RICTOR Antibodies

Structure of RICTOR

RICTOR is a large-scale protein with a molecular weight of approximately 200 kDa. Its precise molecular weight varies among different species, mainly depending on the degree of splicing variants and post-translational modifications.

The RICTOR protein contains over 1,700 amino acid residues and interacts with proteins such as mTOR and mLST8 through multiple domains (such as the amino-terminal RBD domain and the central CRIM domain), jointly forming the structural framework of the mTORC2 complex. The secondary structure of this protein is dominated by α-helices, forming typical HEAT repeat sequences. These repeat units are arranged in a bow shape, constituting the binding interface for protein-protein interactions. The conserved region of its carboxyl terminal is crucial for the assembly and stability of the complex, while multiple variable regions are involved in regulating the subcellular localization and substrate-specific recognition of the complex.

Fig. 1 The mechanisms by which RICTOR participating in tumor growth, invasion and drug resistance.¹

Key structural properties of RICTOR:

• Extended conformation composed of multiple domains
• Contains amino end mediated RBD structure of protein interaction domain
• The central CRIM domain is involved in the assembly of the mTORC2 complex
• The carboxyl terminus contains multiple phosphorylation sites and is involved in signal regulation

Functions of RICTOR

The primary function of RICTOR is to serve as the core scaffold and regulatory protein of the mTORC2 complex, participating in cell survival, metabolism, proliferation, and signal integration of cytoskeletal tissue. Its specific functions are as follows:

Unlike the mTORC1 pathway, which mainly senses nutritional and energy status and regulates anabolic metabolism, the signal response of mTORC2 is more complex. Its function is mainly reflected in the response to growth factor signals and the phosphorylation modification of downstream kinases (such as Akt and PKC), and it often shows abnormal activation in cancer occurrence.

Applications of RICTOR and RICTOR Antibody in Literature

1. Wang, Xinyue, et al. "A novel rabbit anti-myoglobin monoclonal antibody's potential application in rhabdomyolysis associated acute kidney injury." International Journal of Molecular Sciences 24.9 (2023): 7822. https://doi.org/10.1002/ctm2.1686

This study explored the role of the Rictor/mTORC2 signaling pathway in interstitial fibrosis after kidney transplantation. Research has found that Rictor degrades BNIP3 through K48 ubiquitination, inhibits mitochondrial autophagy, and promotes endothelial-mesenchymal transition and fibrosis. Inhibiting Rictor can enhance BNIP3-mediated mitochondrial autophagy, thereby improving fibrosis, indicating its potential as a therapeutic target.

2. Szalai, Fatime, et al. "Rictor—a mediator of progression and metastasis in lung cancer." Cancers 16.3 (2024): 543. https://doi.org/10.3390/cancers16030543

This study indicates that RICTOR gene amplification and protein overexpression can activate mTORC2, promoting the migration and metastasis of lung cancer cells. Studies have shown that inhibiting Rictor/mTORC2 can effectively reduce tumor metastasis, and it has significant potential as a therapeutic target and predictive marker.

3. Ponzone, Luca, et al. "RICTOR/mTORC2 downregulation in BRAFV600E melanoma cells promotes resistance to BRAF/MEK inhibition." Molecular Cancer 23.1 (2024): 105. https://doi.org/10.1186/s12943-024-02010-1

This study indicates that in BRAF-mutated melanoma, low RICTOR levels predict poor efficacy and prognosis of targeted therapy. Studies have found that the absence of RICTOR leads to resistance to BRAF/MEK inhibitors by activating the NAMPT-mitochondrial electron transport chain axis. Inhibiting this pathway can restore drug sensitivity, suggesting that RICTor levels have prognostic and therapeutic guiding value.

4. Wang, Chun, et al. "Rictor mediates p53 deactivation to facilitate the malignant transformation of hepatocytes and promote hepatocarcinogenesis." Journal of Translational Medicine 21.1 (2023): 919. https://doi.org/10.1186/s12967-023-04799-9

This study indicates that in hepatocellular carcinoma (HCC), Rictor exerts a promoting effect by binding to and inhibiting the activity of wild-type p53, and its dynamic nucleoplasmic translocation is associated with malignant progression. miR-192 targets and inhibits Rictor, restores p53 function and slows tumor growth. High expression of Rictor indicates a poor prognosis.

5. Jebali, Ahlem, and Nicolas Dumaz. "The role of RICTOR downstream of receptor tyrosine kinase in cancers." Molecular cancer 17.1 (2018): 39. https://doi.org/10.1186/s12943-018-0794-0

This study indicates that RICTOR is a key component of the mTORC2 complex and acts as an important signaling node in RTK-abnormal tumors to mediate carcinogenesis. Recent studies have found that RICTor variations are widely present in various cancers and have become a promising therapeutic target for RTK in tumor modification.

Creative Biolabs: RICTOR Antibodies for Research

Creative Biolabs specializes in the production of high-quality RICTOR antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom RICTOR Antibody Development: Tailor-made solutions to meet specific research requirements.
• Bulk Production: Large-scale antibody manufacturing for industry partners.
• Technical Support: Expert consultation for protocol optimization and troubleshooting.
• Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our RICTOR antibodies, custom preparations, or technical support, contact us at email.