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).
Synonym(s):
μ-Calpain
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About This Item
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Quality Level
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.
Native calpain-1 from human erythrocytes. Ca2+-dependent heterodimeric cysteine proteinase with low Ca2+ requirement (EC50= 2 µM).
Packaging
Please refer to vial label for lot-specific concentration.
Warning
Toxicity: Harmful (C)
Unit Definition
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.
Physical form
In 20 mM imidazole, 5 mM β-mercaptoethanol, 1 mM EDTA, 1 mM EGTA, 30% glycerol, pH 6.8.
Preparation Note
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).
Analysis Note
Comparable to reference lot by SDS-PAGE
Other Notes
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
Storage Class Code
10 - Combustible liquids
WGK
WGK 2
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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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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