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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About This Item
Produits recommandés
Niveau de qualité
Forme
liquid
Activité spécifique
≥1000 units/mg protein
Fabricant/nom de marque
Calbiochem®
Conditions de stockage
OK to freeze
avoid repeated freeze/thaw cycles
Conditions d'expédition
wet ice
Température de stockage
−70°C
Description générale
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.
Native calpain-1 from human erythrocytes. Ca2+-dependent heterodimeric cysteine proteinase with low Ca2+ requirement (EC50= 2 µM).
Conditionnement
Please refer to vial label for lot-specific concentration.
Avertissement
Toxicity: Harmful (C)
Définition de l'unité
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.
Forme physique
In 20 mM imidazole, 5 mM β-mercaptoethanol, 1 mM EDTA, 1 mM EGTA, 30% glycerol, pH 6.8.
Notes préparatoires
Prepared from blood that has been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV.
Reconstitution
Following initial thaw, aliquot and freeze (-70°C).
Remarque sur l'analyse
Comparable to reference lot by SDS-PAGE
Autres remarques
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.
Informations légales
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 2
Certificats d'analyse (COA)
Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".
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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans 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
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
Olav A Gressner et al.
Journal of cellular and molecular medicine, 12(6B), 2717-2730 (2008-02-13)
Recently, synthesis and secretion of connective tissue growth factor (CTGF)/CYR61/CTGF/NOV-family member 2 (CCN2) in cultures of hepatocytes were shown, which are sensitively up-regulated by exogenous TGF-beta. In this study TGF-beta-dependent CTGF/CCN2 expression in hepatocytes cultured under completely TGF-beta-free conditions was
Joanna M Norman et al.
Autophagy, 6(8), 1042-1056 (2010-12-02)
It is becoming increasingly clear that there is crosstalk between the apoptotic and autophagic pathways, with autophagy helping to contribute to cell death by providing energy to allow the energy-requiring programmed cell death process to complete, as well as degrading
Pimthanya Wanichawan et al.
The Journal of biological chemistry, 289(49), 33984-33998 (2014-10-23)
Cardiac sodium (Na(+))-calcium (Ca(2+)) exchanger 1 (NCX1) is central to the maintenance of normal Ca(2+) homeostasis and contraction. Studies indicate that the Ca(2+)-activated protease calpain cleaves NCX1. We hypothesized that calpain is an important regulator of NCX1 in response to
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