Cathepsin H is a lysosomal cysteine protease of the papain family. It is synthesized as a precursor protein that is proteolytically processed to a mature form consisting of a light chain, a heavy chain, and a minichain. Cathepsin H is the only known monoaminopeptidase in the papain family. Cathepsin H is primarily an aminopeptidase, but also functions as an endopeptidase. Cathepsin H is potently inhibited by cystatins A, B, and C and by ovocystatin. Cathepsin H expression is altered in disease states such as prostate and colorectal cancers.
Source:
Recombinant corresponding to aa23-335 from human Cathepsin H fused to 10-His-tag at C-terminal expressed in CHO cell line.
Molecular Weight:
~37kD
Biological Activity:
Measured by its ability to cleave the fluorogenic peptide substrate, Arg7amido4methylcoumarin
(RAMC).
Specific Activity:
>750 pmol/min/ug, as measured under the described conditions.
Endotoxin: ~1EU/1ug (LAL)
Storage and Stability:
Aliquot to avoid repeated freezing and thawing and store at -70 degrees C. Aliquots are stable for 6 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.