C6854
Cathepsin L from human liver
≥0.5 units/mg protein, solution
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A propos de cet article
Numéro CAS:
UNSPSC Code:
12352200
NACRES:
NA.32
MDL number:
Specific activity:
≥0.5 units/mg protein
Biological source:
human liver
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Laissez-nous vous aiderNom du produit
Cathepsin L from human liver, ≥0.5 units/mg protein, solution
biological source
human liver
form
solution
specific activity
≥0.5 units/mg protein
technique(s)
activity assay: suitable
pH range
4.5—5.5
UniProt accession no.
application(s)
pharmaceutical
shipped in
dry ice
storage temp.
−20°C
Quality Level
Gene Information
human ... CTSL1(1514)
Application
Cathepsin L (CTSL) from human liver has been used:
- to digest mutant transforming growth factor β-induced (TGFBIp) and LC3 (autophagosomes marker) proteins in vitro
- to digest the pH-dependent fibril of a pre-melanosomal protein (Pmel17) repeat domain (RPT) isoform and study the effect of pH on sRPT aggregation kinetics by tryptophan fluorescence
- to analyze the inhibition of CTSL by small molecules or drugs in a cell-free system
Biochem/physiol Actions
Cathepsin L (CTSL) exhibits endopeptidase activity and breaks peptide bonds with aromatic residues. This enzyme is functional at pH 3.0–6.5 with thiol compounds. Elastin, collagen, and α-1 protease inhibitors act as substrates for cathepsin L (CTSL). CTSL cleaves several proteins including enzymes, receptors, and transcription factors. It is involved in antigenic peptide production and controls B-cells homeostasis. It is associated with myofibril necrosis and tumor progression. Increased expression of CTSL promotes metastasis and relates to poor prognosis in cancer patients. Increased expression of CTSL is observed in breast cancer. CTSL is implicated in glioblastoma multiforme (GBM), middle east respiratory syndrome (MERS), gingival overgrowth, and severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). It has a higher specific activity than cathepsin B and H in the degradation of a variety of physiological protein substrates.
General description
The cathepsin L (CTSL) gene is mapped to human chromosome 9q21.33. It encodes a lysosomal cysteine proteinase that belongs to the peptidase C1 family. The enzyme is a dimer of a heavy (175 amino acids) and a light chain (42 amino acids) linked by disulfide bonds.
Other Notes
One unit will hydrolyze 1.0 μmole of Z-Phe-Arg-AFC per minute at pH 5.5 at 25 °C.
Physical form
Solution in in 20 mM malonate, pH 5.5, 1 mM EDTA, and 400 mM NaCl.
Classe de stockage
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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Gustavo E Chavarria et al.
European journal of medicinal chemistry, 58, 568-572 (2012-11-22)
Kinetic analysis of the mode of inhibition of cathepsin L by KGP94, a lead compound from a privileged library of functionalized benzophenone thiosemicarbazone derivatives, demonstrated that it is a time-dependent, reversible, and competitive inhibitor of the enzyme. These results are
Dexter N Dean et al.
Biochimica et biophysica acta. Proteins and proteomics, 1867(10), 961-969 (2019-02-05)
The pre-melanosomal protein (Pmel17) aggregates within melanosomes to form functional amyloid fibrils that facilitate melanin polymerization. The repeat domain (RPT) of Pmel17 fibrillates under strict acidic melanosomal pH. Alternative splicing results in a shortened repeat domain (sRPT), which also forms
M Kathryn Liszewski et al.
Immunity, 39(6), 1143-1157 (2013-12-10)
Complement is viewed as a critical serum-operative component of innate immunity, with processing of its key component, C3, into activation fragments C3a and C3b confined to the extracellular space. We report here that C3 activation also occurred intracellularly. We found
Bailey Miller et al.
Journal of natural products, 77(1), 92-99 (2013-12-25)
A number of marine natural products are potent inhibitors of proteases, an important drug target class in human diseases. Hence, marine cyanobacterial extracts were assessed for inhibitory activity to human cathepsin L. Herein, we have shown that gallinamide A potently
Violeta Morin et al.
PloS one, 7(11), e46850-e46850 (2012-11-13)
Proteolysis of sperm histones in the sea urchin male pronucleus is the consequence of the activation at fertilization of a maternal cysteine protease. We previously showed that this protein is required for male chromatin remodelling and for cell-cycle progression in
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