biological source
rabbit
conjugate
unconjugated
antibody form
serum
antibody product type
primary antibodies
clone
polyclonal
species reactivity
mouse, human
species reactivity (predicted by homology)
rat (100% immunogen homology)
technique(s)
immunoprecipitation (IP): suitable, western blot: suitable
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Gene Information
human ... G3BP1(10146)
mouse ... G3Bp1(27041)
General description
68 kDa
G3BP1 (Ras-GTPase activating protein SH3-domain binding protein 1) directly associates with SH3 domains of GTPase activating proteins (GAPs). It was first discovered by its binding to RasGAP. G3BPs have been shown to be involved in a number of mitogenic signaling pathways. G3BP1 is also known to be over expressed in many human cancers (Kim, 2007) and its expression appears to be inversely correlated with PTEN expression (Kim, 2007). Interestingly, G3BP1, along with G3BP2, has been shown to bind to the C-terminus of p53, playing a crucial role in its activity (Kim, 2007). Furthermore, the G3BPs have two traditional RNA binding motifs.
Immunogen
Epitope: C-terminus
Synthetic peptide corresponding to C-terminal region of human G3BP1.
Application
Anti-G3BP1 Antibody detects level of G3BP1 & has been published & validated for use in WB & IP.
Research Category
Signaling
Signaling
Research Sub Category
RNA Binding Protein (RBP)
RNA Binding Protein (RBP)
Biochem/physiol Actions
Not tested on other species.
This antibody detects G3BP1 at its C-terminal region.
Physical form
Rabbit polyclonal serum with 0.05% NaN3.
Preparation Note
Stable for 1 year at -20ºC from date of receipt.
Analysis Note
Evaluated by western blot on HeLa cell lysates.
Western Blot Analysis:
1:1,000 dilution of this antibody was used to detect G3BP1 in HeLa, 293T and S10 cell lysates.
Western Blot Analysis:
1:1,000 dilution of this antibody was used to detect G3BP1 in HeLa, 293T and S10 cell lysates.
Control
HeLa cell lysates.
HeLa cell lysates.
Disclaimer
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.
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存储类别
10 - Combustible liquids
wgk
WGK 1
N Oi et al.
Oncogene, 34(20), 2660-2671 (2014-07-08)
Resveratrol (trans-3,5,4'-truhydroxystilbene) possesses a strong anticancer activity exhibited as the induction of apoptosis through p53 activation. However, the molecular mechanism and direct target(s) of resveratrol-induced p53 activation remain elusive. Here, the Ras-GTPase-activating protein SH3 domain-binding protein 1 (G3BP1) was identified
Soumitra Ghosh et al.
EBioMedicine, 2(11), 1785-1798 (2016-02-13)
Microglial cells in the brains of Alzheimer's patients are known to be recruited to amyloid-beta (Aβ) plaques where they exhibit an activated phenotype, but are defective for plaque removal by phagocytosis. In this study, we show that microglia stressed by
Kalle Kipper et al.
Journal of molecular biology, 434(20), 167801-167801 (2022-08-30)
The polarized cell morphology of neurons dictates many neuronal processes, including the axodendridic transport of specific mRNAs and subsequent translation. mRNAs together with ribosomes and RNA-binding proteins form RNA granules that are targeted to axodendrites for localized translation in neurons.
Jozsef Gal et al.
Acta neuropathologica, 132(4), 563-576 (2016-08-03)
Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disease. Mutations in Cu/Zn superoxide dismutase (SOD1) are responsible for approximately 20 % of the familial ALS cases. ALS-causing SOD1 mutants display a gain-of-toxicity phenotype, but the nature of this toxicity is still
Chelsea J Webber et al.
Human molecular genetics, 32(20), 2966-2980 (2023-07-31)
Aggregation of TAR DNA-binding protein 43 kDa (TDP-43) is thought to drive the pathophysiology of amyotrophic lateral sclerosis and some frontotemporal dementias. TDP-43 is normally a nuclear protein that in neurons translocates to the cytoplasm and can form insoluble aggregates upon
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