Cathepsin F Polyclonal Antibody, Invitrogen™

Description

• The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE)
• 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.