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anti-Human PREX1 Antibodies:
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Human Polyclonal PREX1 Primary Antibody for ICC, IF - ABIN4342143
Lindsay, Lawn, Campbell, Faller, Rambow, Mort, Timpson, Li, Cammareri, Ridgway, Morton, Doyle, Hegarty, Rafferty, Murphy, McDermott, Sheahan, Pedone, Finn, Groben, Thomas, Hao, Carson, Norman et al.: P-Rex1 is required for efficient melanoblast migration and melanoma metastasis. ... in Nature communications 2011
Show all 3 Pubmed References
Human Polyclonal PREX1 Primary Antibody for ELISA, IHC (p) - ABIN4342144
Qin, Xie, Wang, Hoshino, Wolff, Zhao, Scofield, Dowd, Lin, Tu: Upregulation of PIP3-dependent Rac exchanger 1 (P-Rex1) promotes prostate cancer metastasis. in Oncogene 2009
a novel role for GRK2 as a target of TCR signaling that is responsible for TCR-induced transactivation of CXCR4 and TCR-CXCR4 complex formation that signals via PI3Kgamma/PREX1 to mediate cytokine production.
Authors suggest that control of P-Rex1 activity depends on a highly dynamic interplay among distinct signalling routes and its multisite phosphorylation is controlled by the action of different kinases.
PREX1 integrates dopamine receptor and phosphoinositide 3-kinase signaling to promote glioblastoma tumor cell invasion.
There is a significant association in the expression of P-Rex1 and MMP10 in human luminal breast cancer, and their co-expression is indicative of poor prognosis.
Data suggest that PREX1 and PREX2 share similarities in amino acid sequence, domain structure, activation by PIP(3) [phosphatidylinositol 3,4,5-triphosphate] and G-protein-coupled receptors beta/gamma subunits; expression of PREX1 and PREX2 is altered in many cancers. [REVIEW]
upon ligation of the T-cell antigen receptor (TCR), the TCR associates with and transactivates CXCR4 via phosphorylation of S339-CXCR4 in order to activate a PREX1-Rac1-signaling pathway that stabilizes interleukin-2(IL-2), IL-4, and IL-10 messenger RNA (mRNA) transcripts.
data point to multiple mechanisms of PREX1 negative regulation by PAKs within receptor tyrosine kinase and GPCR-stimulated signaling pathways
PREX1 overexpression reduced staurosporine-induced apoptosis whereas its shRNA knockdown promoted apoptosis in response to staurosporine or the anti-estrogen drug tamoxifen.
An unexpected role for P-Rex1 and Rac1 activation in the genesis of prostate cancer stem cells and resistance to bevacizumab and sunitinib.
P-Rex1 contributes to the spatiotemporal localization of type I PKA, which tightly regulates this guanine exchange factor by a multistep mechanism.
findings suggest a vital role of P-Rex1 signaling in CA1 LTD that is critical for social behavior and cognitive function and offer new insight into the etiology of ASDs
The P-Rex1-Rac1 interface is critical for Rac1 activation in breast cancer cells.
P-REX1 promotes both PI3K/AKT and MEK/ERK signaling in breast cancer.
PREX1 gene promoter hypomethylation is a prognostic marker of poor patient survival.
Phosphorylation of P-Rex1 at serine 1169 participates in IGF-1R signaling in breast cancer cells.
Cucurbitacin I also failed to affect the activation of P-Rex1 by heregulin.
These data suggest that P-Rex1 has an influence on physiological migratory processes, such as invasion of cancer cells, both through effects upon classical Rac1-driven motility and a novel association with RTK signalling complexes.
Studies indicate relevance of P-Rex1 and P-Rex2a, in breast tumorigenesis, and suggest that the exchange factors Vav2 and Vav3 play synergistic roles in breast cancer by sustaining tumor growth, neoangiogenesis, and metastasis.
We have identified a novel mechanism for direct activation of P-Rex1 through PP1alpha-dependent dephosphorylation.
Demonstrate presence of P-Rex1 in platelets as well as its role in platelet secretion and aggregation induced by low-dose agonists for g-protein coupled receptors and by collagen.
These findings identify P-Rex1 as a novel player of pulmonary fibrosis.
A novel mechanism of P-Rex1 regulation through the GPCR-adaptor protein Norbin.
Tiam1 and P-Rex1 promote Rac1 anti- and pro-migratory signalling cascades.
regulates GPCR-driven Rac signalling and actin polarity in neutrophils
Platelet P-Rex and Vav family Rac-GEFs play important proinflammatory roles in leukocyte recruitment.
We have elucidated a proliferative role of P-Rex1 when Rac1 is deleted in melanoblasts.
P-Rex1 may serve as a biomarker to predict response to single-agent PI3K inhibitors within a subset of breast cancers.
In vivo, in an ischemia-reperfusion-induced model of acute kidney injury, abolished selectin-mediated integrin activation contributed to decreased neutrophil recruitment and reduced kidney damage in P-Rex1-deficient mice.
P-rex1 expressed in endothelial cells is a critical mediator of vascular barrier disruption by an upstream pathway.
Data conclude that P-Rex1 has an important role in melanoblast migration and cancer progression to metastasis in mice and humans.
Studies identify a novel RacGEF in adipocytes as P-Rex1 that, at physiological insulin concentrations, functions as an insulin-dependent regulator of the actin cytoskeleton that contributes to GLUT4 trafficking to the plasma membrane.
Either P-Rex1 or Vav1 alone can produce sufficient active Rac for G protein-coupled receptor-dependent cell responses but under normal circumstances both contribute, presumably to ensure robust cell responses of primary neutrophils.
PI3K/P-Rex/Rac pathway is required for late phase long-term potentiation in the mouse cerebellum
P-Rex1 is an important regulator of neutrophil function by mediating a subset of Rac-dependent neutrophil responses.
P-Rex1 is a primary Rac2 guanine nucleotide exchange factor in mouse neutrophils.
P-Rex1 is one of the major GEFs in macrophage regulating Rac1 activation and chemotaxis.
The protein encoded by this gene acts as a guanine nucleotide exchange factor for the RHO family of small GTP-binding proteins (RACs). It has been shown to bind to and activate RAC1 by exchanging bound GDP for free GTP. The encoded protein, which is found mainly in the cytoplasm, is activated by phosphatidylinositol-3,4,5-trisphosphate and the beta-gamma subunits of heterotrimeric G proteins.
phosphatidylinositol-3,4,5-trisphosphate-dependent Rac exchange factor 1
, phosphatidylinositol 3,4,5-trisphosphate-dependent RAC exchanger 1
, phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein-like
, phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein
, ptdIns(3,4,5)-dependent Rac exchanger 1
, SET domain containing 6