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219402

Sigma-Aldrich

Cathepsin L, Human Liver

Cathepsin L, Human Liver, CAS 60616-82-2, is a native, the most potent of all the lysosomal proteinases. Plays a major role in the proteolysis of both cellular and endocytosed macromolecules.

Synonyme(s) :

CTSL, CTSL1, Human Cathepsin L, Major excreted protein (MEP)

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About This Item

Numéro de classification (Commission des enzymes):
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.77

Source biologique

human liver

Niveau de qualité

Forme

liquid

Fabricant/nom de marque

Calbiochem®

Conditions de stockage

OK to freeze
avoid repeated freeze/thaw cycles

Technique(s)

activity assay: suitable

Adéquation

suitable for molecular biology

Application(s)

life science and biopharma

Conditions d'expédition

wet ice

Température de stockage

−70°C

Informations sur le gène

human ... CTSL(1514)

Description générale

Research area: Cell Signaling
Cathepsin L, Human Liver, native, is the most potent of all the lysosomal proteinases. Cathepsin L (CTSL) belongs to the papain subfamily of cysteine proteases and is mainly located in endolysosomal vesicles.

Actions biochimiques/physiologiques

Cathepsin L (CTSL) has higher activity than cathepsins B and H in the degradation of a variety of physiological protein substrates. It is believed to be responsible for the generation of endostatin from the NC1 domain in collagen XVII. It is responsible for regulating cell cycle, nucleotide-binding domain, leucine-rich–containing family, pyrin domain–containing-3 (NLRP3) inflammasome activation, proteolytic processing of Bid during apoptosis, and TGF-β signaling. It can degrade a wide range of proteins, encompassing enzymes, receptors, and transcription factors. Additionally, it produces active enzymes, receptors, and biologically active peptides through controlled proteolysis. Moreover, Cathepsin L has been observed to enhance tumor cell migration by lowering cell-cell adhesion and breaking down elements of the extracellular matrix. The expression of CTSL escalates in several types of cancers, including glioma, melanoma, pancreatic, prostate, and breast cancer. It plays a major role in the proteolysis of both cellular and endocytosed macromolecules.

Conditionnement

Please refer to vial label for lot-specific concentration.

Avertissement

Toxicity: Standard Handling (A)

Définition de l'unité

One unit is defined as the amount of enzyme that will hydrolyze 1.0 µmol of Z-FR-AFC per min at 25°C, pH 5.5.

Forme physique

In 400 mM NaCl, 20 mM malonate buffer, 1 mM EDTA, pH 5.5.

Notes préparatoires

Prepared from tissue of individuals that have been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV.

Reconstitution

Following initial thaw, aliquot and freeze (-70°C).

Autres remarques

Note: 1 mU = 1 milliunit

Informations légales

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 2


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

Tulasi Yadati et al.
Cells, 9(7) (2020-07-17)
Cathepsins are the most abundant lysosomal proteases that are mainly found in acidic endo/lysosomal compartments where they play a vital role in intracellular protein degradation, energy metabolism, and immune responses among a host of other functions. The discovery that cathepsins
Cathepsin L
Kirschke H
Handbook of Proteolytic Enzymes, 2.0, 1808-1817 (2013)
Targeting Cathepsin L in Cancer Management: Leveraging Machine Learning, Structure-Based Virtual Screening, and Molecular Dynamics Studies
Almalki AA, et al.
International Journal of Molecular Sciences, 24(24), 17208-17208 (2023)
Blockage of Lysosomal Degradation Is Detrimental to Cancer Cell Survival: Role of Autophagy Activation
Schwartz-Roberts JL and Clarke R
Autophagy: Cancer, Other Pathologies, Inflammation, Immunity, Infection, and Aging, 121-133 (2015)
Zsanett Jancsó et al.
Gastroenterology, 158(4), 1083-1094 (2019-11-22)
Mutations in the human serine protease 1 gene (PRSS1), which encodes cationic trypsinogen, can accelerate its autoactivation and cause hereditary or sporadic chronic pancreatitis. Disruption of the locus that encodes cationic trypsinogen in mice (T7) causes loss of expression of

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