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C6108 Sigma-Aldrich

Calpain 1 human

aqueous glycerol solution

Synonym: Calcium-activated neutral protease 1

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Description

Application

Human calpain 1 has been used in a study to assess how the crystal structures of human calpains 1 and 9 imply diverse mechanisms of action and auto-inhibition. Human calpain 1 has also been used in a study to investigate the synthesis, biological evaluation and molecular modelling of N-heterocyclic dipeptide aldehydes as selective calpain inhibitors.

Biochem/physiol Actions

Caplain 1 is a neutral calcium-dependent cysteine protease containing the EF-hand motif. The protease consists of two subunits; the larger subunit has four domains that are homologous with papain and calmodulin. The smaller subunit has one domain that shares homology with calmodulin. It is activated by micromolar levels of calcium and hence, it is also called as micro-calpain. Its activation leads to cellular protein degradation, neuronal cell degeneration, and autoimmune demyelinating diseases such as multiple sclerosis.

Cytosolic protease with involvement in cytoskeletal remodeling, autophagy, and apoptosis as an upstream regulator.

Physical properties

Calpain 1 is a heterodimeric calcium-activated thiol-protease.

Unit Definition

One unit will hydrolyze 1 picomole Suc-LLVY-AMC per minute at 25 deg C.

Physical form

Solution in 20 mM Imidazole-HCl, 5 mM β-Mercaptoethanol, 1 mM EDTA, 1 mM EGTA, and 30% glycerol.

Safety & Documentation

Safety Information

RIDADR 
NONH for all modes of transport
WGK Germany 
WGK 3
Flash Point(F) 
Not applicable
Flash Point(C) 
Not applicable

Documents

Certificate of Analysis (COA)

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Certificate of Origin (COO)

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Protocols & Articles

Articles

Huntington's Disease

Huntington's disease (HD) is an autosomal dominant, late-onset neurodegenerative disorder characterized by a selective neuronal cell death in the cortex and striatum leading to cognitive dysfunction,...
Carolyn L. Crankshaw
BioFiles v7 n2, 2011, 9–14
Keywords: Apoptosis, Huntington Disease, Transcription

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Peer-Reviewed Papers
15

References

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