background:
The cathepsin family of proteolytic enzymes contains several diverse classes of proteases. The cysteine protease class comprises cathepsins B, L, H, K, S, and O (1-6). The aspartyl protease class is composed of cathepsins D and E (7,8). Cathepsin G is in the serine protease class (9). Most cathepsins are lysosomal and each is involved in cellular metabolism, participating in various events such as peptide biosynthesis and protein degradation. Cathepsin S has been shown to be an elastinolytic cysteine proteinase present in aveloar macrophages.
Function:
Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N.
Subunit:
Monomer.
Subcellular Location:
Lysosomal.
Similarity:
Belongs to the peptidase C1 family.
Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
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