form
Lyophilized powder containing lactose, dithiothreitol and tris buffer salts.
inhibitor
Product No.
Description
Pricing
substrate
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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S Tsuji et al.
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.
L Santella et al.
Cell calcium, 23(2-3), 123-130 (1998-05-28)
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
S Kawashima et al.
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
E Solary et al.
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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