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Cathepsins are papain family cysteine proteinases that represent a major component of the lysosomal proteolytic system. Additionally we are shipping Cathepsin F Proteins (9) and Cathepsin F Kits (7) and many more products for this protein.
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Human Polyclonal Cathepsin F Primary Antibody for ELISA, WB - ABIN250491
Dorn, Zhao, Granberg, Hösel, Webb, Svensson, Pettersson, Doerfler: Identification of specific cellular genes up-regulated late in adenovirus type 12 infection. in Journal of virology 2005
Show all 3 Pubmed References
Biallelic mutations in this gene have been shown to cause Type B Kufs disease, an adult-onset neuronal ceroid lipofuscinosis (show CLN6 Antibodies) with some cases resembling the impairment seen in AD.
Disease-causing cathepsin-F mutants fail to cleave LIMP-2 (show SCARB2 Antibodies). Our findings provide evidence that LIMP-2 (show SCARB2 Antibodies) represents an in vivo substrate of cathepsin-F with relevance for understanding the pathophysiology of type-B-Kufs-disease.
Homozygous and compound heterozygous missense mutations in CTSF are associated with adult-onset neuronal ceroid lipofuscinosis (show CLN6 Antibodies).
cathepsin F has a role in modifying low density lipoprotein particles
cathepsin F, matrix metalloproteinases 11 and 12 are upregulated in cervical cancer
data demonstrate a novel proatherogenic role for AngII, namely its ability to enhance secretion of lysosomal cathepsin F by monocyte-derived macrophages
cathepsin F inactivation causes a lysosomal storage defect and progressive neurological features in mice
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.
, hypothetical protein LOC100158959
, Cathepsin F
, cathepsin F-like