KLK7 is a secreted serine protease that plays critical roles in both normal physiology and disease. Functionally, KLK7 catalyzes degradation of intercellular cohesive structures in the skin's cornified layer, facilitating continuous epidermal desquamation 1. The protease specifically cleaves substrates with aromatic amino acids in the P1 position and activates procaspase-14 during keratinocyte terminal differentiation 2. In skin barrier maintenance, KLK7 activity is tightly regulated by LEKTI; imbalance causes excessive desquamation in Netherton syndrome and atopic dermatitis 1. Beyond dermatology, KLK7 contributes to inflammatory responses by promoting immune cell infiltration in adipose tissue during obesity, with elevated serum KLK7 correlating with inflammatory markers in diabetic patients 3. Pathologically, KLK7 is significantly overexpressed across multiple cancers including pancreatic, cervical, thyroid, and ovarian carcinomas 4567. In cervical cancer, KLK7 drives tumorigenesis via KLK14-dependent RhoA and NF-κB signaling 5, while elevated expression associates with reduced progression-free survival in ovarian cancer 7. KLK7 expression is epigenetically regulated through histone acetylation and Sp1-dependent mechanisms 4. Therapeutically, bispecific antibodies inhibiting KLK5/7 show promise for inflammatory dermatoses 1, while KLK7 represents an emerging cancer therapy target 8.