Recombinant Human S100A7 protein

S100A7. also known as psoriasin, is a member of the S100 family of calcium-binding proteins characterized by two EF-hand structural motifs. Initially identified in psoriatic keratinocytes, S100A7 has since been implicated in diverse physiological and pathological processes, including inflammatory responses, immune regulation, and epithelial cell differentiation. Its expression is strongly associated with inflammatory skin disorders, particularly psoriasis, but it is also overexpressed in cancers such as breast, lung, and squamous cell carcinomas, where it may promote tumor progression and metastasis.

Recombinant S100A7 protein is produced using genetic engineering techniques, often expressed in bacterial (e.g., *E. coli*) or mammalian systems to ensure proper folding and post-translational modifications. This engineered protein retains the functional properties of native S100A7. including calcium-dependent interactions with target molecules like fatty acid-binding proteins, receptors for advanced glycation end products (RAGE), and extracellular matrix components. Its recombinant form typically includes purification tags (e.g., His-tag) for efficient isolation and experimental applications.

Research on recombinant S100A7 has advanced understanding of its dual roles: as a pro-inflammatory mediator activating NF-κB and MAPK pathways, and as a chemoattractant for immune cells. Paradoxically, it exhibits antimicrobial activity in skin defense while potentially fueling chronic inflammation in diseases. In cancer biology, studies using recombinant S100A7 highlight its involvement in tumor angiogenesis, immune evasion, and resistance to therapies. Recent work also explores its diagnostic potential as a biomarker in liquid biopsies and its therapeutic targeting using monoclonal antibodies or small-molecule inhibitors. Ongoing investigations aim to unravel context-dependent mechanisms, particularly its cross-talk with stromal cells in the tumor microenvironment.