Cathepsins are proteases which are found in all animals plus other organisms. There are around 12 members in this family, established by catalytic mechanism, structure, and their protein targets.
Cysteine and Aspartyl Proteases
The cysteine protease class is made up of cathepsins B, L, H, K, S, and O. The aspartyl protease class is made up of cathepsins D and E.
Many of the members become activated at the low pH located in lysosomes. However, there are exceptions, such as cathepsin K, which works extracellularly after secretion by osteoclasts in bone resorption. Cathepsins play a key part in mammalian cellular turnover, e.g. bone resorption. Cysteine cathepsins are highly upregulated in a large number of cancers.
Cathepsins for Research
Cathepsins are also implicated in a number of other diseases such as Alzheimer’s disease, arthritis, COPD, stroke, pancreatitis, chronic periodontitis, polycystic kidney disease and a number of ocular diseases including AMD, keratoconus, retinal detachment, glaucoma etc.
BioVision is proud to provide a number of active recombinant enzymes/proteins, assay kits, antibodies, blocking peptides and inhibitors for research in these and additional areas related to cathepsins.
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