SCP0110
Cathepsin L Inhibitor
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About This Item
Formule empirique (notation de Hill):
C35H59N11O5
Poids moléculaire :
713.91
Code UNSPSC :
12352200
Nomenclature NACRES :
NA.32
Produits recommandés
Pureté
≥95% (HPLC)
Forme
lyophilized
Composition
Peptide Content, ≥55%
Conditions de stockage
protect from light
Température de stockage
−20°C
Amino Acid Sequence
Arg-Lys-Leu-Leu-Trp-NH2
Description générale
Cathepsin L Inhibitor is a histone H3-processing enzyme. It is important for maintaining epidermal homeostasis, regular hair follicle morphogenesis and cycling. Cathepsin L is involved in protein degradation. It might regulate normal functioning of the immune system. Cathepsin L regulates the death of macrophages, necrotic core formation and development of atherosclerotic plaque instability.
Application
Cathepsin L is a lysosomal cysteine proteinase that metabolizes collagens and elastins. The roles and activity of Cathepsin L can be studied with the aid of peptide inhibitors such as the pentapeptide amide RKLLW-NH2 (Arg-Lys-Leu-Leu-Trp-NH2).
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
A Brinker et al.
European journal of biochemistry, 267(16), 5085-5092 (2000-08-10)
By screening a combinatorial pentapeptide amide collection in an inhibition assay, we systematically evaluated the potential of 19 proteinogenic amino acids and seven nonproteinogenic amino acids to serve as building blocks for inhibitors of human cathepsin L. Particularly efficient were
Cathepsin L is significantly associated with apoptosis and plaque destabilization in human atherosclerosis
Li W, et al.
Atherosclerosis, 202(1), 92-102 (2009)
Protease signalling: the cutting edge
Turk B, et al.
The Embo Journal, 31(7), 1630-1643 (2012)
Cathepsin L expression and regulation in human abdominal aortic aneurysm, atherosclerosis, and vascular cells
Liu J, et al.
Atherosclerosis, 184(2), 302-311 (2006)
V Turk et al.
The EMBO journal, 20(17), 4629-4633 (2001-09-05)
From their discovery in the first half of the 20th century, lysosomal cysteine proteases have come a long way: from being the enzymes non-selectively degrading proteins in lysosomes to being those responsible for a number of important cellular processes. Some
Notre équipe de scientifiques dispose d'une expérience dans tous les secteurs de la recherche, notamment en sciences de la vie, science des matériaux, synthèse chimique, chromatographie, analyse et dans de nombreux autres domaines..
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