219402

Cathepsin L, Human Liver

Name: Cathepsin L, Human Liver
Brand: MM

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.

Synonym(s):

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

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About This Item

EC Number:

3.4.22.15 (BRENDA, IUBMB)

NACRES:

NA.77

UNSPSC Code:

12352202

Product Name

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.

biological source

human liver

description

Merck USA index - 14, 1905

form

liquid

manufacturer/tradename

Calbiochem^®

storage condition

OK to freeze
avoid repeated freeze/thaw cycles

technique(s)

activity assay: suitable

suitability

suitable for molecular biology

application(s)

life science and biopharma

shipped in

wet ice

storage temp.

−70°C

Quality Level

100

Gene Information

human ... CTSL(1514)

Biochem/physiol Actions

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.

Disclaimer

Toxicity: Standard Handling (A)

General description

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.

Other Notes

Note: 1 mU = 1 milliunit

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.

Packaging

Please refer to vial label for lot-specific concentration.

Physical form

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

Preparation Note

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

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

Legal Information

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

Storage Class

12 - Non Combustible Liquids

wgk

WGK 2

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘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

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)

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)

Mutation That Promotes Activation of Trypsinogen Increases Severity of Secretagogue-Induced Pancreatitis in Mice.

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