CTSC
CTSC (cathepsin C), also known as dipeptidyl peptidase 1 (DPP1), PLS or PALS, is a lysosomal cysteine protease of the peptidase C1 family. It removes dipeptides from substrates and activates several serine proteases in cells of the immune system. Browse Assay Genie's current range of CTSC research reagents below, or read on for the biology behind the target.
CTSC is a thiol protease with dipeptidylpeptidase activity. It acts on a broad range of dipeptide substrates containing both polar and hydrophobic amino acids, although proline cannot occupy the P1 position and arginine cannot occupy the P2 position. The enzyme can act as both an exopeptidase and an endopeptidase. Its best-described role is as an activator of serine proteases, including elastase, cathepsin G and granzymes A and B, which is why it is regarded as a central coordinator of serine protease activation in immune cells. The enzyme requires chloride ions for activity and can degrade glucagon.
The CTSC gene encodes a member of the peptidase C1 family and a lysosomal cysteine proteinase. Alternative splicing produces multiple transcript variants, at least one of which encodes a preproprotein. This is processed proteolytically into heavy and light chains that form a disulfide-linked dimer. A portion of the propeptide acts as an intramolecular chaperone, supporting folding and stabilisation of the mature enzyme. CTSC belongs to the HGNC cathepsin gene group, and orthologues are annotated in mouse and rat (Ctsc).
Defects in the CTSC gene cause Papillon-Lefevre syndrome, an autosomal recessive disorder characterised by palmoplantar keratosis and periodontitis. The protein is known by several names, including cathepsin C, dipeptidyl peptidase 1 and the aliases DPP1, PLS and PALS, so literature searches benefit from using all of them.
CTSC activates elastase, cathepsin G and granzymes A and B, making it a focus for studying serine protease control in immune cells.
As a lysosomal cysteine proteinase of the peptidase C1 family, CTSC is studied for propeptide chaperoning, chain processing and chloride-dependent activity.
Defects in CTSC cause this autosomal recessive disorder of palmoplantar keratosis and periodontitis, so the gene is central to its molecular study.
CTSC removes dipeptides with defined P1 and P2 restrictions and has both exopeptidase and endopeptidase activity, informing enzymology work.
CTSC is a lysosomal thiol protease that cleaves dipeptides from substrates and can act as both an exopeptidase and an endopeptidase. It activates serine proteases such as elastase, cathepsin G and granzymes A and B, and it can also degrade glucagon.
CTSC is also called cathepsin C, dipeptidyl peptidase 1, DPP1, PLS and PALS. Alternative splicing gives several transcript variants. At least one encodes a preproprotein that is processed into heavy and light chains joined by a disulfide bond.
Defects in CTSC cause Papillon-Lefevre syndrome, an autosomal recessive disorder with palmoplantar keratosis and periodontitis. Mouse and rat orthologues are both named Ctsc; check the datasheet of any product for its validated reactivity.
Other cathepsins, serine protease targets activated by CTSC and related immune protease markers with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P53634; product specifications from Assay Genie datasheets.