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Recombinant Mouse Cathepsin L Protein, CF

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Product Details

Summary
Reactivity MuSpecies Glossary
Applications Enzyme Activity
Format
Carrier-Free

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Recombinant Mouse Cathepsin L Protein, CF Summary

Details of Functionality
Measured by its ability to cleave the fluorogenic peptide substrate Z-LR-AMC (Catalog # ES008). The specific activity is >5,000 pmol/min/µg, as measured under the described conditions.
Source
Mouse myeloma cell line, NS0-derived mouse Cathepsin L protein
Thr18-Asn334, with a C-terminal 10-His tag
Accession #
N-terminal Sequence
Thr18
Structure / Form
Pro form
Protein/Peptide Type
Recombinant Enzymes
Gene
Ctsl
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Enzyme Activity
Theoretical MW
37 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
35-40 kDa, reducing conditions
Publications
Read Publications using
1515-CY in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after opening.
Buffer
Supplied as a 0.2 μm filtered solution in Tris and NaCl.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Assay Procedure
  • Activation Buffer: 50 mM Sodium Citrate, 150 mM NaCl, 1 mM EDTA, 0.615% CHAPS, pH 3.0
  • Assay Buffer: 25 mM MES, 5 mM DTT, pH 6.0
  • Recombinant Mouse Cathepsin L (rmCathepsin L) (Catalog # 1515-CY)
  • Substrate: Z-Leu-Arg-AMC (Catalog # ES008), 10 mM stock in DMSO
  • F16 Black Maxisorp Plate (Nunc, Catalog # 475515)
  • Fluorescent Plate Reader (Model: SpectraMax Gemini EM by Molecular Devices) or equivalent
  1. Activate rmCathepsin L at 100 µg/mL in Activation Buffer.
  2. Incubate at room temperature for 60 minutes.
  3. Dilute activated rmCathepsin L to 0.05 ng/µL in Assay Buffer.
  4. Dilute Substrate to 20 µM in Assay Buffer.
  5. In a plate load 50 µL of 0.05 ng/µL rmCathepsin L to wells, and start the reaction by adding 50 µL of 20 µM Substrate. Include a Substrate Blank containing of 50 µL Assay Buffer and 50 µL of 20 µM Substrate.
  6. Read at excitation and emission wavelengths of 380 nm and 460 nm (top read), respectively, in kinetic mode for 5 minutes.
  7. Calculate specific activity:

     Specific Activity (pmol/min/µg) =

Adjusted Vmax* (RFU/min) x Conversion Factor** (pmol/RFU)
amount of enzyme (µg)

     *Adjusted for Substrate Blank
     **Derived using calibration standard 7-Amino, 4-Methyl Coumarin (AMC) (Sigma, Catalog # A-9891)

Per Well:
  • rmCathepsin L: 0.0025 µg
  • Substrate: 10 µM

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse Cathepsin L Protein, CF

  • Cathepsin L
  • cathepsin L1
  • CATL
  • CTSL
  • CTSL1
  • CTSLEC 3.4.22.15
  • EC 3.4.22
  • FLJ31037
  • Major excreted protein
  • MEP

Background

Cathepsin L is a lysosomal cysteine protease expressed in most eukaryotic cells. Cathepsin L is known to hydrolyze a number of proteins, including the proform of urokinase‑type plasminogen activator, which is activated by Cathepsin L cleavage (1). Cathepsin L has also been shown to proteolytically inactivate alpha 1-antitrypsin and secretory leucoprotease inhibitor, two major protease inhibitors of the respiratory tract (2). These observations, combined with the demonstration of increased Cathepsin L activity in the epithelial lining fluid of the lungs of emphysema patients, have led to the suggestion that the enzyme may be involved in the progression of this disease. Cathepsin L has also been identified as a major excreted protein of transformed fibroblasts, indicating the enzyme could be involved in malignant tumor growth (3). In Cathepsin L‑deficient mice, it appears to play a critical role in cardiac morphology and function, epidermal homeostasis, regulation of the hair cycle, and MHC class II‑mediated antigen presentation in cortical epithelial cells of the thymus (4, 5). Mouse Cathepsin L is synthesized as a 334 amino acid precursor with a signal peptide (residues 1‑17), a pro region (residues 18‑113) and a mature chain (residues 114‑334).

