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Cathepsins are papain family cysteine proteinases that represent a major component of the lysosomal proteolytic system. Zusätzlich bieten wir Ihnen Cathepsin F Antikörper (107) und Cathepsin F Proteine (11) und viele weitere Produktgruppen zu diesem Protein an.
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The CTSF gene may function as a tumor suppressor in gastric cancer
Biallelic mutations in this gene have been shown to cause Type B Kufs disease, an adult-onset neuronal ceroid lipofuscinosis with some cases resembling the impairment seen in AD.
Disease-causing cathepsin-F mutants fail to cleave LIMP-2. Our findings provide evidence that LIMP-2 represents an in vivo substrate of cathepsin-F with relevance for understanding the pathophysiology of type-B-Kufs-disease.
Small hairpin RNA silencing of proteinases overexpressed in diabetic corneas enhanced corneal epithelial and stem cell marker staining and accelerated wound healing.
Homozygous and compound heterozygous missense mutations in CTSF are associated with adult-onset neuronal ceroid lipofuscinosis.
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
This gene is known to be important for immune responses and may potentially regulate alcohol consumption.
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