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C6854

Sigma-Aldrich

Cathepsin L from human liver

≥0.5 units/mg protein, solution

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25 μG
$444.00

$444.00

Estimated to ship onMarch 29, 2025

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25 μG
$444.00

About This Item

CAS Number:
60616-82-2
Enzyme Commission number:
3.4.22.15 (BRENDA, IUBMB)
MDL number:
MFCD00163235
UNSPSC Code:
12352200
NACRES:
NA.32

$444.00

Estimated to ship onMarch 29, 2025

Request a Bulk Order

biological source

human liver

Quality Level

200

form

solution

specific activity

≥0.5 units/mg protein

technique(s)

activity assay: suitable

pH range

4.5—5.5

UniProt accession no.

P07711

application(s)

pharmaceutical

shipped in

dry ice

storage temp.

−20°C

Gene Information

human ... CTSL1(1514)

General description

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.

Application

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 Actions

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.

Unit Definition

One unit will hydrolyze 1.0 μmole of Z-Phe-Arg-AFC per minute at pH 5.5 at 25 °C.

Physical form

Solution in in 20 mM malonate, pH 5.5, 1 mM EDTA, and 400 mM NaCl.

Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

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Certificates of Analysis (COA)

Lot/Batch Number
0000264664
SLCR2105
0000266834
SLCQ7903
SLCP3765

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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.
M Kathryn Liszewski et al.
Immunity, 39(6), 1143-1157 (2013-12-10)
Complement is viewed as a critical serum-operative component of innate immunity, with processing of its key component, C3, into activation fragments C3a and C3b confined to the extracellular space. We report here that C3 activation also occurred intracellularly. We found
Gustavo E Chavarria et al.
European journal of medicinal chemistry, 58, 568-572 (2012-11-22)
Kinetic analysis of the mode of inhibition of cathepsin L by KGP94, a lead compound from a privileged library of functionalized benzophenone thiosemicarbazone derivatives, demonstrated that it is a time-dependent, reversible, and competitive inhibitor of the enzyme. These results are
Dexter N Dean et al.
Biochimica et biophysica acta. Proteins and proteomics, 1867(10), 961-969 (2019-02-05)
The pre-melanosomal protein (Pmel17) aggregates within melanosomes to form functional amyloid fibrils that facilitate melanin polymerization. The repeat domain (RPT) of Pmel17 fibrillates under strict acidic melanosomal pH. Alternative splicing results in a shortened repeat domain (sRPT), which also forms
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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Questions

  1. Hello, What is the protocol to bring this up in solution to have a concentration of 0.5 units/µL? Does units mean µg where the amount needed for performing digestions? Is there a protocol associated with this?

    1 answer

    1. This product is supplied as a solution. The minimum activity for each lot will be ≥0.5 units/mg protein. The specific activity of each lot is reported on the Certificate of Analysis. See the link below to review a sample Certificate:
      https://www.sigmaaldrich.com/certificates/sapfs/PROD/sap/certificate_pdfs/COFA/Q14/C6854-25UGSLCR2105.pdf

      The product is supplied in 20 mM malonate buffer, pH 5.5, with 1 mM EDTA and 400 mM NaCl. One unit is defined as the amount of Cathepsin L that hydrolyzes 1 uM Z-PHE-Arg-AFC per minute at 22 - 25 °C, in 400 mM Sodium Acetate, pH 5.5, containing 4 mM EDTA and 8 mM DTT.

      Please access the product datasheet at the link below:
      https://www.sigmaaldrich.com/deepweb/assets/sigmaaldrich/product/documents/130/380/c6854dat.pdf

      Helpful?

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