Recombinant Human RRAGA protein

**Background of RRAGA Recombinant Protein**

RRAGA (Ras-related GTP-binding protein A) is a member of the Rag GTPase family, a subgroup of small GTPases critical for cellular nutrient sensing and signaling. These proteins function as heterodimers (typically RagA/B paired with RagC/D) and play a central role in regulating the mechanistic target of rapamycin complex 1 (mTORC1), a master regulator of cell growth, metabolism, and autophagy. RRAGA specifically binds GTP, while its partner Rag GTPase binds GDP, creating an active conformation that recruits mTORC1 to lysosomal surfaces in response to nutrient availability, particularly amino acids. This interaction enables mTORC1 to phosphorylate downstream targets, promoting anabolic processes and suppressing catabolic pathways like autophagy.

Recombinant RRAGA protein is engineered in vitro using expression systems (e.g., *E. coli* or mammalian cells*) to study its structure, function, and interactions within the mTORC1 pathway. Its production often involves tags (e.g., GST, His) for purification and detection. Researchers utilize RRAGA recombinant proteins to investigate dysregulated nutrient signaling in diseases such as cancer, metabolic disorders, and neurodegenerative conditions, where mTORC1 hyperactivity is frequently observed. Additionally, it serves as a tool for screening therapeutic agents targeting the Rag GTPase-mTORC1 axis, a promising avenue for diseases linked to aberrant cell growth or autophagy. The recombinant protein’s stability and activity are rigorously validated to ensure its utility in biochemical assays, structural studies, and drug discovery.