|Other Names||Rho guanine nucleotide exchange factor 18, 114 kDa Rho-specific guanine nucleotide exchange factor, p114-Rho-GEF, p114RhoGEF, Septin-associated RhoGEF, SA-RhoGEF, ARHGEF18, KIAA0521|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPases. May play a role in actin cytoskeleton reorganization in different tissues since its activation induces formation of actin stress fibers. Also act as a GEF for RAC1, inducing production of reactive oxygen species (ROS). Does not act as a GEF for CDC42. The G protein beta-gamma (Gbetagamma) subunits of heterotrimeric G proteins act as activators, explaining the integrated effects of LPA and other G-protein coupled receptor agonists on actin stress fiber formation, cell shape change and ROS production.|
|Cellular Location||Cytoplasm. Note=Colocalizes with actin stress fibers|
|Tissue Location||Expressed in all tissues tested with highest expression in kidney and pancreas. Weakly or not expressed in liver, skeletal muscle and testis.|
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Provided below are standard protocols that you may find useful for product applications.
Rho GTPases are GTP binding proteins that regulate a widespectrum of cellular functions. These cellular processes includecytoskeletal rearrangements, gene transcription, cell growth andmotility. Activation of Rho GTPases is under the direct control ofguanine nucleotide exchange factors (GEFs). The protein encoded bythis gene is a guanine nucleotide exchange factor and belongs tothe Rho GTPase GFE family. Family members share a common feature, aDbl (DH) homology domain followed by a pleckstrin (PH) homologydomain. Alternatively spliced transcript variants encodingdifferent isoforms have been identified.
Ichikawa, S., et al. J. Bone Miner. Res. 25(8):1821-1829(2010)Niu, J., et al. Circ. Res. 93(9):848-856(2003)Rabizadeh, S., et al. Cytokine Growth Factor Rev. 14 (3-4), 225-239 (2003) :Salehi, A.H., et al. J. Biol. Chem. 277(50):48043-48050(2002)Harrington, A.W., et al. J. Neurosci. 22(1):156-166(2002)
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