research use only

RagC Antibody [H17M14]

Cat.No.: F1263

    Application: Reactivity:

    Usage Information

    Dilution
    1:1000
    1:50
    1:50 - 1:200
    1:200 - 1:800
    Application
    WB, IP, IF, FCM
    Reactivity
    Human, Mouse, Rat, Monkey
    Source
    Rabbit Monoclonal Antibody
    Storage Buffer
    PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3
    Storage (from the date of receipt)
    -20°C (avoid freeze-thaw cycles), 2 years
    Predicted MW
    50 kDa
    Positive Control 293 cells; 293T cells; PANC-1 cells; mIMCD-3 cells; KNRK cells; NBT-II cells; HeLa cells
    Negative Control

    Datasheet & SDS

    Biological Description

    Specificity
    RagC (D8H5) Rabbit mAb detects endogenous levels of total RagC protein.
    Clone
    H17M14
    Synonym(s)
    Ras-related GTP-binding protein C; Rag C; RagC; GTPase-interacting protein 2; TIB929; RRAGC
    Background
    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
    • https://pubmed.ncbi.nlm.nih.gov/20381137/
    • https://pubmed.ncbi.nlm.nih.gov/31601764/

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