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VC004). Before incubation with the primary antibody, tissue was subjected to heat-induced epitope retrieval using VisUCyte Antigen Retrieval Reagent-Basic (Catalog # VCTS021). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to sarcoplasm in cardiomyocytes. View our protocol for IHC Staining with VisUCyte HRP Polymer Detection Reagents." class="big_lightbox" target="_blank">
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.
![Immunohistochemistry Cathepsin F Antibody [Unconjugated]](http://images.novusbio.com/images/antibody/af2075_human-cathepsin-f-affinity-purified-polyclonal-ab-immunohistochemistry-10102023151443..jpg)
![Immunohistochemistry Cathepsin F Antibody (237208) [Unconjugated]](http://images.novusbio.com/images/antibody/Cathepsin_F_MAB2075_Immunohistochemistry_6963.jpg)
