Recombinant Human VSTM5 protein

VSTM5 (V-set and transmembrane domain-containing protein 5) is a poorly characterized protein belonging to the immunoglobulin (Ig) superfamily. It is encoded by the VSTM5 gene in humans and is predicted to function as a cell surface receptor or adhesion molecule, potentially involved in intercellular signaling or immune regulation. Structurally, it contains an extracellular V-set Ig-like domain, a transmembrane region, and a short cytoplasmic tail, suggesting roles in ligand binding and signal transduction. However, its precise biological functions, endogenous ligands, and downstream pathways remain largely unexplored.

Recombinant VSTM5 protein is engineered through molecular cloning techniques, typically expressed in mammalian cell systems (e.g., HEK293 or CHO cells) to ensure proper post-translational modifications such as glycosylation. This engineered protein often includes affinity tags (e.g., Fc-fusion or His-tag) for purification and detection. Current research focuses on elucidating its physiological role through in vitro binding assays, receptor-ligand interaction studies, and cellular signaling experiments. Some studies suggest potential associations with immune disorders, neurodegenerative conditions, or cancer progression, though these links require validation.

The development of recombinant VSTM5 has enabled structural characterization (e.g., crystallography) and antibody production for diagnostic applications. Challenges persist in defining its native expression patterns across tissues and clarifying conflicting data about its soluble versus membrane-bound forms. As an emerging target in biomedicine, further investigation of VSTM5 could reveal novel therapeutic strategies for diseases involving immune dysregulation or abnormal cell communication. Its recombinant form serves as a critical tool for bridging knowledge gaps between genetic information and functional proteomics.