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Merck

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).

Synonyme(s) :

μ-Calpain

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A propos de cet article

Numéro CE :
NACRES:
NA.77
UNSPSC Code:
12352202
Specific activity:
≥1000 units/mg protein
Assay:
≥95.0% (SDS-PAGE)
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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

Catégories apparentées

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.

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Disclaimer

Toxicity: Harmful (C)

Classe de stockage

10 - Combustible liquids

wgk

WGK 2


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Consulter la Bibliothèque de documents

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
Michelle M White et al.
EBioMedicine, 23, 173-184 (2017-08-25)
Identification of mechanisms promoting neutrophil trafficking to the lungs of patients with cystic fibrosis (CF) is a challenge for next generation therapeutics. Cholesterol, a structural component of neutrophil plasma membranes influences cell adhesion, a key step in transmigration. The effect
Eshwar R Tammineni et al.
eLife, 12 (2023-02-02)
Calcium ion movements between cellular stores and the cytosol govern muscle contraction, the most energy-consuming function in mammals, which confers skeletal myofibers a pivotal role in glycemia regulation. Chronic myoplasmic calcium elevation ("calcium stress"), found in malignant hyperthermia-susceptible (MHS) patients
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

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