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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.

Sinónimos:

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

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About This Item

Comisión internacional de enzimas:
Código UNSPSC:
12352202
NACRES:
NA.77

origen biológico

human liver

Nivel de calidad

descripción

Merck USA index - 14, 1905

Formulario

liquid

fabricante / nombre comercial

Calbiochem®

condiciones de almacenamiento

OK to freeze
avoid repeated freeze/thaw cycles

técnicas

activity assay: suitable

idoneidad

suitable for molecular biology

aplicaciones

life science and biopharma

Condiciones de envío

wet ice

temp. de almacenamiento

−70°C

Información sobre el gen

human ... CTSL(1514)

Descripción general

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.

Acciones bioquímicas o fisiológicas

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.

Envase

Please refer to vial label for lot-specific concentration.

Advertencia

Toxicity: Standard Handling (A)

Definición de unidad

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.

Forma física

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

Nota de preparación

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

Reconstitución

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

Otras notas

Note: 1 mU = 1 milliunit

Información legal

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

Código de clase de almacenamiento

12 - Non Combustible Liquids

Clase de riesgo para el agua (WGK)

WGK 2


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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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
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)
Cathepsin L
Kirschke H
Handbook of Proteolytic Enzymes, 2.0, 1808-1817 (2013)
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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