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Key Documents

C6108

Sigma-Aldrich

Calpain 1 human

aqueous glycerol solution

Sinônimo(s):

Calcium-activated neutral protease 1

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About This Item

Número da licença da enzima:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.54

Ensaio

≥95% (SDS-PAGE)

forma

aqueous glycerol solution

atividade específica

≥1000 U/mg

nº de adesão UniProt

Condições de expedição

dry ice

temperatura de armazenamento

−70°C

Informações sobre genes

human ... CAPN1(823)

Aplicação

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.

Ações bioquímicas/fisiológicas

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.

propriedades físicas

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

Definição da unidade

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

forma física

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

inibidor

Nº do produto
Descrição
Preços

Código de classe de armazenamento

10 - Combustible liquids

Classe de risco de água (WGK)

WGK 1

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


Certificados de análise (COA)

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A series of N-heterocyclic dipeptide aldehydes 4-13 have been synthesised and evaluated as inhibitors of ovine calpain 1 (o-CAPN1) and ovine calpain 2 (o-CAPN2). 5-Formyl-pyrrole 9 (IC(50) values of 290 and 25nM against o-CAPN1 and o-CAPN2, respectively) was the most
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A high-Mr neutral endopeptidase-24.5 (NE) that cleaved bradykinin at the Phe5-Ser6 bond was purified to apparent homogeneity from human lung by (NH4)2SO4 fractionation, ion-exchange chromatography and gel filtration. The final enzyme preparation produced a single enzymically active protein band after
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