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anti-Human ARHGEF1 Antikörper:
anti-Mouse (Murine) ARHGEF1 Antikörper:
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Human Polyclonal ARHGEF1 Primary Antibody für WB - ABIN2801964
Hart, Sharma, elMasry, Qiu, McCabe, Polakis, Bollag: Identification of a novel guanine nucleotide exchange factor for the Rho GTPase. in The Journal of biological chemistry 1996
Show all 3 Pubmed References
Human Monoclonal ARHGEF1 Primary Antibody für IF, ELISA - ABIN522597
Zizer, Beilke, Bäuerle, Schilling, Möhnle, Adler, Fischer, Wagner: Loss of Lsc/p115 protein leads to neuronal hypoplasia in the esophagus and an achalasia-like phenotype in mice. in Gastroenterology 2010
Human Polyclonal ARHGEF1 Primary Antibody für ICC, IF - ABIN4281534
Stadler, Rexhepaj, Singan, Murphy, Pepperkok, Uhlén, Simpson, Lundberg: Immunofluorescence and fluorescent-protein tagging show high correlation for protein localization in mammalian cells. in Nature methods 2013
High ARHGEF1 expression is associated with asthmatic airway hyper-responsiveness.
Data suggest that MCP1/CCL2 induces activation/tyrosine phosphorylation of ARHGEF1/p115-RhoGEF and up-regulates RAC1 signaling in vascular smooth muscle cells (VSMCs); ARHGEF1 inhibition suppresses MCP1-induced VSMC migration and proliferation. (ARHGEF1 = Rho guanine nucleotide exchange factor 1; RAC1 = Rac family small GTPase 1; CCL2 = C-C motif chemokine ligand 2)
Data indicate that the crystal structure of PDZ-RhoGEF PDZ domain in complex with the CXC chemokine receptor 2 (CXCR2) C-terminal PDZ binding motif.
We have reported here for the first time a reduced activity of both Rac1 and Cdc42 in human pheochromocytoma resection as well as tumor-associated expression changes of FARP1, ARHGEF1, and ARHGAP36
contactin-1 displayed the ability to phosphorylate the RhoA activator p115 RhoGEF
The novel role for p115RhoGEF in regulation of epithelial plasticity is dependent on Rho-DRF signaling module.
Regulated localization is sufficient for hormonal control of regulator of G protein signaling homology Rho guanine nucleotide exchange factors (RH-RhoGEFs).
Modification of p115RhoGEF at Serine(330) regulates its RhoGEF activity.
The action of DOCK7 in vivo may involve the coordinated integration of Cdc42/Rac1 signaling in the context of the membrane recruitment of a DOCK7 guanine nucleotide exchange factor (GEF) complex.
High GEF1 expression is associated with metastasis of pancreatic cancer.
Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.
Upon beta(2)AR activation, both betaArrestin2 and p115RhoGEF translocate to the plasma membrane, with concomitant activation of RhoA and formation of focal adhesions and stress fibers.
Thromboxane receptor signaling is required for fibronectin-induced matrix metalloproteinase 9 production by human and murine macrophages and is attenuated by the Arhgef1 molecule.
Mechanistic insights into specificity, activity, and regulatory elements of the regulator of G-protein signaling (RGS)-containing Rho-specific guanine nucleotide exchange factors (GEFs) p115, PDZ-RhoGEF (PRG), and leukemia-associated RhoGEF (LARG).
The linker region connecting the N-terminal RGS-homology domain and the Dbl homology domain inhibits the intrinsic guanine nucleotide exchange activity of p115.
ARHGEF1 is involed in hypertension by controlling its molecular mechanisms.
coexpression of a dominant negative PDZ-RhoGEF abrogated the ability of plexin-B1 to cause stress fiber formation
rgRGS domain may serve a structural or allosteric role in the regulation of the nucleotide exchange activity of p115RhoGEF on Rho by Galpha(13)
CD44 interaction with p115RhoGEF and ROK plays a pivotal role in promoting Gab-1 phosphorylation leading to Gab-1.PI 3-kinase membrane localization, AKT signaling, and cytokine (M-CSF) production during HA-mediated breast cancer progression
data demonstrate a pathway of Rho activation involving protein kinase c alpha-dependent phosphorylation of p115Rho guanine exchange factor
data highlight the importance of Arhgef1 in cardiovascular disease and suggest targeting Arhgef1 as a potential therapeutic strategy against atherosclerosis.
Arhgef1 controls the process of neurite formation in newborn cortical neurons derived from neural progenitor cells
these findings reveal that Arhgef1 functions as a negative regulator of neurite outgrowth through regulating RhoA-cofilin pathway and actin dynamics.
Results show that PKC-alpha phosphorylation of p115RhoGEF mediates TNF-alpha signaling to RhoA, and that this plays a critical role in signaling F-actin rearrangement and barrier dysfunction in endothelial cells.
lsc/p115 deficiency results in impaired neuronal innervation and in motor dysfunction recapitulating several aspects of esophageal achalasia.
These data demonstrate that Arhgef1 regulates alpha5beta1-mediated MMP expression by macrophages and that loss of Arhgef1 by leukocytes leads to pulmonary pathology.
results show that control of RhoA signaling through Arhgef1 is central to the development of angiotensin II-dependent hypertension and identify Arhgef1 as a potential target for the treatment of hypertension
First, Lsc homo-oligomerizes and is negatively regulated through domains in its C terminus; and second, functionally distinct isoforms of Lsc lacking these domains are present in the spleen.
Lsc is essential for mediating TXA(2 )signaling involved in apoptosis and actin organization and suggest that TXA(2) regulates thymic cellularity via Lsc.
Lsc is a RhoA guanine nucleotide exchange factor that binds the heterotrimeric G-protein alpha-subunits, Galpha12 and Galpha13.
lsc(-/-) marginal-zone B cells do not traffick appropriately in an immune response
T cells depend on Arhgef1 to promote lung inflammation, and a deficiency in Arhgef1 results in reduced T cell-CD11c+ antigen-presenting cell interaction
These data demonstrate that Lsc regulates integrin-mediated adhesive events at the trailing edge of migrating cells.
Replacement of key residues in this motif with their counterparts in p115RhoGEF confers GAP activity.
Rho GTPases play a fundamental role in numerous cellular processes that are initiated by extracellular stimuli that work through G protein coupled receptors. The encoded protein may form complex with G proteins and stimulate Rho-dependent signals. Multiple alternatively spliced transcript variants have been found for this gene, but the full-length nature of some variants has not been defined.
rho guanine nucleotide exchange factor (GEF) 1
, Rho guanine nucleotide exchange factor (GEF) 1
, rho guanine nucleotide exchange factor 1-like
, 115 kDa guanine nucleotide exchange factor
, 115-kD protein
, Lsc homolog
, rho guanine nucleotide exchange factor 1
, lbc's second cousin
, lymphoid blast crisis like 2
, lymphoid blast crisis-like 2