Recombinant Human RRAGC protein

RRAGC (Ras-related GTP-binding protein C) is a member of the Rag GTPase family, which plays a critical role in nutrient-sensing signaling pathways, particularly the mechanistic target of rapamycin complex 1 (mTORC1) pathway. As a small GTPase, RRAGC cycles between GTP-bound (active) and GDP-bound (inactive) states, forming heterodimers with RagA/B or RagC/D to regulate mTORC1 localization and activity. This process is essential for cellular responses to amino acid availability, energy status, and growth signals, influencing processes like protein synthesis, autophagy, and metabolic homeostasis. Dysregulation of RRAGC-associated pathways is linked to diseases such as cancer, metabolic disorders, and neurodegenerative conditions.

Recombinant RRAGC proteins are engineered in vitro using expression systems (e.g., *E. coli*, mammalian cells) to produce purified, functional forms of the protein for research. These proteins retain GTP/GDP-binding capacity and interaction properties with binding partners like the Ragulator complex or GATOR1/GATOR2 regulators. Their production enables mechanistic studies on mTORC1 activation, nutrient signaling crosstalk, and mutations found in diseases (e.g., cancer-associated RRAGC variants). Recombinant RRAGC is also used in drug discovery to screen inhibitors targeting mTOR pathway components, with potential therapeutic applications. Structural studies using recombinant proteins have advanced understanding of Rag GTPase conformational changes during nutrient sensing. As a key node in cellular metabolism, RRAGC remains a focus for elucidating disease mechanisms and developing targeted therapies.