HRAS Antibodies

Structure of HRAS

HRAS is a small signal transduction protein with a molecular weight of approximately 21.3 kDa, and its precise molecular weight varies slightly among different splicing variants.

This protein is composed of 189 amino acids, and its tertiary structure forms typical RAS family folding features: with six β -folds at the core and five α -helices surrounding it. Amino acids at positions 12, 13 and 61 constitute the key "switch regions". Mutations at these sites can disrupt the hydrolytic activity of GTP, leading to the continuous activation of the protein. The CAAX motif at its C-terminal achieves membrane localization through fanicylation modification, a feature that is crucial for the cell's signal transduction function.

Fig. 1 Frequencies of HRAS mutations among solid cancer types.¹

Key structural properties of HRAS:

• Typical folded conformation of the RAS family
• GTP/GDP binding pockets and their surrounding switching regions
• Highly conserved phosphate-binding ring (P-loop) domains
• Amino acids at positions 12, 13 and 61 constitute mutation hotspots
• C-terminal CAAX motifs mediate membrane localization and signal transduction

Functions of HRAS

The main function of HRAS protein is to act as a molecular switch in cellular signal transduction. However, it is also involved in regulating various cellular physiological processes, including proliferation, differentiation and survival.

The affinity of HRAS for GTP exhibits typical single-molecule binding characteristics, in contrast to the synergistic effect of large signal complexes, which reflects its high response characteristics as a fundamental signal hub.

Applications of HRAS and HRAS Antibody in Literature

1. Mathiot, Laurent, et al. "HRAS Q61L mutation as a possible target for non-small cell lung cancer: Case series and review of literature." Current Oncology 29.5 (2022): 3748-3758. https://doi.org/10.3390/curroncol29050300

The article indicates that in non-small cell lung cancer, the incidence of HRAS p.glln61LEU mutation is approximately 0.25%, which is more common in smokers and often accompanied by pleural or pericardial effusion, with a poor prognosis. The current therapies have limited effects. The farnesyltransferase inhibitor tipifarnib may offer a new treatment direction for patients with this mutation.

2. Bièche, Ivan, et al. "HRAS is a therapeutic target in malignant chemo-resistant adenomyoepithelioma of the breast." Journal of Hematology & Oncology 14.1 (2021): 143. https://doi.org/10.1186/s13045-021-01158-3

Studies have found that hotspot mutations of HRAS G13R or G12S are common in malignant adenomyoepitheliomas of the breast. Patient-derived transplanted tumor models have confirmed that the MEK inhibitor trametinib has a significant therapeutic effect on this type of HRAS-mutated tumors, providing a potential treatment direction for advanced patients.

3. Lü, Guohua, et al. "LINC00623/miR-101/HRAS axis modulates IL-1β-mediated ECM degradation, apoptosis and senescence of osteoarthritis chondrocytes." Aging (Albany NY) 12.4 (2020): 3218. https://doi.org/10.18632/aging.102801

Research has found that HRAS is down-regulated in osteoarthritis. HRAS alleviates chondrocyte apoptosis and extracellular matrix degradation through the LINC00623/miR-101 molecular axis, thereby delaying the progression of osteoarthritis. This mechanism provides new potential targets for treatment.

4. Lindsey-Temple, Suzanna, et al. "A novel HRAS c. 466C> T p.(Phe156Leu) variant in two patients with attenuated features of Costello syndrome." European Journal of Human Genetics 30.9 (2022): 1088-1093. https://doi.org/10.1038/s41431-022-01139-1

The report found that the novel P. he156Leu mutation of HRAS can lead to Costrol syndrome. The patient presented with typical symptoms such as feeding difficulties and developmental delay, but the facial and skin features were relatively mild. Functional studies have shown that this mutation enhances downstream signal transduction, confirming the diversity of the pathogenic mechanisms of HRAS mutations.

5. Pareja, Fresia, et al. "Immunohistochemical assessment of HRAS Q61R mutations in breast adenomyoepitheliomas." Histopathology 76.6 (2020): 865-874. https://doi.org/10.1111/his.14057

This study evaluated the efficacy of RAS Q61R immunohistochemistry in detecting HRAS Q61R mutations in adenomyoepithelioma of the breast. The results show that this technique has a specificity of 100% and a sensitivity of 71%. It can effectively identify specific mutations in ER-negative cases and is a practical auxiliary diagnostic method.

Creative Biolabs: HRAS Antibodies for Research

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

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