Anti-phospho-G3BP (pSer149) antibody produced in rabbit is suitable for western blotting at a working concentration of 5-10μg/mL using whole extract of human K562 and HeLa cells.
Anti-G3BP antibody produced in rabbit has been used in co-immunoprecipitation assay.
G3BP is a RNA-binding protein that contains a RNA binding domain, the RRM-type domain, at the carboxyl-terminal. The N-terminal domain is homologous to nuclear transporter factor 2 (NTF2) and the central domain is rich in acidic residues. The RRM domain is involved in the binding of G3BP to specific RNA sequences. This helps G3BP to function as a CA dinucleotide-specific endoribonuclease. G3BP′s subcellular localization and protein-protein interactions are mediated by the phosphorylation of G3BP at Ser149, near NTF2-like domain. G3BP is found in abundance in many kinds of malignant tumors such as lung, colon, gastric, and breast cancer.
G3BP (Ras-GTPase-activating protein SH3 domain binding protein 1) is a endoribonuclease that is phosphorylation-dependent and specific to single strand. It cleaves between cytosine and adenine (CA). It binds to the SH3 domain of RasGAP. It forms a link between RasGAP-mediated signaling pathway and RNA turnover. G3BP is required for the assembly of stress granules (SGs), which are involved in the regulation of mRNA metabolism during stress. It may be used as a cytoplasmic SG marker.