Anti-CTSC Antibody Picoband® Fluoro647 Conjugated

Cathepsin C (CTSC) also known as dipeptidyl peptidase I (DPP-I) is a lysosomal exo-cysteine protease belonging to the peptidase C1 protein family, a subgroup of the cysteine cathepsins. In humans, it is encoded by the CTSC gene. 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.

Highly expressed in adult liver, lung and spleen than in corresponding fetal tissue. Also expressed in the lymph node, placenta, spinal cord and heart tissues. Expression is more elevated in peripheral blood leukocytes than in the bone marrow and in normal cells than malignant cells. Expressed at low levels in the early development of the hematopoietic system and in the promonocytic stage and at high levels in mature monocytes. Strongly expressed in acute inflammatory lesions caused by bacteria and fungi. Isoform 2 was detected in the lung, liver and mature monocytes.

Stimulates neutrophil and monocyte-mediated inflammatory responses. Triggers release of pro-inflammatory chemokines and cytokines, as well as increased surface expression of cell activation markers. Amplifier of inflammatory responses that are triggered by bacterial and fungal infections and is a crucial mediator of septic shock.

1. Cigic, B., Dahl, S. W., Pain, R. H. The residual pro-part of cathepsin C fulfills the criteria required for an intramolecular chaperone in folding and stabilizing the human proenzyme. Biochemistry 39: 12382-12390, 2000. 2. Gorlin, R. J., Pindborg, J. J., Cohen, M. M., Jr. Syndromes of the Head and Neck. (2nd ed.) New York: McGraw-Hill (pub.) 1976. Pp. 373-376. 3. Hart, P. S., Zhang, Y., Firatli, E., Uygur, C., Lotfazar, M., Michalec, M. D., Marks, J. J., Lu, X., Coates, B. J., Seow, W. K., Marshall, R., Williams, D., Reed, J. B., Wright, J. T., Hart, T. C. Identification of cathepsin C mutations in ethnically diverse Papillon-Lefevre syndrome patients. J. Med. Genet. 37: 927-932, 2000.