Recombinant Human Cathepsin L Protein, CF

Catalog # Availability Size / Price Qty
952-CY-010
Product Details
Citations (17)
FAQs
Supplemental Products
Reviews (1)

Recombinant Human Cathepsin L Protein, CF Summary

Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<1.0 EU per 1 μg of the protein by the LAL method.
Activity
Measured by its ability to cleave the fluorogenic peptide substrate Z-LR-AMC (Catalog # ES008). The specific activity is >25,000 pmol/min/µg, as measured under the described conditions.
Source
Mouse myeloma cell line, NS0-derived human Cathepsin L protein
Glu113-Val333 & Ala114-Val333, both with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Analysis
Glu113 & Ala114
Structure / Form
Mature form
Predicted Molecular Mass
26 kDa
SDS-PAGE
36 kDa, reducing conditions

Product Datasheets

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

952-CY

Formulation Supplied as a 0.2 μm filtered solution in Sodium Acetate and NaCl.
Shipping The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.

Assay Procedure

Materials
  • Assay Buffer: 50 mM MES, 5 mM DTT, 1 mM EDTA, 0.005% (w/v) Brij-35, pH 6.0
  • Recombinant Human Cathepsin L (rhCathepsin L) (Catalog # 952-CY)
  • Fluorogenic Peptide Substrate VII: Z-Leu-Arg-AMC (Catalog # ES008)
  • F16 Black Maxisorp Plate (Nunc, Catalog # 475515)
  • Fluorescent Plate Reader (Model: SpectraMax Gemini EM by Molecular Devices) or equivalent
  1. Dilute rhCathepsin L to 40 µg/mL in Assay Buffer.
  2. Incubate diluted rhCathepsin L on ice for 15 minutes.
  3. Dilute incubated 40 µg/mL rhCathepsin L to 0.02 ng/µL in Assay Buffer.
  4. Dilute Substrate to 80 µM in Assay Buffer.
  5. Load 50 µL of 0.02 ng/µL rhCathepsin L into a black well plate, and start the reaction by adding 50 µL of 80 µM Substrate. Include a Substrate Blank containing 50 µL Assay Buffer and 50 µL of 80 µM Substrate without any rhCathepsin L.
  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:
  • rhCathepsin L: 0.001 µg
  • Substrate: 40 µM
Reconstitution Calculator

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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Background: Cathepsin L

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). Human Cathepsin L activity is greatest under mildly acidic conditions, from pH 4.5 - 6.5. The stability of the enzyme decreases at higher pH values.

References
  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.
Entrez Gene IDs
1514 (Human); 1514 (Human); 13039 (Mouse)
Alternate Names
Cathepsin L; cathepsin L1; CATL; CTSL; CTSL1; CTSLEC 3.4.22.15; EC 3.4.22; FLJ31037; Major excreted protein; MEP

Citations for Recombinant Human Cathepsin L Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

