C6854
Cathepsin L from human liver
≥0.5 units/mg protein, solution
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About This Item
CAS-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352200
NACRES:
NA.32
Empfohlene Produkte
Biologische Quelle
human liver
Qualitätsniveau
Form
solution
Spezifische Aktivität
≥0.5 units/mg protein
Methode(n)
activity assay: suitable
pH-Bereich
4.5—5.5
UniProt-Hinterlegungsnummer
Anwendung(en)
pharmaceutical
Versandbedingung
dry ice
Lagertemp.
−20°C
Angaben zum Gen
human ... CTSL1(1514)
Allgemeine Beschreibung
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.
Anwendung
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. Wirkung
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.
Einheitendefinition
One unit will hydrolyze 1.0 μmole of Z-Phe-Arg-AFC per minute at pH 5.5 at 25 °C.
Physikalische Form
Solution in in 20 mM malonate, pH 5.5, 1 mM EDTA, and 400 mM NaCl.
Ähnliches Produkt
Lagerklassenschlüssel
10 - Combustible liquids
WGK
WGK 3
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Analysenzertifikate (COA)
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Bing-Jie Lv et al.
Atherosclerosis, 230(1), 100-105 (2013-08-21)
Cathepsin L (CatL), cathepsin K (CatK), and cathepsin V (CatV) are potent elastases implicated in human arterial wall remodeling. Whether plasma levels of these cathepsins are altered in patients with abdominal aortic aneurysms (AAAs) remains unknown. Plasma samples were collected
Stefan Tholen et al.
Cellular and molecular life sciences : CMLS, 71(5), 899-916 (2013-07-03)
Endolysosomal cysteine cathepsins functionally cooperate. Cathepsin B (Ctsb) and L (Ctsl) double-knockout mice die 4 weeks after birth accompanied by (autophago-) lysosomal accumulations within neurons. Such accumulations are also observed in mouse embryonic fibroblasts (MEFs) deficient for Ctsb and Ctsl.
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
M Hafner Česen et al.
Cell death & disease, 4, e818-e818 (2013-10-05)
A sigma-2 receptor agonist siramesine has been shown to trigger cell death of cancer cells and to exhibit a potent anticancer activity in vivo. However, its mechanism of action is still poorly understood. We show that siramesine can induce rapid
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
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