Anti-G3BP antibody produced in rabbit

G3BP 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.

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.

Anti-G3BP antibody produced in rabbit has been used in co-immunoprecipitation assay.

Anti-G3BP antibody produced in rabbit has been used in

• immunofluorescence analysis
• immunostaining
• immunoblotting
• immunoprecipitation

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.

Ras-GAP SH3 domain binding protein (G3BP) is overexpressed in many kinds of malignant tumors such as breast, colon, lung and gastric breast cancer. G3BP expression is correlated with lymph node metastasis in breast cancer.

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

In immunoblotting assays, it is highly recommended to dilute the antibody in 5% NFDM (w/v).

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