Cathepsin L Antibody#71298,Cell Signaling Technology (CST),71298

Cathepsin L Antibody recognizes endogenous levels of total cathepsin L protein. This antibody detects full-length cathepsin L pro-enzyme in addition to the processed (active) form of cathepsin L.

Reactivity

Human, Monkey

Application

Western Blotting: 1:1000

Platform ID

BAB405405985

Cell Signaling Technology (CST)

Headquarters

3 Trask Lane Danvers, MA 01923

Contact

Tel: 877-616-2355,978-867-2388
Fax: 877-616-2355

Product Specifications
Scientific Background
Synonyms

Specifications

NameCathepsin L Antibody#71298
Cat. No.71298
Accession NumberP07711
Gene ID (Entrez)07711, 1514
SensitivityEndogenous
ReactivityHuman, Monkey
ApplicationWestern Blotting: 1:1000
Molecular Weight25-42
FormulationSupplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C.Do not aliquot the antibody.
StorageSupplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C.Do not aliquot the antibody.
Regulatory StatusResearch Use Only

Scientific Background

Cathepsin L belongs to the C1 family of peptidases, a large and diverse family of cysteine (thiol) proteases that play fundamental roles in protein processing and degradation. The catalytic activity of C1 peptidases maps to a nucleophilic cysteine thiol, usually found within a catalytic dyad or triad (1). Cathepsin L, initially synthesized as procathepsin L before undergoing proteolytic cleavage to its active form, is a ubiquitously expressed thiol protease, expressed primarily in lysosomes but which is also secreted by some cell types. Its diverse functions include general protein catabolism and autophagy (2), antigen processing (3), promoting angiogenesis (4), and extracellular matrix degradation (5,6). An isoform of cathepsin L has also been reported in the nucleus, where it was shown to be involved in the regulation of transcription factor activity (7). Targeted deletion of theCtslgene in mice embryos was non-lethal, but resulted in periodic hair loss and skin defects, including epidermal hyperplasia, acanthosis, and hyperkeratosis (8). More recently, research studies have reported that cathepsin L is involved in viral protein processing during viral replication, and that cathepsin L inhibitors may have utility in combating infection by SARS-CoV-2 and related coronaviruses (9).Rawlings, N.D. et al. (2018)Nucleic Acids Res46, D624-D632.Kaminskyy, V. and Zhivotovsky, B. (2012)Biochim Biophys Acta1824, 44-50.Nakagawa, T. et al. (1998)Science280, 450-3.Pan, T. et al. (2020)Gastric Cancer23, 974-987.Dykes, S.S. et al. (2019)Oncotarget10, 5560-5568.Felbor, U. et al. (2000)EMBO J19, 1187-94.Burton, L.J. et al. (2017)Mol Cell Biol37, e00297-16. doi: 10.1128/MCB.00297-16.Roth, W. et al. (2000)FASEB J14, 2075-86.Zhao, M.M. et al. (2021)Signal Transduct Target Ther6, 134.Alternate Namescathepsin L; Cathepsin L1; Cathepsin L1 heavy chain; Cathepsin L1 light chain; CATL; CATL1; CTSL; CTSL1; FLJ31037; Major excreted protein; MEP; Procathepsin L

Synonyms

cathepsin L; Cathepsin L1; Cathepsin L1 heavy chain; Cathepsin L1 light chain; CATL; CATL1; CTSL; CTSL1; FLJ31037; Major excreted protein; MEP; Procathepsin L

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