< 1 EU per 1 ug of protein (determined by LAL method)
Activity:
Specific activity is > 5 pmol/min/ug, and is defined as the amount of enzyme that hydrolyze 1pmole of Z-Phe-Arg-AMC to Z-Phe-Arg and AMC per minute at pH 5.0 at 37°C.
Quality Control Testing:
3 ug by SDS-PAGE under reducing condition and visualized by Coomassie blue stain.
Storage Buffer:
In Phosphate-Buffer Saline pH 7.4 (40% glycerol)
Storage Instruction:
Store at 2°C to 8°C for 1 week. For long term storage, aliquot and store at -20°C to -80°C. Aliquot to avoid repeated freezing and thawing.
Cathepsins are papain family cysteine proteinases that represent a major component of the lysosomal proteolytic system. Cathepsins generally contain a signal sequence, followed by a propeptide and then a catalytically active mature region. The very long (251 amino acid residues) proregion of the cathepsin F precursor contains a C-terminal domain similar to the pro-segment of cathepsin L-like enzymes, a 50-residue flexible linker peptide, and an N-terminal domain predicted to adopt a cystatin-like fold. The cathepsin F proregion is unique within the papain family cysteine proteases in that it contains this additional N-terminal segment predicted to share structural similarities with cysteine protease inhibitors of the cystatin superfamily. This cystatin-like domain contains some of the elements known to be important for inhibitory activity. CTSF encodes a predicted protein of 484 amino acids which contains a 19 residue signal peptide. Cathepsin F contains five potential N-glycosylation sites, and it may be targeted to the endosomal/lysosomal compartment via the mannose 6-phosphate receptor pathway. The cathepsin F gene is ubiquitously expressed, and it maps to chromosome 11q13, close to the gene encoding cathepsin W. [provided by RefSeq