ELISA/assay

Goat Cathepsin C ELISA Kit

MBS019674

96 Strip Wells

600 USD

ELISA Kit

Goat Cathepsin C ELISA Kit

Cathepsin C

CTSC protein; Dipeptidyl peptidase 1; dipeptidyl peptidase 1; cathepsin J; dipeptidyl peptidase I; dipeptidyl transferase; dipeptidyl-peptidase I; cathepsin C; Cathepsin C; Cathepsin J; Dipeptidyl peptidase I; DPP-I; DPPI; Dipeptidyl transferaseCleaved into the following 3 chains:Dipeptidyl peptidase 1 exclusion domain chain; Alternative name(s):; Dipeptidyl peptidase I exclusion domain chainDipeptidyl peptidase 1 heavy chain; Alternative name(s):; Dipeptidyl peptidase I heavy chainDipeptidyl peptidase 1 light chain; Alternative name(s):; Dipeptidyl peptidase I light chain

CTSC

CTSC; CTSC; JP; HMS; JPD; PLS; CPPI; DPP1; DPPI; PALS; DPP-I; PDON1; CPPI; DPP-I; DPPI

CATC_HUMAN

Goat

Store all reagents at 2-8 degree C

ELISA Type: Sandwich

88683003

AAI13851.1

P53634

51,854 Da

Adaptive Immune System Pathway 366160!!Immune System Pathway 106386!!Lysosome Pathway 99052!!Lysosome Pathway 96865!!MHC Class II Antigen Presentation Pathway 645290

The protein encoded by this gene, a member of the peptidase C1 family, is a lysosomal cysteine proteinase that appears to be a central coordinator for activation of many serine proteinases in immune/inflammatory cells. It is composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor, and a residual 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. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]

Function: 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. Ref.14. Catalytic activity: Release of an N-terminal dipeptide, Xaa-Yaa- -Zaa-, except when Xaa is Arg or Lys, or Yaa or Zaa is Pro. Cofactor: Binds 1 chloride ion per heavy chain. Enzyme regulation: Strongly inhibited by the cysteine peptidase inhibitors mersalyl acid, iodoacetic acid and cystatin. Inhibited by N-ethylmaleimide, Gly-Phe-diazomethane, TLCK, TPCK and, at low pH, by dithiodipyridine. Not inhibited by the serine peptidase inhibitor PMSF, the aminopeptidase inhibitor bestatin, or metal ion chelators. Ref.14. Subunit structure: Tetramer of heterotrimers consisting of exclusion domain, heavy- and light chains. Ref.14 Ref.18. Subcellular location: Lysosome. Tissue specificity: Ubiquitous. Highly expressed in lung, kidney and placenta. Detected at intermediate levels in colon, small intestine, spleen and pancreas. Ref.2. Induction: Up-regulated in lymphocytes by IL2/interleukin-2. Ref.2 Ref.14. Post-translational modification: N-glycosylated. While glycosylation at Asn-53, Asn-119 and Asn-276 is mediated by STT3A-containing complexes, glycosylation at Asn-29 is mediated STT3B-containing complexes. Ref.11 Ref.14 Ref.15 Ref.18In approximately 50% of the complexes the exclusion domain is cleaved at position 58 or 61. The two parts of the exclusion domain are held together by a disulfide bond. Involvement in disease: Papillon-Lefevre syndrome (PLS) [MIM:245000]: 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.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3 Ref.4 Ref.19 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29Haim-Munk syndrome (HMS) [MIM:245010]: An autosomal recessive disorder characterized by palmoplantar keratosis, onychogryphosis and periodontitis. Additional features are pes planus, arachnodactyly, and acroosteolysis.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20Periodontititis, aggressive, 1 (AP1) [MIM:170650]: A disease characterized by severe and protracted gingival infections, generalized or localized, leading to tooth loss. Amounts of microbial deposits are generally inconsistent with the severity of periodontal tissue destruction and the progression of attachment and bone loss may be self arresting.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.21 Ref.27. Sequence similarities: Belongs to the peptidase C1 family. Biophysicochemical propertiespH dependence:High activity at pH 4.5-6.8. Ref.14. Sequence caution: The sequence CAD97897.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

96 Strip Wells

600 USD