Recombinant Human RNF181 protein

RNF181 (Ring Finger Protein 181) is a member of the RING finger protein family, characterized by a conserved zinc-binding RING domain that often confers E3 ubiquitin ligase activity. This protein is implicated in regulating ubiquitination, a post-translational modification critical for protein degradation, signaling, and cellular homeostasis. RNF181 is broadly expressed in human tissues, including the cardiovascular system, brain, and immune cells, suggesting diverse functional roles. Studies link it to cellular processes such as cell adhesion, proliferation, apoptosis, and inflammatory responses, though its precise molecular mechanisms remain under investigation.

Research highlights RNF181's interaction with integrins, key mediators of cell-extracellular matrix communication. By modulating integrin signaling pathways, RNF181 may influence platelet activation, vascular function, and immune cell trafficking. Its E3 ligase activity likely targets specific substrates for ubiquitination, potentially regulating their stability or interactions. Dysregulation of RNF181 has been associated with pathological conditions, including atherosclerosis, thrombosis, and cancer metastasis, positioning it as a potential therapeutic target or biomarker.

Recombinant RNF181 protein is produced using expression systems like *E. coli* or mammalian cells, often fused with tags (e.g., His-tag) for purification and detection. It serves as a vital tool for *in vitro* studies to elucidate RNF181's structure-function relationships, substrate specificity, and interaction networks. Current research aims to clarify its role in disease contexts and explore its utility in drug discovery or diagnostic applications. Despite progress, further work is needed to fully unravel its biological significance and translational potential.