P4533
Calpain II from rabbit skeletal muscle
lyophilized powder, 15-40 units/mg protein
别名:
Calcium Activated Neutral Protease
生物来源
rabbit skeletal muscle
质量水平
表单
lyophilized powder
比活
15-40 units/mg protein
组成
Protein, 2-10% Lowry
浓度
2-10% protein (Lowry)
UniProt登记号
储存温度
−20°C
基因信息
rabbit ... CAPN2(100009092)
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生化/生理作用
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.
外形
Lyophilized powder containing lactose, dithiothreitol and tris buffer salts.
其他说明
80K subunit of mCANP
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.)
储存分类代码
11 - Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
法规信息
新产品
此项目有
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)
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
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.
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