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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


Certificates of Analysis (COA)

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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)
Cathepsin L expression and regulation in human abdominal aortic aneurysm, atherosclerosis, and vascular cells
Liu J, et al.
Atherosclerosis, 184(2), 302-311 (2006)
Protease signalling: the cutting edge
Turk B, et al.
The Embo Journal, 31(7), 1630-1643 (2012)
Brendan Reed et al.
The Journal of experimental medicine, 218(2) (2020-10-24)
The identification of the peptide epitopes presented by major histocompatibility complex class II (MHCII) molecules that drive the CD4 T cell component of autoimmune diseases has presented a formidable challenge over several decades. In type 1 diabetes (T1D), recent insight

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