epitope mapping at the C-terminus of G3BP1 of human origin
recommended for detection of G3BP1 of mouse, rat and human origin by WB, IF and ELISA; also reactive with additional species, including canine, bovine and porcine
G3BP1 Background Information G3BP1 (GTPase activating protein (SH3 domain) binding protein 1), also known as G3BP or HDH-VIII, is a ubiquitously expressed protein that localizes to the cytoplasm in proliferating cells and to the nucleus in non-proliferating cells. One of several DNA-unwinding enzymes, G3BP1 functions as a sequence-specific, phosphorylation-dependent helicase that unwinds partial RNA and DNA duplexes containing hanging 3’- or 5’- ends. G3BP1 uses magnesium as a cofactor and, in addition to its helicase activity, acts as an endoribonuclease that cleaves mRNA between adenine and cytosine residues at the 3’-UTR. An element of the Ras signaling pathway, G3BP1 binds to the SH3 domain of Ras GTPase-activating protein (Ras GAP) in proliferating cells, thereby regulating Ras signaling events in developing tissues. Due to its involvement in both DNA replication and signaling pathways within the cell, G3BP1 expression is implicated in the pathogenesis of several cancers, including esophageal squamous carcinoma.
