Anti-phospho-G3BP (pSer¹⁴⁹) antibody produced in rabbit

G3BP (Ras-GTPase-activating protein SH3 domain binding protein 1) is a 68kDa, single-strand-specific endoribonuclease that is phosphorylation-dependent.

G3BP (pSer¹⁴⁹) encodes one of the DNA-unwinding enzymes which prefers partially unwound 3′-tailed substrates and can also unwind partial RNA/DNA and RNA/RNA duplexes in an ATP-dependent fashion.

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.

G3BP (Ras-GTPase-activating protein SH3 domain binding protein 1) exclusively cleaves between cytosine and adenine (CA). In dividing cells, G3BP interacts with RasGAP, linking between a RasGAP-mediated signaling pathway and RNA turnover. It is a RNA-binding protein that contains a carboxyl-terminal RNA binding domain, the RRM-type domain. It also has an amino-terminal domain homologous to nuclear transporter factor 2 (NTF2), and a central domain rich in acidic residues. The RRM domain is involved in the binding of G3BP to specific RNA sequences. A Ser149 residue is present 20 amino acids C terminal to the NTF2-like domain. Phosphorylation of this residue is crucial in mediating protein-protein interactions and in controlling the subcellular localization of G3BP. G3BP facilitates the assembly of stress granules that are invoved in the regulation of mRNA metabolism during stress. Dephosphorylation of Ser149 results in oligomerization and SG assembly. Overexpression of G3BP is observed in malignant tumors such as lung cancer, colon cancer, gastric cancer, and breast cancer. The level of G3BP expression in breast cancer specimens is positively correlated to the presence of lymph node metastasis.

Solution 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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