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Merck

P4533

Sigma-Aldrich

Calpain II from rabbit skeletal muscle

lyophilized powder, 15-40 units/mg protein

Sinónimos:

Calcium Activated Neutral Protease

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About This Item

Número de CAS:
Comisión internacional de enzimas:
MDL number:
UNSPSC Code:
12352202

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

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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[1]

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.

Substrate

Referencia del producto
Descripción
Precios

inhibitor

Referencia del producto
Descripción
Precios

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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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)
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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