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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).

Synonym(s):

μ-Calpain

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About This Item

EC Number:
NACRES:
NA.77
UNSPSC Code:
12352202

Product Name

Calpain-1, Human Erythrocytes, Calpain-1, Human Erythrocytes, is a native calpain-1. A heterodimeric cysteine proteinase with low Ca2+ requirement (EC50 = 2 µM).

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

Quality Level

Analysis Note

Comparable to reference lot by SDS-PAGE

Disclaimer

Toxicity: Harmful (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.

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.

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.

Legal Information

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

Storage Class

10 - Combustible liquids

wgk

WGK 2


Certificates of Analysis (COA)

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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
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)
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
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
Bruno Becker et al.
Molecular neurodegeneration, 13(1), 47-47 (2018-08-31)
Neurogranin (Ng) is a small 7.6 kDa postsynaptic protein that has been detected at elevated concentrations in cerebrospinal fluid (CSF) of patients with Alzheimer's disease (AD), both as a full-length molecule and as fragments from its C-terminal half. Ng is involved

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