Dipeptidyl Peptidase 1 (CTSC) ELISA Kit for Human

This gene encodes a member of the peptidase C1 family and lysosomal cysteine proteinase that appears to be a central coordinator for activation of many serine proteinases in cells of the immune system. Alternative splicing results in multiple transcript variants, at least one of which encodes a preproprotein that is proteolytically processed to generate heavy and light chains that form a disulfide-linked dimer. A portion of the propeptide acts as an intramolecular chaperone for the folding and stabilization of the mature enzyme. This enzyme requires chloride ions for activity and can degrade glucagon. Defects in the encoded protein have been shown to be a cause of Papillon-Lefevre syndrome, an autosomal recessive disorder characterized by palmoplantar keratosis and periodontitis. [provided by RefSeq, Nov 2015]

CTSC: Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII. Defects in CTSC are a cause of Papillon-Lefevre syndrome (PLS); also known as keratosis palmoplantaris with periodontopathia. PLS is an autosomal recessive disorder characterized by palmoplantar keratosis and severe periodontitis affecting deciduous and permanent dentitions and resulting in premature tooth loss. The palmoplantar keratotic phenotype vary from mild psoriasiform scaly skin to overt hyperkeratosis. Keratosis also affects other sites such as elbows and knees. Defects in CTSC are a cause of Haim-Munk syndrome (HMS); also known as keratosis palmoplantaris with periodontopathia and onychogryposis or Cochin Jewish disorder. HMS is an autosomal recessive disorder characterized by palmoplantar keratosis, onychogryphosis and periodontitis. Additional features are pes planus, arachnodactyly, and acroosteolysis. Defects in CTSC are a cause of aggressive periodontititis type 1 (AP1); also known as juvenile periodontitis (JPD) and prepubertal periodontitis (PPP). AP1 is characterized by severe and protracted gingival infections, leading to tooth loss. AP1 inheritance is autosomal dominant. Belongs to the peptidase C1 family. 3 isoforms of the human protein are produced by alternative splicing.

Protein type: EC 3.4.14.1; Endoplasmic reticulum; Protease

Chromosomal Location of Human Ortholog: 11q14.2

Cellular Component: endoplasmic reticulum lumen; ER to Golgi transport vesicle; ER-Golgi intermediate compartment membrane; extracellular space; Golgi membrane; lysosome; membrane

Molecular Function: apoptotic protease activator activity; chaperone binding; chloride ion binding; cysteine-type endopeptidase activity; cysteine-type peptidase activity; identical protein binding; phosphatase binding; protein binding; protein self-association; serine-type endopeptidase activity

Biological Process: aging; apoptosis; cellular protein metabolic process; COPII coating of Golgi vesicle; ER to Golgi vesicle-mediated transport; immune response; post-translational protein modification; protein amino acid N-linked glycosylation via asparagine; proteolysis; proteolysis involved in cellular protein catabolic process; response to organic substance; T cell mediated cytotoxicity

Disease: Haim-munk Syndrome; Papillon-lefevre Syndrome; Periodontitis, Aggressive, 1