RhoGEF p115 Polyclonal Antibody
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Application ![]()
| WB |
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Primary Accession | Q92888 |
Reactivity | Human, Mouse, Rat |
Host | Rabbit |
Clonality | Polyclonal |
Calculated MW | 102435 Da |
Gene ID | 9138 |
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Other Names | ARHGEF1; Rho guanine nucleotide exchange factor 1; 115 kDa guanine nucleotide exchange factor; p115-RhoGEF; p115RhoGEF; Sub1.5 |
Dilution | WB~~Western Blot: 1/500 - 1/2000. ELISA: 1/40000. Not yet tested in other applications. |
Format | Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.09% (W/V) sodium azide. |
Storage Conditions | -20℃ |
Name | ARHGEF1 |
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Function | Seems to play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13) subunits (PubMed:9641915, PubMed:9641916). Acts as a GTPase-activating protein (GAP) for GNA12 and GNA13, and as guanine nucleotide exchange factor (GEF) for RhoA GTPase (PubMed:30521495, PubMed:8810315, PubMed:9641915, PubMed:9641916). Activated G alpha 13/GNA13 stimulates the RhoGEF activity through interaction with the RGS-like domain (PubMed:9641916). This GEF activity is inhibited by binding to activated GNA12 (PubMed:9641916). Mediates angiotensin-2-induced RhoA activation (PubMed:20098430). In lymphoid follicles, may trigger activation of GNA13 as part of S1PR2-dependent signaling pathway that leads to inhibition of germinal center (GC) B cell growth and migration outside the GC niche. |
Cellular Location | Cytoplasm. Membrane. Note=Translocated to the membrane by activated GNA13 or LPA stimulation |
Tissue Location | Ubiquitously expressed. |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
Seems to play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13) subunits. Acts as GTPase-activating protein (GAP) for GNA12 and GNA13, and as guanine nucleotide exchange factor (GEF) for RhoA GTPase. Activated G alpha 13/GNA13 stimulates the RhoGEF activity through interaction with the RGS-like domain. This GEF activity is inhibited by binding to activated GNA12. Mediates angiotensin-2- induced RhoA activation.

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