research use only
Cat.No.: F1263
| Dilution |
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|
| Application |
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| WB, IP, IF, FCM |
| Reactivity |
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| Human, Mouse, Rat, Monkey |
| Source |
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| Rabbit Monoclonal Antibody |
| Storage Buffer |
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| PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3 |
| Storage (from the date of receipt) |
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| -20°C (avoid freeze-thaw cycles), 2 years |
| Predicted MW |
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| 50 kDa |
| Positive Control | 293 cells; 293T cells; PANC-1 cells; mIMCD-3 cells; KNRK cells; NBT-II cells; HeLa cells |
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| Negative Control |
| Specificity |
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| RagC (D8H5) Rabbit mAb detects endogenous levels of total RagC protein. |
| Clone |
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| H17M14 |
| Synonym(s) |
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| Ras-related GTP-binding protein C; Rag C; RagC; GTPase-interacting protein 2; TIB929; RRAGC |
| Background |
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| RagC is a Ras-related small GTPase from the Rag family that acts as the GDP-bound subunit in RagA or RagB (GTP)-RagC or RagD (GDP) heterodimers, which are essential for recruiting mTORC1 to lysosomes and enabling amino acid-dependent activation of cell growth and metabolism. This protein contains an N-terminal GTPase domain with switch I and II regions that shift conformation based on nucleotide binding, as well as a C-terminal Roadblock domain that interacts with Ragulator or LAMTOR complexes for lysosomal anchoring. Key residues in the interswitch helix allow allosteric communication, coordinating RagA GTP loading with the RagC GDP conformation to support RAPTOR binding. RagC stabilize the active Rag heterodimer on the lysosome via Ragulator attachment, thus facilitating mTORC1 recruitment, where Rheb-GTP then allosterically activates mTORC1 to phosphorylate targets such as S6K1, 4E-BP1, and TFEB/TFE3. This drives anabolic processes like protein synthesis, lipid production, and lysosome biogenesis, while suppressing catabolic pathways. The GDP-bound state of RagC fixes RagA’s switch regions for high-affinity docking of the RAPTOR N-terminal cassette, preserving nutrient-responsive mTORC1 signaling without altering the complex’s structure. Oncogenic mutations in RagC can lead to amino acid-independent mTORC1 hyperactivation, resembling the effects seen in tuberous sclerosis, and dysregulation of this pathway is linked to both cancer and metabolic disorders. |
| References |
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