|Positive WB detected in||HL-60 cells, PC-12 cells, HeLa cells, MCF-7 cells, rat brain tissue|
|Positive IF detected in||HeLa cells|
|Western Blot (WB)||WB : 1:500-1:2000|
|Immunofluorescence (IF)||IF : 1:50-1:500|
|Sample-dependent, check data in validation data gallery|
10749-1-AP targets RHOA in WB, IHC, IF,ELISA applications and shows reactivity with human, mouse, rat samples.
|Tested Reactivity||human, mouse, rat|
|Cited Reactivity||human, mouse, rat|
|Host / Isotype||Rabbit / IgG|
|Immunogen||RHOA fusion protein Ag1141|
|Full Name||ras homolog gene family, member A|
|Calculated molecular weight||22 kDa|
|Observed molecular weight||22 kDa|
|GenBank accession number||BC005976|
|Gene ID (NCBI)||387|
|Purification Method||Antigen affinity purification|
|Storage Buffer||PBS with 0.02% sodium azide and 50% glycerol pH 7.3.|
|Storage Conditions||Store at -20°C. Stable for one year after shipment. Aliquoting is unnecessary for -20oC storage.|
What is the function of RhoA?
Ras homolog gene family, member A (RhoA) is a small GTPase that is involved in cytoskeleton organization.1 It is important in actomyosin contractility, as when RhoA binds to GTP it initiates a cascade of events mediating stress fiber or contractile ring formation, where actin bundles crosslink with other proteins. It is also associated with actin polymerization, making RhoA important in membrane ruffling and cell motility.2 The role of RhoA is essential in cell migration and adhesion.
What is the cellular localization of RhoA?
In motile cells, a leading edge stretches ahead, stabilizes, the cytoskeleton is reorganized, and the tail of the cell retracts. The role of RhoA in contracting actomyosin has linked RhoA with the tail retraction in this process, but studies into the spatiotemporal kinetics of GTPases have revealed that RhoA is also located at the leading edge of migrating cells.3 This highlights the dual roles of this protein in actin contractility and polymerization.
What is the role of RhoA in disease?
Though it is not an oncogene, the role of RhoA in adhesion and migration has implicated this protein in cancer biology. Expression of RhoA has been found to be higher in malignant tumors compared to benign tumors or in non-tumor tissue, and more invasive tumors have been found to overexpress RhoA.4 This protein is also implicated in neurodegenerative diseases and aging due to its role in axon guidance, with abnormal localization of RhoA associated with Alzheimer’s and Parkinson’s pathology.5,6
1. Ridley, A. J. & Hall, A. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70, 389–399 (1992).
2. 21. Kurokawa, K. & Matsuda, M. Localized RhoA Activation as a Requirement for the Induction of Membrane Ruffling. Mol. Biol. Cell 16, 4294–4303 (2005).
3. 22. Struckhoff, A. P., Rana, M. K. & Worthylake, R. A. RhoA can lead the way in tumor cell invasion and metastasis. Front. Biosci. (Landmark Ed. 16, 1915–26 (2011).
4. 23. Mcglasson, S. et al. Rare variants of the 3’-5’ DNA exonuclease in early onset TREX1 small vessel stroke [version 1; referees: awaiting peer review]. doi:10.12688/wellcomeopenres.12631.1
5. 24. Huesa, G. et al. Altered Distribution of RhoA in Alzheimer’s Disease and AβPP Overexpressing Mice. J. Alzheimer’s Dis. 19, 37–56 (2010).
6. 25. Hynds, D. L. Subcellular localization of Rho GTPases: implications for axon regeneration. Neural Regen. Res. 10, 1032–3 (2015).
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