208713
Calpain-1, Human Erythrocytes
Calpain-1, Human Erythrocytes, is a native calpain-1. A heterodimeric cysteine proteinase with low Ca2+ requirement (EC50 = 2 µM).
别名:
μ-Calpain
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Quality Level
assay
≥95.0% (SDS-PAGE)
form
liquid
specific activity
≥1000 units/mg protein
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze, avoid repeated freeze/thaw cycles
shipped in
wet ice
storage temp.
−70°C
General description
Native calpain-1 from human erythrocytes. Ca2+-dependent cysteine proteinase with low Ca2+ requirement (half-maximal activation = 2 µM). Participates in the ATP release reaction of platelets stimulated with thrombin.
Packaging
Please refer to vial label for lot-specific concentration.
Physical form
In 20 mM imidazole, 5 mM β-mercaptoethanol, 1 mM EDTA, 1 mM EGTA, 30% glycerol, pH 6.8.
Preparation Note
Following initial thaw, aliquot and freeze (-70°C).
Prepared from blood that has been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV.
Other Notes
One unit is defined as the amount of enzyme that will hydrolyze 1 pmol Suc-LLVY-AMC in 1 min, 25°C using the Calpain Activity Assay Kit, Fluorogenic (Cat. No. QIA120). Note: 1 caseinolytic unit = 1 fluorogenic unit.
Vanderklish, P.W., and Bahr, B.A. 2000. Int. J. Exp. Pathol.81, 323.
Sorimachi, H., et al. 1997. Biochem. J. 328, 721.
Croall, D.E., and McGrody, K.S. 1994. Biochemistry33, 13223.
Sorimachi, H., et al. 1997. Biochem. J. 328, 721.
Croall, D.E., and McGrody, K.S. 1994. Biochemistry33, 13223.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Disclaimer
Toxicity: Harmful (C)
存储类别
10 - Combustible liquids
wgk
WGK 2
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Kun Xie et al.
Autophagy, 12(2), 381-396 (2016-01-05)
Autophagy and apoptosis, which could be induced by common stimuli, play crucial roles in development and disease. The functional relationship between autophagy and apoptosis is complex, due to the dual effects of autophagy. In the Bombyx Bm-12 cells, 20-hydroxyecdysone (20E)
Peter Tompa et al.
The Journal of biological chemistry, 277(11), 9022-9026 (2002-01-26)
The inhibitory domains of calpastatin contain three highly conserved regions, A, B, and C, of which A and C bind calpain in a strictly Ca(2+)-dependent manner but have no inhibitory activity whereas region B inhibits calpain on its own. We
Courtney Blachford et al.
Cell calcium, 46(4), 257-262 (2009-09-08)
Neuronal calcium sensor-1 (NCS-1) is a high-affinity, low-capacity Ca(2+)-binding protein expressed in many cell types. We previously showed that NCS-1 interacts with inositol 1,4,5-trisphosphate receptor (InsP(3)R) and modulates Ca(2+)-signaling by enhancing InsP3-dependent InsP(3)R channel activity and intracellular Ca(2+) transients. Recently
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| 货号 | GTIN |
|---|---|
| 208713-500UG | 07790788048501 |