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SCP0110

Sigma-Aldrich

Cathepsin L Inhibitor

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About This Item

Empirische Formel (Hill-System):
C35H59N11O5
Molekulargewicht:
713.91
UNSPSC-Code:
12352200
NACRES:
NA.32

Assay

≥95% (HPLC)

Form

lyophilized

Zusammensetzung

Peptide Content, ≥55%

Lagerbedingungen

protect from light

Lagertemp.

−20°C

Amino Acid Sequence

Arg-Lys-Leu-Leu-Trp-NH2

Allgemeine Beschreibung

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.

Anwendung

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).

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


Analysenzertifikate (COA)

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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)
Cathepsin L is significantly associated with apoptosis and plaque destabilization in human atherosclerosis
Li W, et al.
Atherosclerosis, 202(1), 92-102 (2009)
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
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

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