17 Citations: Showing 1 - 10
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  1. Human Cysteine Cathepsins Degrade Immunoglobulin G In Vitro in a Predictable Manner
    Authors: RA Høglund, SB Torsetnes, A Lossius, B Bogen, EJ Homan, R Bremel, T Holmøy
    Int J Mol Sci, 2019;20(19):.
    Species: Human
    Sample Types: Protein
    Applications: Bioassay
  2. Cell penetrable, clickable and tagless activity-based probe of human cathepsin L
    Authors: D Dana, J Garcia, AI Bhuiyan, P Rathod, L Joo, DA Novoa, S Paroly, KR Fath, EJ Chang, SK Pathak
    Bioorg. Chem., 2019;85(0):505-514.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Click Chemistry
  3. Image-guided surgery using near-infrared Turn-ON fluorescent nanoprobes for precise detection of tumor margins
    Authors: R Blau, Y Epshtein, E Pisarevsky, G Tiram, S Israeli Da, E Yeini, A Krivitsky, A Eldar-Booc, D Ben-Shusha, H Gibori, A Scomparin, O Green, Y Ben-Nun, E Merquiol, H Doron, G Blum, N Erez, R Grossman, Z Ram, D Shabat, R Satchi-Fai
    Theranostics, 2018;8(13):3437-3460.
    Species: Synthetic
    Sample Types: Polymer
    Applications: Enzyme Assay
  4. The lysosomal protein cathepsin L is a progranulin protease
    Authors: CW Lee, JN Stankowski, J Chew, CN Cook, YW Lam, S Almeida, Y Carlomagno, KF Lau, M Prudencio, FB Gao, M Bogyo, DW Dickson, L Petrucelli
    Mol Neurodegener, 2017;12(1):55.
    Species: Human
    Sample Types: Protein
    Applications: Bioassay
  5. Enzymatic cleavage of myoferlin releases a dual C2-domain module linked to ERK signalling
    Authors: AK Piper, SE Ross, GM Redpath, FA Lemckert, N Woolger, A Bournazos, PA Greer, RB Sutton, ST Cooper
    Cell. Signal, 2017;33(0):30-40.
    Species: Human
    Sample Types: Protein
    Applications: Bioassay
  6. Suppression and resolution of autoimmune arthritis by rhesus ?-defensin-1, an immunomodulatory macrocyclic peptide
    Authors: JB Schaal, DQ Tran, A Subramania, R Patel, T Laragione, KD Roberts, K Trinh, P Tongaonkar, PA Tran, D Minond, GB Fields, P Beringer, AJ Ouellette, PS Gulko, ME Selsted
    PLoS ONE, 2017;12(11):e0187868.
    Species: N/A
    Sample Types: Recombinant Protein
    Applications: Bioassay
  7. Immunization-Elicited Broadly Protective Antibody Reveals Ebolavirus Fusion Loop as a Site of Vulnerability
    Authors: X Zhao, KA Howell, S He, JM Brannan, AZ Wec, E Davidson, HL Turner, CI Chiang, L Lei, JM Fels, H Vu, S Shulenin, AN Turonis, AI Kuehne, G Liu, M Ta, Y Wang, C Sundling, Y Xiao, JS Spence, BJ Doranz, FW Holtsberg, AB Ward, K Chandran, JM Dye, X Qiu, Y Li, MJ Aman
    Cell, 2017;169(5):891-904.e15.
    Species: Human
    Sample Types: Complex Sample Type
    Applications: Bioassay
  8. Endosomal acidification and cathepsin L activity is required for calicivirus replication.
    Authors: Shivanna V, Kim Y, Chang K
    Virology, 2014;464(0):287-95.
    Species: Porcine
    Sample Types: Whole Cells
    Applications: Bioassay
  9. Cathepsin K-mediated Notch1 activation contributes to neovascularization in response to hypoxia.
    Authors: Jiang H, Cheng X, Shi G, Hu L, Inoue A, Yamamura Y, Wu H, Takeshita K, Li X, Huang Z, Song H, Asai M, Hao C, Unno K, Koike T, Oshida Y, Okumura K, Murohara T, Kuzuya M
    Nat Commun, 2014;5(0):3838.
    Species: Mouse
    Sample Types: Tissue Homogenates
    Applications: Bioassay
  10. Regulation of cathepsin g reduces the activation of proinsulin-reactive T cells from type 1 diabetes patients.
    Authors: Zou F, Schafer N, Palesch D, Brucken R, Beck A, Sienczyk M, Kalbacher H, Sun Z, Boehm BO, Burster T
    PLoS ONE, 2011;6(8):e22815.
    Species: Human
    Sample Types: Protein
    Applications: Enzyme Assay
  11. Fine-tuning nucleophosmin in macrophage differentiation and activation.
    Authors: Guery L, Benikhlef N, Gautier T, Paul C, Jego G, Dufour E, Jacquel A, Cally R, Manoury B, Vanden Berghe T, Vandenabeele P, Droin N, Solary E
    Blood, 2011;118(17):4694-704.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Enzyme Assay
  12. Development and validation of sandwich ELISA microarrays with minimal assay interference.
    Authors: Gonzalez RM, Seurynck-Servoss SL, Crowley SA
    J. Proteome Res., 2008;7(6):2406-14.
    Species: N/A
    Sample Types: N/A
    Applications: ELISA (Standard)
  13. Cystatin F is a cathepsin C-directed protease inhibitor regulated by proteolysis.
    Authors: Hamilton G, Colbert JD, Schuettelkopf AW, Watts C
    EMBO J., 2008;27(3):499-508.
    Species: N/A
    Sample Types: Fluorogenic Peptide Substrate
    Applications: Enzyme Assay
  14. Inhibition of the activation of multiple serine proteases with a cathepsin C inhibitor requires sustained exposure to prevent pro-enzyme processing.
    Authors: Methot N, Rubin J, Guay D, Beaulieu C, Ethier D, Reddy TJ, Riendeau D, Percival MD
    J. Biol. Chem., 2007;282(29):20836-46.
    Species: N/A
    Sample Types: Fluorogenic Peptide Substrate
    Applications: Enzyme Assay
  15. Design of protease-resistant myelin basic protein-derived peptides by cleavage site directed amino acid substitutions.
    Authors: Burster T, Marin-Esteban V, Boehm BO, Dunn S, Rotzschke O, Falk K, Weber E, Verhelst SH, Kalbacher H, Driessen C
    Biochem. Pharmacol., 2007;74(10):1514-23.
    Species: Human
    Sample Types: Cell Lysates
    Applications: Enzyme Assay
  16. Distinct roles for cysteine cathepsin genes in multistage tumorigenesis.
    Authors: Gocheva V, Zeng W, Ke D, Klimstra D, Reinheckel T, Peters C, Hanahan D, Joyce JA
    Genes Dev., 2006;20(5):543-56.
    Species: Human
    Sample Types: Buffer
    Applications: Enzyme Assay
  17. Cystatin M/E is a high affinity inhibitor of cathepsin V and cathepsin L by a reactive site that is distinct from the legumain-binding site. A novel clue for the role of cystatin M/E in epidermal cornification.
    Authors: Cheng T, Hitomi K, van Vlijmen-Willems IM, de Jongh GJ, Yamamoto K, Nishi K, Watts C, Reinheckel T, Schalkwijk J, Zeeuwen PL
    J. Biol. Chem., 2006;281(23):15893-9.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Enzyme Assay

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Reviews for Recombinant Human Cathepsin L Protein, CF

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Recombinant Human Cathepsin L Protein, CF
By Anonymous on 02/21/2017
Application: Enzymatic activity in vitro
Reason for Rating: Excellent product. The consistency between lots seems to be high.