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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
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.
HDACs could regulate P-Rex1 gene transcription by interaction with Sp1 and by region-specific changes in histone acetylation within the P-Rex1 promoter
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