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C6108

Sigma-Aldrich

Calpain 1 human

aqueous glycerol solution

Sinónimos:

Calcium-activated neutral protease 1

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About This Item

Comisión internacional de enzimas:
3.4.22.52 (BRENDA, IUBMB)
Número MDL:
MFCD00217575
Código UNSPSC:
12352204
NACRES:
NA.54

Análisis

≥95% (SDS-PAGE)

formulario

aqueous glycerol solution

actividad específica

≥1000 U/mg

Nº de acceso UniProt

P07384

Condiciones de envío

dry ice

temp. de almacenamiento

−70°C

Información sobre el gen

human ... CAPN1(823)

Aplicación

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.

Acciones bioquímicas o 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.

Propiedades físicas

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

Definición de unidad

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.

inhibidor

Referencia del producto
Descripción
Precios

A6060

Calpain Inhibitor II, powder

Código de clase de almacenamiento

10 - Combustible liquids

Clase de riesgo para el agua (WGK)

WGK 1

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

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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Xuan Zhang et al.
PloS one, 7(2), e31458-e31458 (2012-02-23)
Hepatitis B virus X protein (HBx) plays an important role in the development of hepatocellular carcinoma (HCC). However, the mechanism remains unclear. Recently, we have reported that HBx promotes hepatoma cell migration through the upregulation of calpain small subunit 1
Matthew A Jones et al.
Bioorganic & medicinal chemistry, 16(14), 6911-6923 (2008-06-24)
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
M K Squier et al.
Journal of immunology (Baltimore, Md. : 1950), 158(8), 3690-3697 (1997-04-15)
Apoptosis is the common phenotype of programmed or physiologic cell death, the process used to remove excess or defunct cells during normal tissue maintenance. One of the most studied cell types with respect to apoptosis is the immature T cell
Rebecca M Kandell et al.
ACS nano, 15(12), 20504-20516 (2021-12-07)
Traumatic brain injury (TBI) is a critical public health concern and major contributor to death and long-term disability. After the initial trauma, a sustained secondary injury involving a complex continuum of pathophysiology unfolds, ultimately leading to the destruction of nervous
R Zolfaghari et al.
The Biochemical journal, 241(1), 129-135 (1987-01-01)
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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