RRAS Antibodies

Structure of RRAS

The RRAS gene encodes a small GTP-binding protein with a molecular weight of approximately 21.5 kDa. There are slight differences in this molecular weight among different species, mainly due to the substitution of individual amino acids in the RAS domain.

This protein is composed of 189 amino acids and presents a classic GTPase folding structure. Its three-dimensional structure contains a RAS domain composed of six β -folded sheets and five α -helices, which forms a highly conserved nucleotide binding pocket. The GTP hydrolytic activity of this protein depends on the glycine residue in its P-ring (G1 motif) and the glutamine residue in the G3 motif. The threonine residue located in the switch I region (G2 motif) directly participates in the hydrolysis process of GTP, while the switch II region (G4 motif) is responsible for recognizing downstream effector molecules, thereby transmitting the activation signal of GTP binding to pathways such as MAPK.

Fig. 1 R-Ras molecular structure and domains.¹

Key structural properties of RRAS:

• Classical GTPase folded conformation
• Conserved nucleotide-binding pockets
• Switch I/II conformational changes determine the functional state
• The effector domain mediates downstream signal conduction

Functions of RRAS

The core function of the RRAS gene is to act as a molecular switch to regulate intracellular signal transduction. However, it is also involved in a variety of cellular physiological processes, including cytoskeletal recombination and regulation of cell adhesion.

Compared with the classic HRAS and KRAS, RRAS has a higher sensitivity to GAP proteins, which enables a faster GTP hydrolysis rate. This characteristic makes it particularly suitable for functioning in physiological processes that require rapid signal termination, such as local adhesion spot turnover during cell migration.

Applications of RRAS and RRAS Antibody in Literature

1. Miller, John P., et al. "A genome-scale RNA–Interference screen identifies RRAS signaling as a pathologic feature of Huntington's disease." PLoS genetics 8.11 (2012): e1003042. https://doi.org/10.1371/journal.pgen.1003042

The article indicates that a genomic screening found that the pathogenic protein of Huntington's disease abnormally activates the RRAS signaling pathway. In cell and animal models, reducing the function of RRAS or its pathway components can effectively alleviate toxicity, suggesting that this pathway is a potential new target for drug treatment.

2. Perrot, Carole Y., Junko Sawada, and Masanobu Komatsu. "Prolonged activation of cAMP signaling leads to endothelial barrier disruption via transcriptional repression of RRAS." The FASEB Journal 32.11 (2018): 5793. https://doi.org/10.1096/fj.201700818RRR

The article indicates that long-term elevated cAMP signaling can inhibit the expression of the RRAS gene through the transcription factor CREB3. The reduction of RRAS disrupts endothelial cell junctions, ultimately leading to impaired vascular barrier function and abnormally increased permeability.

3. Alcover‐Sanchez, Berta, et al. "R‐Ras1 and R‐Ras2 regulate mature oligodendrocyte subpopulations." Glia 73.4 (2025): 701-719. https://doi.org/10.1002/glia.24643

Studies have shown that R-Ras1 and R-Ras2 are the key factors for balancing different subsets of mature oligodendrocytes (MOL). When the function of RRAS is reduced or absent, it will disrupt the normal proportion of subgroups, leading to an abnormal increase in the MOL1 subgroup and a decrease in the MOL2 and MOL5/6 subgroups, thereby affecting myelin formation.

4. Iida, Takaya, et al. "Functional analysis of RRAS2 pathogenic variants with a Noonan-like phenotype." Frontiers in Genetics 15 (2024): 1383176. https://doi.org/10.3389/fgene.2024.1383176

Research has found that novel pathogenic mutations in the RRAS2 gene (such as P. Gly23val) can abnormally enhance its function, thereby overactivating the RAS signaling pathway. This functional gain causes developmental malformations and high mortality rates in fruit fly and zebrafish models, leading to a Nounan syndrome-like phenotype in humans.

5. Alcover-Sanchez, Berta, et al. "R-Ras GTPases signaling role in myelin neurodegenerative diseases." International Journal of Molecular Sciences 21.16 (2020): 5911. https://doi.org/10.3390/ijms21165911

The review indicates that myelin formation is regulated by signaling pathways such as PI3K, ERK and Wnt. Ras GTPases (including R-Ras) are key participants in these pathways and may act as cross-dialogue nodes among them to coordinate the myelination process, thus being regarded as potential therapeutic research targets.

Creative Biolabs: RRAS Antibodies for Research

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

• Custom RRAS 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 RRAS antibodies, custom preparations, or technical support, contact us at email.