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Safety Information

SCP0110

Sigma-Aldrich

Cathepsin L Inhibitor

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About This Item

Empirical Formula (Hill Notation):
C35H59N11O5
Molecular Weight:
713.91
UNSPSC Code:
12352200
NACRES:
NA.32

Assay

≥95% (HPLC)

form

lyophilized

composition

Peptide Content, ≥55%

storage condition

protect from light

storage temp.

−20°C

Amino Acid Sequence

Arg-Lys-Leu-Leu-Trp-NH2

General description

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).

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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  1. Which document(s) contains shelf-life or expiration date information for a given product?

    If available for a given product, the recommended re-test date or the expiration date can be found on the Certificate of Analysis.

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  5. Do you have any references for product SCP0110, Cathepsin L Inhibitor?

    Product SCP0110, Cathepsin L inhibitor peptide has the sequence Arg-Lys-Leu-Leu-Trp-NH2, which can be abbreviated RKLLW-NH2.See the following paper for reference: A. Brinker, et al.: Eur. J. Biochem., 267(16), 5085-5092 (2000). Highly potent inhibitors of human cathepsin L identified by screening combinatorial pentapeptide amide collections.

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Cathepsin L is significantly associated with apoptosis and plaque destabilization in human atherosclerosis
Li W, et al.
Atherosclerosis, 202(1), 92-102 (2009)
Cathepsin L expression and regulation in human abdominal aortic aneurysm, atherosclerosis, and vascular cells
Liu J, et al.
Atherosclerosis, 184(2), 302-311 (2006)
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
Protease signalling: the cutting edge
Turk B, et al.
The Embo Journal, 31(7), 1630-1643 (2012)
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

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