  1. Goretzki, L. et al. (1992) FEBS Lett. 297:112.
  2. Taggart, C.C. et al. (2001) J. Biol. Chem. 276:33345.
  3. Gottesman, M.M. and F. Cabral (1981) Biochemistry 20:1659.
  4. Stypmann, J. et al. (2002) Proc. Natl. Acad. Sci. USA 99: 6234.
  5. Reinheckel, T. et al. (2001) Biol. Chem. 382:735.
  6.    

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1515-CY
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Publications for Cathepsin L (1515-CY)(8)

We have publications tested in 3 confirmed species: Human, Mouse, Diplozoidae - Eudiplozoon nipponicum.

We have publications tested in 2 applications: Bioassay, Enzyme Assay.


Filter By Application
Bioassay
(7)
Enzyme Assay
(1)
All Applications
Filter By Species
Human
(1)
Mouse
(5)
Diplozoidae - Eudiplozoon nipponicum
(1)
All Species
Showing Publications 1 - 8 of 8.
Publications using 1515-CY Applications Species
J Ilgová, L Kavanová, K Matiašková, J Salát, M Kašný Effect of cysteine peptidase inhibitor of Eudiplozoon nipponicum (Monogenea) on cytokine expression of macrophages in vitro Mol. Biochem. Parasitol., 2019-12-23;235(0):111248. 2019-12-23 [PMID: 31874193] (Bioassay, Diplozoidae - Eudiplozoon nipponicum) Bioassay Diplozoidae - Eudiplozoon nipponicum
J Ilgová, L Jedli?ková, H Dvo?áková, M Benovics, L Mikeš, L Janda, J Vorel, P Roudnický, D Pot?šil, Z Zdráhal, M Gelnar, M Kašný A novel type I cystatin of parasite origin with atypical legumain-binding domain Sci Rep, 2017-12-13;7(1):17526. 2017-12-13 [PMID: 29235483] (Bioassay, Mouse) Bioassay Mouse
C Tohda, M Tohda Extracellular cathepsin L stimulates axonal growth in neurons BMC Res Notes, 2017-11-23;10(1):613. 2017-11-23 [PMID: 29169406] (Bioassay, Mouse) Bioassay Mouse
X Zhou, DH Paushter, T Feng, L Sun, T Reinheckel, F Hu Lysosomal processing of progranulin Mol Neurodegener, 2017-08-23;12(1):62. 2017-08-23 [PMID: 28835281] (Bioassay, Mouse) Bioassay Mouse
Akia N Parks Supraspinatus tendon overuse results in degenerative changes to tendon insertion region and adjacent humeral cartilage in a rat model J. Orthop. Res, 2016-12-21;0(0):. 2016-12-21 [PMID: 28001327] (Bioassay) Bioassay
McComb S, Shutinoski B, Thurston S, Cessford E, Kumar K, Sad S Cathepsins limit macrophage necroptosis through cleavage of Rip1 kinase. J Immunol, 2014-05-05;192(12):5671-8. 2014-05-05 [PMID: 24799565] (Bioassay, Mouse) Bioassay Mouse
Zeeuwen PL, van Vlijmen-Willems IM, Cheng T The cystatin M/E-cathepsin L balance is essential for tissue homeostasis in epidermis, hair follicles, and cornea. FASEB J., 2010-05-21;24(10):3744-55. 2010-05-21 [PMID: 20495178] (Enzyme Assay, Mouse) Enzyme Assay Mouse
Duncan EM, Muratore-Schroeder TL, Cook RG, Garcia BA, Shabanowitz J, Hunt DF, Allis CD Cathepsin L proteolytically processes histone H3 during mouse embryonic stem cell differentiation. Cell, 2008-10-17;135(2):284-94. 2008-10-17 [PMID: 18957203] (Bioassay, Human) Bioassay Human

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Bioinformatics

Gene Symbol Ctsl
Uniprot