• Cathepsin H is a disulfide-linked heavy and light chain dimer which belongs to the peptidase C1 protein family, can act both as an aminopeptidase and as an endopeptidase. (scbt.com)
  • cathepsin H Inhibitors offered by Santa Cruz inhibit cathepsin H and, in some cases, other cellular metabolism and protein degradation related proteins. (scbt.com)
  • Cathepsin G is a 255-amino-acid-residue protein including an 18-residue signal peptide, a two-residue activation peptide at the N-terminus and a carboxy terminal extension. (wikipedia.org)
  • Cathepsin C catalyses excision of dipeptides from the N-terminus of protein and peptide substrates, except if (i) the amino group of the N-terminus is blocked, (ii) the site of cleavage is on either side of a proline residue, (iii) the N-terminal residue is lysine or arginine, or (iv) the structure of the peptide or protein prevents further digestion from the N-terminus. (wikipedia.org)
  • The activity of cathepsin G depends on a catalytic triad composed of aspartate, histidine and serine residues which are widely separated in the primary sequence but close to each other at the active site of the enzyme in the tertiary structure. (wikipedia.org)
  • Cathepsin Z has an exposed integrin-bindign Arg-Gly-Asp motif within the propeptide of the enzyme, through which cathepsin Z has been shown to interact with several integrins during normal homeostasis, immune processes and cancer. (wikipedia.org)
  • The cDNAs encoding rat, human, murine, bovine, dog and two Schistosome cathepsin Cs have been cloned and sequenced and show that the enzyme is highly conserved. (wikipedia.org)
  • The signal peptide is removed during translocation or secretion of the pro-enzyme (pro-cathepsin C) and a large N-terminal proregion fragment (also known as the exclusion domain), which is retained in the mature enzyme, is separated from the catalytic domain by excision of a minor C-terminal part of the pro-region, called the activation peptide. (wikipedia.org)
  • Cathepsin C functions as a key enzyme in the activation of granule serine peptidases in inflammatory cells, such as elastase and cathepsin G in neutrophils cells and chymase and tryptase in mast cells. (wikipedia.org)
  • 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. (wikipedia.org)
  • Unlike the other members of the papain family, mature cathepsin C consists of four subunits, each composed of the N-terminal proregion fragment, the heavy chain and the light chain. (wikipedia.org)
  • It is an exopeptidase with strict carboxypeptidase activity, while most other cathepsins are endopeptidases. (wikipedia.org)
  • Similarities between human and rat leukocyte elastase and cathepsin G". European Journal of Biochemistry / FEBS. (wikipedia.org)
  • Santa Cruz Biotechnology now offers a broad range of cathepsin H Inhibitors. (scbt.com)
  • Elevated levels of cathepsin H correlates with malignant progression of prostate tumors. (scbt.com)
  • Other functions of cathepsin G have been reported, including cleavage of receptors, conversion of angiotensin Ⅰ to angiotensin Ⅱ, platelet activation, and induction of airway submucosal gland secretion. (wikipedia.org)
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