Immunogen Sequence: GI # 5031703, sequence 132-350
Recombinant ras-GTPase-activating protein SH3-domain-binding protein
Application
Anti-G3BP antibody produced in chicken is suitbale for western blotting analysis at a dilution of 1:500, for tissue or cell staining at a dilution of 1:200.
Biochem/physiol Actions
Ras GTPase-activating protein-binding protein 1 is an enzyme encoded by the G3BP1 gene in humans. It is a ubiquitously expressed cytosolic 68kDa protein that physically associates with the SH3 domain of GAP and is essential for Ras signaling. The protein binds to RasGAP and is overexpressed in many human cancers. Down regulation of G3BP1 suppresses cell growth and induces apoptosis in HCT116 cells. It acts as a potential anti-cancer drug target implicated in several cellular functions.
Physical form
Solution in phosphate buffered saline containing 0.02% sodium azide.
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Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
G3BP is a RasGAP binding protein that is overexpressed in many human cancers. We previously reported that downregulation of G3BP suppressed cell growth and induced apoptosis in HCT116 cells. Here we report that both transient and stable knockdown of G3BP
Ras GTPase Activating Protein SH3 Domain Binding Protein (G3BP) is a potential anti-cancer drug target implicated in several cellular functions. We have used protein crystallography to solve crystal structures of the human G3BP1 NTF2-like domain both alone and in complex
Molecular and cellular biology, 16(6), 2561-2569 (1996-06-01)
We report the purification of a Ras-GTPase-activating protein (GAP)-binding protein, G3BP, a ubiquitously expressed cytosolic 68-kDa protein that coimmunoprecipitates with GAP. G3BP physically associates with the SH3 domain of GAP, which previously had been shown to be essential for Ras
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