Kallikrein-7 (KLK7) is also known as kallikrein-related peptidase 7, Stratum corneum chymotryptic enzyme, Serine protease 6, KLK7, and PRSS6, is a secreted protein which belongs to the peptidase S1 family and Kallikrein subfamily. KLK7 is secreted as an inactive zymogen in the stratum granulosum layer of the epidermis, requiring proteolytic cleavage of the short N-terminal pro-region to liberate activated enzyme. This may be performed by KLK5 or matriptase, which are in vitro activators of KLK7. Once active, KLK7 is able to cleave desmocollin and corneodesmosin. KLK7 activity is regulated by a number of endogenous protein inhibitors including LEKTI, SPINK6, elafin and alpha-2-Macroglobulin-like 1. Both Zn2+ and Cu2+ ions are also able to inhibit KLK7. Dysregulation of KLK7 has been linked to several skin disorders, and overexpression of KLK7 may provide a route for metastasis in several cancers.