Cathepsin L; Human Liver

General description

Note: 1 mU = 1 milliunit.

Native 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.

Cathepsin L, Human Liver, CAS 60616-82-2, is a native, the most potent of all the lysosomal proteinases. Plays a major role in the proteolysis of both cellular and endocytosed macromolecules.

Native 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.

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Other Notes

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.

Packaging

25 µg in Glass bottle

Please refer to vial label for lot-specific concentration.

Physical form

In 400 mM NaCl, 20 mM malonate buffer, 1 mM EDTA, pH 5.5.

Preparation Note

Prepared from tissue of individuals that have been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV.

Reconstitution

Following initial thaw, aliquot and freeze (-70°C).

Unit Definition

One 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.

Warning

Toxicity: Standard Handling (A)