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208713

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Calpain-1, Human Erythrocytes

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

Sinónimos:

μ-Calpain

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About This Item

Comisión internacional de enzimas:
UNSPSC Code:
12352202
NACRES:
NA.77

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

Categorías relacionadas

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.

Legal Information

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

Storage Class

10 - Combustible liquids

wgk_germany

WGK 2


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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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
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
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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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
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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