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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.. Additionally we are shipping IQSEC1 Antibodies (10) and many more products for this protein.
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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 (show EGFR Proteins)-GEP100-Arf6 (show ARF6 Proteins) axis affected the prognosis of patients with primary lung adenocarcinoma.
Data show that co-overexpression of GEP100 and AMAP1 (ASAP1 (show ASAP1 Proteins)) correlates with rapidity of the local recurrence.
GEP100 regulates an Arf6 (show ARF6 Proteins)/ERK (show EPHB2 Proteins)/uPAR (show PLAUR Proteins) signaling cascade in EGF (show EGF Proteins)-induced breast cancer cell invasion.
GEP100 plays a significant role in pancreatic cancer invasion through regulating the expression of E-cadherin (show CDH1 Proteins) 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 (show ARF6 Proteins)-AMAP1 (show ASAP1 Proteins)-cortactin (show CTTN Proteins) pathway, activated by VEGFR2 (show KDR Proteins), 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 (show ERBB2 Proteins) with GEP100 in primary lung adenocarcinomas of patients is correlated with the presence of their node-metastasis with a statistical significance.
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