Recombinant Human SLFN5 protein

Schlafen family member 5 (SLFN5) is a multifunctional protein belonging to the Schlafen (SLFN) gene family, which is evolutionarily conserved in mammals and implicated in immune regulation, cell differentiation, and tumorigenesis. SLFN5. first identified in 2008. is characterized by an N-terminal Schlafen domain and a C-terminal helicase-like domain, though it lacks canonical enzymatic activity. It is widely expressed in immune cells (e.g., T cells, macrophages) and certain epithelial tissues, with its expression often modulated by interferons (IFNs) or cellular stress signals.

Functionally, SLFN5 regulates chromatin remodeling by interacting with histone deacetylases (HDACs) and other epigenetic modifiers, influencing gene transcription. It acts as a transcriptional repressor, suppressing viral replication by inhibiting promoter activity of viruses like HIV-1. In cancer biology, SLFN5 exhibits context-dependent roles: it may suppress tumor progression by enhancing chemotherapy sensitivity in some cancers (e.g., breast, gastric), yet promote metastasis in others (e.g., melanoma) through mechanisms involving epithelial-mesenchymal transition (EMT) or immune evasion.

Recombinant SLFN5 protein is typically produced in E. coli or mammalian expression systems, enabling studies on its structural features, post-translational modifications, and interaction partners. Its recombinant form aids in elucidating mechanisms of antiviral defense, immune checkpoint regulation, and tumor microenvironment modulation. Recent research highlights its potential as a therapeutic target or biomarker for immunotherapy response prediction. However, contradictory findings across cancer types emphasize the need for further investigation into its tissue-specific signaling networks and clinical relevance.