SCP0108
Cathepsin B Substrate
≥95% (HPLC), lyophilized
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About This Item
Formule empirique (notation de Hill):
C26H36N10O6
Poids moléculaire :
584.63
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.32
Produits recommandés
product name
Cathepsin B Substrate, colorimetric,
Pureté
≥95% (HPLC)
Forme
lyophilized
Composition
Peptide Content, ≥80%
Conditions de stockage
protect from light
Température de stockage
−20°C
Amino Acid Sequence
Z-Arg-Arg-pNA
Description générale
Cathepsin B, a bilobal protein, belongs to the papain-like family of cysteine proteases. It is produced as a preproenzyme. Its catalytic site is present at the interface between the two lobes. Cathepsin B has an occluding loop. It is located in the secretory vesicles of the neuronal cells. Active cathepsin B is found in the endosomal or lysosomal compartment under normal physiological conditions.
Actions biochimiques/physiologiques
Cathepsin B is a lysosomal cysteine proteinase that metabolizes important molecules such as β-amyloid precursor protein into harmless fragments. Cathepsin B may be detected using the chromogenic substrate Z-Arg-Arg-pNA (z-arg-arg-p-nitroanalide) or flourogenic substrate Z-Arg-Arg-AMC (z-Arg-Arg-amino-4-methylcoumarin).
Cathepsin B possesses endopeptidase and exopeptidase activity. Active cathepsin B is mostly engaged in intracellular and extracellular protein turnover, which helps cells maintain homeostatic metabolic activity. It also participates in the regulation of pro-hormone and pro-enzyme activation, antigen processing, inflammatory reactions against antigens, tissue remodeling, and apoptosis. Cathepsin B plays a key role in acute pancreatitis. It also plays a vital role in lipid metabolism in atherosclerosis.
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
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Les clients ont également consulté
Cathepsin B: Basis Sequence: Mouse.
Dora Cavallo-Medved et al.
The AFCS-nature molecule pages, 2011 (2011-01-01)
S Hasnain et al.
The Journal of biological chemistry, 268(1), 235-240 (1993-01-05)
The pH dependence of cathepsin B-catalyzed hydrolyzes is very complex. At least seven dissociable groups are involved in the binding and hydrolysis of 7-amido-4-methyl coumarin and p-nitroaniline (pNA)-based substrates containing a P1 Arg and either a Phe or Arg at
Yasuhito Sako et al.
Experimental parasitology, 127(3), 693-701 (2010-11-26)
Cysteine peptidases have potent activities in the pathogenesis of various parasitic infections, and are considered as targets for chemotherapy and antigens for vaccine. In this study, two cathepsin B-like cysteine peptidases (EmCBP1 and EmCBP2) from Echinococcus multilocularis metacestodes were identified
Ilaria Giusti et al.
Neoplasia (New York, N.Y.), 10(5), 481-488 (2008-05-14)
Vesicles shed by cancer cells are known to mediate several tumor-host interactions. Tumor microenvironment may, in turn, influence the release and the activity of tumor-shed microvesicles. In this study, we investigated the molecular mediators of the pH-dependent proinvasive activity of
Angela J Eykelbosh et al.
Comparative biochemistry and physiology. Part A, Molecular & integrative physiology, 156(2), 218-223 (2010-02-23)
This study presents evidence that cathepsin B, a lysosomal protease, may be involved in the regulation of apoptosis during serum-starvation in teleost follicles. Zebrafish vitellogenic follicles were isolated, incubated under serum-free conditions and homogenized. The follicle extracts demonstrated caspase-3-like activity
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