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219402 Cathepsin L, Human Liver

219402
Purchase on Sigma-Aldrich

Overview

Replacement Information

Key Spec Table

Products

Catalogue NumberPackaging Qty/Pack
219402-25UG Glass bottle 25 μg
Description
OverviewNative cathepsin L from human liver. The most potent of the lysosomal proteinases, having a higher activity than cathepsins B and H in the degradation of a variety of physiological protein substrates. Cathepsin L is believed to be responsible for the generation of endostatin from NC1 domain in collagen XVII.
Note: 1 mU = 1 milliunit.
Catalogue Number219402
Brand Family Calbiochem®
References
ReferencesKurata, M., et al. 2001. J. Biochem. (Tokyo) 130, 857.
Ferreras, M., et al. 2000. FEBS Lett. 486, 247.
Baricos, W.H., et al. 1988. Biochem. J. 252, 301.
McDonald, J.K., et al. 1988. Biochem. Biophys. Res. Commun. 151, 827.
Product Information
Unit of DefinitionOne 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.
EC number3.4.22.15
FormLiquid
FormulationIn 400 mM NaCl, 20 mM malonate buffer, 1 mM EDTA, pH 5.5.
Quality LevelMQ100
Applications
Biological Information
SourcePrepared from tissue of individuals that have been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV.
Concentration Label Please refer to vial label for lot-specific concentration
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Storage and Shipping Information
Ship Code Dry Ice Only
Toxicity Standard Handling
Storage ≤ -70°C
Avoid freeze/thaw Avoid freeze/thaw
Do not freeze Ok to freeze
Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
Packaging Information
Transport Information
Supplemental Information
Specifications

Documentation

Cathepsin L, Human Liver SDS

Title

Safety Data Sheet (SDS) 

Cathepsin L, Human Liver Certificates of Analysis

TitleLot Number
219402

References

Reference overview
Kurata, M., et al. 2001. J. Biochem. (Tokyo) 130, 857.
Ferreras, M., et al. 2000. FEBS Lett. 486, 247.
Baricos, W.H., et al. 1988. Biochem. J. 252, 301.
McDonald, J.K., et al. 1988. Biochem. Biophys. Res. Commun. 151, 827.

Brochure

Title
Cathepsins and Related Products Technical Bulletin

Citations

Title
  • Moin U Fareed, et al. (2006) Treatment of rats with calpain inhibitors prevents sepsis-induced muscle proteolysis independent of atrogin-1/MAFbx and MuRF1 expression. American Journal of Physiology Regulatory, Integrative and Comparative Physiology 290, R1589-R1597.
  • Data Sheet

    Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

    Revision28-April-2008 RFH
    DescriptionNative cathepsin L from human liver. The most powerful of the lysosomal proteinases, having a higher specific activity than cathepsins B and H in the degradation of a variety of physiological protein substances.
    FormLiquid
    FormulationIn 400 mM NaCl, 20 mM malonate buffer, 1 mM EDTA, pH 5.5.
    Concentration Label Please refer to vial label for lot-specific concentration
    SourcePrepared from tissue of individuals that have been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV.
    EC number3.4.22.15
    Unit definitionOne 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.
    Storage ≤ -70°C
    Avoid freeze/thaw
    Do Not Freeze Ok to freeze
    Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
    Toxicity Standard Handling
    Merck USA index14, 1905
    ReferencesKurata, M., et al. 2001. J. Biochem. (Tokyo) 130, 857.
    Ferreras, M., et al. 2000. FEBS Lett. 486, 247.
    Baricos, W.H., et al. 1988. Biochem. J. 252, 301.
    McDonald, J.K., et al. 1988. Biochem. Biophys. Res. Commun. 151, 827.
    Citation
  • Moin U Fareed, et al. (2006) Treatment of rats with calpain inhibitors prevents sepsis-induced muscle proteolysis independent of atrogin-1/MAFbx and MuRF1 expression. American Journal of Physiology Regulatory, Integrative and Comparative Physiology 290, R1589-R1597.