WFDC1 (WAP four-disulfide core domain protein 1), also known as PS20 or SWC3. is a secreted glycoprotein belonging to the WAP-type protease inhibitor family. It contains a conserved WAP domain characterized by eight cysteine residues forming four disulfide bonds, which is critical for its structural stability and functional interactions. Initially identified in prostate stromal cells, WFDC1 is broadly expressed in extracellular matrices and body fluids, including seminal plasma, saliva, and bronchoalveolar lavage fluid.
Functionally, WFDC1 has been implicated in tissue remodeling, immune regulation, and tumor suppression. Studies suggest it may inhibit serine proteases, modulate cell adhesion, and interact with integrins or growth factors to influence cellular signaling. Its role in cancer is context-dependent: WFDC1 acts as a tumor suppressor in prostate cancer, glioblastoma, and non-small cell lung cancer by regulating apoptosis and metastasis, while exhibiting oncogenic properties in certain ovarian cancers. It also participates in inflammatory responses, such as modulating neutrophil activity in rheumatoid arthritis.
WFDC1 antibodies are essential tools for detecting protein expression, localization, and interaction partners in research. They are widely used in techniques like Western blotting, immunohistochemistry, and ELISA. Commercial antibodies target specific epitopes, with validation often involving knockout cell lines or recombinant protein controls. Recent studies utilizing WFDC1 antibodies have expanded insights into its diagnostic potential and therapeutic targeting in fibrosis, chronic inflammation, and cancer progression.