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In addition to accelerate GTP gamma S binding by ARFs of all three classes, it appears to function preferentially as a guanine nucleotide exchange protein for ARF6, mediating internalisation of beta-1 integrin.. De plus, nous expédions IQSEC1 Anticorps (10) et beaucoup plus de produits pour cette protéine.
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both Arf6 activation through GluN2B-BRAG1 during early development and the transition from BRAG1- to BRAG2-dependent Arf6 signaling induced by the GluN2 subunit switch are critical for the development of mature glutamatergic synapses.
Brag2 is essential for developmental and pathological angiogenesis by promoting endothelial cell sprouting through regulation of adhesion by beta1-integrin internalization and link for the first time the process of beta1-integrin endocytosis with angiogenesis.
The EGFR-GEP100-Arf6 axis affected the prognosis of patients with primary lung adenocarcinoma.
Data show that co-overexpression of GEP100 and AMAP1 (ASAP1) correlates with rapidity of the local recurrence.
GEP100 regulates an Arf6/ERK/uPAR signaling cascade in EGF-induced breast cancer cell invasion.
GEP100 plays a significant role in pancreatic cancer invasion through regulating the expression of E-cadherin and the process of mesenchymal to epithelial transition (MET).
BRAG2 acts at clathrin-coated pits to promote integrin internalization by activating Arf5 and suggest a previously unrecognized role for Arf5 in clathrin-mediated endocytosis of specific cargoes.
GEP100/Arf6 is required for epidermal growth factor-induced ERK/Rac1 signaling and cell migration in human hepatoma HepG2 cells.
The PH domain and the interdomain linker of Brag2 may be targets for selectively regulating the activity of Brag2.
Data suggest that GEP100-Arf6-AMAP1-cortactin pathway, activated by VEGFR2, appears to be common in angiogenesis and cancer invasion and metastasis, and provides their new therapeutic targets.
Cinical study indicates that co-overexpression of Her2 with GEP100 in primary lung adenocarcinomas of patients is correlated with the presence of their node-metastasis with a statistical significance.
a novel phospholipid-regulated antiangiogenic signaling pathway whereby Sema3E activates Arf6 through Plexin-D1 and consequently controls integrin-mediated endothelial cell attachment to the extracellular matrix and migration.
GEP100 functions in phagocytosis via its role in ARF6-dependent actin remodeling.
Arf6 regulates both endocytosis and recycling of beta1 integrins and BRAG2 (IQSEC1) functions selectively to activate Arf6 during integrin internalization
Guanine nucleotide-exchange protein (GEP) 100/BRAG2 has an important role in the activation of ADP-ribosylation factor (ARF)6 for its functions in both E-cadherin recycling and actin remodeling.
Results indicate that GEP100 links EGFR signalling to Arf6 activation to induce invasive activities of some breast cancer cells, and hence may contribute to their metastasis and malignancy.
The present study provided evidence that BRAG2a is a novel component of the photoreceptor dystrophin-associated glycoprotein complex (DGC), suggesting functional involvement of the BRAG2a-Arf6 pathway downstream of the DGC.
BRAG2 localized to postsynaptic processes at bipolar dyads, while BRAG3 localized to postsynaptic components at conventional synapses in mouse retina
In addition to accelerate GTP gamma S binding by ARFs of all three classes, it appears to function preferentially as a guanine nucleotide exchange protein for ARF6, mediating internalisation of beta-1 integrin.
ADP-ribosylation factors guanine nucleotide-exchange protein 100
, ADP-ribosylation factors guanine nucleotide-exchange protein 2
, IQ motif and SEC7 domain-containing protein 1
, brefeldin A-resistant ARF-GEF2
, brefeldin-resistant Arf-GEF 2 protein