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p-G3BP1 (Ser 232) Antibody: sc-101684 |
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- rabbit polyclonal IgG, 100 µg/ml
- epitope corresponding to phosphorylated Ser 232 of G3BP1 of human origin
- recommended for detection of Ser 232 phosphorylated G3BP1 of h origin by WB, IP, IF and IHC(P)
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p-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. Human G3BP1 can be phosphorylated on specific serine residues, producing a phosphoprotein (p-G3BP1) that may have a different conformation and/or localization than endogenous G3BP1. 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.
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p-G3BP1 (Ser 232)
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p-G3BP1 (Ser 232): sc-101684. Immunoperoxidase staining of formalin-fixed, paraffin-embedded human breast carcinoma tissue showing cytoplasmic staining.
Western blot analysis of phosphorylated G3BP1 expression in 293 whole cell lysate (A,B). Blots were probed with p-G3BP1 (Ser 232): sc-101684 preincubated with cognate phosphorylated peptide (A) and p-G3BP1 (Ser 232): sc-101684 (B).
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