Recombinant Human VNN3 protein

**Background of VNN3 Recombinant Protein**

VNN3 (Vanin-3), a member of the vanin protein family, is a glycosylphosphatidylinositol (GPI)-anchored ectoenzyme encoded by the *VNN3* gene in humans. The vanin family, including VNN1. VNN2. and VNN3. is evolutionarily conserved and characterized by pantetheinase activity, which hydrolyzes pantetheine to produce cysteamine and pantothenic acid (vitamin B5). These metabolites play critical roles in oxidative stress response, inflammation, and metabolic regulation. While VNN1 and VNN2 have been extensively studied in immune modulation and tissue repair, VNN3 remains less characterized, though it shares structural homology with other vanins, including a conserved catalytic domain.

VNN3 is predominantly expressed in specific tissues, such as the liver, kidneys, and gastrointestinal tract, suggesting organ-specific functions. Its GPI anchor enables membrane localization, potentially influencing cell-matrix interactions or signaling pathways. Studies implicate VNN3 in modulating cellular redox balance by regulating cysteamine levels, which affect glutathione synthesis and detoxification processes. Dysregulation of VNN3 has been loosely associated with metabolic disorders, inflammatory conditions, and cancer progression, though mechanistic insights are limited.

Recombinant VNN3 protein is produced via heterologous expression systems (e.g., mammalian or insect cells) to ensure proper post-translational modifications, such as glycosylation and GPI anchoring. This engineered protein serves as a tool to study VNN3’s enzymatic activity, substrate specificity, and interactions in vitro or in cellular models. It also aids in exploring therapeutic potential, such as targeting oxidative stress-related diseases or developing biomarkers. Despite its emerging relevance, further research is needed to fully elucidate VNN3’s physiological and pathological roles, distinguishing it from other vanin family members.