Supporting information

Cathepsins are a group of lysosomal proteases that have a key role in cellular protein turnover. The term cathepsin includes serine proteases (cathepsins A and G), aspartic proteases (cathepsin D and E) as well as the cysteine proteases (cathepsins B, C, F, H, K, L, O, S, W and Z).

Most cathepsins are endopeptidases, with the exception of cathepsin C and Z. Cathepsins are synthesized as inactive proenzymes, glycosylated post-translationally, and directed towards the lysosomal compartment by cellular mannose-6-phosphate receptors. Their activity is regulated by several mechanisms including regulation of synthesis, zymogen processing, inhibition by endogenous inhibitors (e.g. stefins and cystatins for cysteine cathepsins) and pH.

The main function of cathepsins is protein recycling within the lysosome but they are also known to be involved in a range of other physiological, as well as pathological processes, including maturation of the MHC class II complex, bone remodeling, keratinocyte differentiation, tumor progression and metastasis, rheumatoid arthritis, osteoarthritis and atherosclerosis.

View all products for Cathepsin »
Gene Species Gene Symbol Gene Accession No. Protein Accession No.
Cathepsin A Human CTSA NM_000308 P10619
Mouse Ctsa NM_011497 P97477
Cathepsin B Human CTSB NM_147780 P07858
Mouse Ctsb NM_007798 P10605
Rat Ctsb NM_012838 P01041
View all Cathepsin Gene Data »

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