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S100 calcium binding protein A15 (commonly abbreviated as S100A15 and also known as Koebnerisin) is a member of the S100 family of calcium-binding proteins characterized by two EF-hand motifs. It is mainly expressed in the epidermis and plays a crucial role in the regulation of keratinocyte differentiation, antimicrobial host defense, inflammation, and epithelial tumorigenesis. S100A15 is upregulated in inflamed and psoriatic human skin, and its murine ortholog (mS100a7a15) is used in mouse models for these functions. The protein acts as a chemotactic factor, recruiting immune cells via RAGE, and modulates the cutaneous immunological response. It has been implicated in the progression of epithelial cancers such as breast cancer, but it is not an established therapeutic target
Not applicable due to lack of known drug interactions. S100A15 acts through protein-protein interactions (with RAGE—receptor for advanced glycation end-products—and through chemotactic signaling), but there are no current drugs targeting it directly.
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