SCAMP3 (Secretory Carrier Membrane Protein 3) is a crucial component of vesicular trafficking pathways and plays important roles in endocytosis and protein recycling. Previous studies demonstrate SCAMP3 dysregulation in various cancers, suggesting potential applications as a biomarker and therapeutic target. Understanding SCAMP3 expression and post-translational processing provides insights into its biological functions and potential applications in cancer diagnostics and therapy. In this study, we utilized transgenic Bombyx mori (silkworm) with the Bac-to-Bac expression system to produce recombinant SCAMP3. Protein expression was analyzed using Western blot and enzyme-linked immunosorbent assay (ELISA) techniques. Both methods confirmed successful SCAMP3 expression in transgenic silkworms. Western blot analysis revealed multiple protein products, indicating proteolytic processing during or following expression. This cleavage pattern may reflect functional protein maturation or processing, providing insights into SCAMP3 structural dynamics and functional domains. These findings demonstrate the utility of B. mori as a robust eukaryotic expression system for producing and studying proteins requiring complex post-translational modifications. The transgenic silkworm platform offers advantages for investigating structure-function relationships and generating proteins for potential therapeutic applications. © 2025 Selly S. Rajagukguk, Sabar Pambudi, Astari Dwiranti1, Doddy I. S. Utomo, Retno Lestari, Upi C. Nisa, Fadhillah, Anom Bowolaksono.