Rho-related GTP-binding protein RhoC (176-185)

Rho-related GTP-binding protein RhoC

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.

CAT No: ta-397

Synonyms/Alias:Rho-related GTP-binding protein RhoC (176-185)

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Sequence
RAGLQVRKNK
Areas of Interest
Antigen-presenting Cells; Cancer Research

Rho-related GTP-binding protein RhoC (176-185) is a synthetic peptide fragment derived from the C-terminal region of the RhoC protein, a member of the Rho family of small GTPases. This peptide encompasses residues 176 to 185, representing a functionally relevant sequence motif associated with the regulation of cytoskeletal dynamics, cell migration, and intracellular signaling pathways. As RhoC is recognized for its involvement in actin filament organization and cellular motility, the peptide fragment provides a valuable biochemical tool for dissecting the structural and functional properties of RhoC and its interaction networks. Researchers utilize such peptides to probe the molecular mechanisms underpinning Rho-mediated signal transduction and to facilitate the study of protein-protein interactions within the broader context of cell biology and cancer research.

Peptide mapping: As a defined sequence corresponding to a specific region of RhoC, the 176-185 peptide is frequently employed in peptide mapping studies. By serving as a reference standard, it enables mass spectrometric analysis and epitope mapping to confirm the identity and post-translational modifications of the native RhoC protein. Such applications are critical for characterizing protein isoforms, validating antibody specificity, and elucidating structural motifs essential for RhoC's biological activity.

Protein-protein interaction studies: The RhoC (176-185) peptide is instrumental in investigating the binding interfaces between RhoC and its effector proteins or regulatory partners. By mimicking a native segment of the full-length protein, the peptide can be used in pull-down assays, surface plasmon resonance, or fluorescence polarization experiments to define interaction affinities, map critical contact residues, and uncover the molecular determinants governing RhoC-mediated signaling. These insights are valuable for understanding how RhoC orchestrates cytoskeletal remodeling and cell motility.

Antibody production and validation: Synthetic peptides such as RhoC (176-185) are widely utilized as immunogens for generating sequence-specific polyclonal or monoclonal antibodies. The defined sequence allows for the selective targeting of the C-terminal epitope of RhoC, facilitating the development of reagents for immunoblotting, immunoprecipitation, or immunofluorescence applications. The peptide also serves as a crucial control for antibody validation, ensuring specificity and minimizing cross-reactivity with related Rho GTPases.

Cell signaling assays: In cell-based or in vitro signaling assays, this peptide fragment can be used as a competitive inhibitor or as a probe to dissect the downstream consequences of RhoC activation. By introducing the peptide into cellular systems, researchers can modulate or track the involvement of RhoC in pathways regulating actin cytoskeleton organization, focal adhesion dynamics, and cell migration. These applications provide mechanistic insights into RhoC's functional roles in processes such as metastasis, wound healing, and tissue remodeling.

Peptide-based assay development: The RhoC (176-185) sequence is also valuable for the design and optimization of peptide-based assays, including enzyme-linked immunosorbent assays (ELISA) and high-throughput screening platforms. Its well-defined structure and biochemical relevance enable the establishment of robust detection systems for monitoring RhoC expression, post-translational modifications, or inhibitor screening. Such assays are essential for advancing research in cell signaling, cancer biology, and drug discovery targeting Rho GTPase pathways.

Source#
Homo sapiens (human)
Epitope
176-185
Restricting HLA
HLA-A3
References
Wenandy; Cancer Immunol Immunother 2008

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