Recombinant Human HRASLS3 protein

HRASLS3 (HRAS-like suppressor 3), also known as PLA2G16 or H-REV107. is a member of the HRASLS (HRL) family of proteins, which share structural homology with the Ras GTPase superfamily but lack intrinsic GTPase activity. Initially identified as a tumor suppressor, HRASLS3 is implicated in regulating cell proliferation, differentiation, and apoptosis, particularly through its interaction with oncogenic Ras signaling pathways. The protein is characterized by an N-terminal acyltransferase/phospholipase A1 (PLA1) domain, enabling enzymatic activity in lipid metabolism, and a C-terminal domain involved in membrane association and protein-protein interactions.

HRASLS3 plays a dual role in lipid remodeling and tumor suppression. Its phospholipase activity contributes to the hydrolysis of phospholipids, influencing membrane dynamics, lipid droplet formation, and signaling pathways. Studies link HRASLS3 dysregulation to cancer progression, obesity, and metabolic disorders. For instance, reduced HRASLS3 expression correlates with poor prognosis in certain cancers, while its overexpression suppresses tumor growth by inducing apoptosis or inhibiting Ras-mediated oncogenesis.

Recombinant HRASLS3 protein is typically produced in bacterial (e.g., *E. coli*) or mammalian expression systems to study its biochemical properties, structure-function relationships, and therapeutic potential. Purified recombinant HRASLS3 is utilized in enzymatic assays to characterize lipid-modifying activities, screen inhibitors, or explore its role in cellular pathways via *in vitro* models. Its tumor-suppressive and metabolic regulatory functions make it a candidate for targeted drug development. Research also investigates its involvement in inflammation and viral infections, as some studies suggest interactions with viral entry mechanisms. Overall, HRASLS3 represents a multifunctional protein bridging lipid biology and disease pathogenesis.