G8046
Anti-phospho-G3BP (pSer149) antibody produced in rabbit
~1.0 mg/mL, affinity isolated antibody, buffered aqueous solution
Synonym(s):
Anti-G3BP1, Anti-GAP SH3 domain-binding protein, Anti-HDH-VIII, Anti-RAS-GTPase-activating protein SH3-domain binding protein 1, Anti-human DNA helicase VIII
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About This Item
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biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen ~68 kDa
species reactivity
human, rat (predicted), mouse (predicted)
concentration
~1.0 mg/mL
technique(s)
western blot: 5-10 μg/mL using whole extract of human K562 and HeLa cells
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
phosphorylation (pSer149)
Gene Information
human ... G3BP1(10146)
mouse ... G3bp1(27041)
rat ... G3bp1(171092)
General description
G3BP (Ras-GTPase-activating protein SH3 domain binding protein 1) is a 68kDa, single-strand-specific endoribonuclease that is phosphorylation-dependent.
Application
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.
Biochem/physiol Actions
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.
Target description
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.
Physical form
Solution 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
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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Product No.
Description
Pricing
Storage Class Code
10 - Combustible liquids
WGK
nwg
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Marc D Panas et al.
The Journal of cell biology, 218(7), 2425-2432 (2019-06-07)
Tourrière et al. (2013. J. Cell Biol. https://doi.org/10.1083/jcb.200212128) reported that G3BP1-S149 dephosphorylation promotes stress granule formation. We show that constructs used to establish this conclusion contain additional mutations causing these phenotypes, and that S149 phosphorylation status does not change upon
Helene Tourrière et al.
The Journal of cell biology, 160(6), 823-831 (2003-03-19)
Stress granules (SGs) are formed in the cytoplasm in response to various toxic agents, and are believed to play a critical role in the regulation of mRNA metabolism during stress. In SGs, mRNAs are stored in an abortive translation initiation
Paul Anderson et al.
The Journal of cell biology, 172(6), 803-808 (2006-03-08)
Cytoplasmic RNA granules in germ cells (polar and germinal granules), somatic cells (stress granules and processing bodies), and neurons (neuronal granules) have emerged as important players in the posttranscriptional regulation of gene expression. RNA granules contain various ribosomal subunits, translation
I E Gallouzi et al.
Molecular and cellular biology, 18(7), 3956-3965 (1998-06-25)
A potential p120 GTPase-activating protein (RasGAP) effector, G3BP (RasGAP Src homology 3 [SH3] binding protein), was previously identified based on its ability to bind the SH3 domain of RasGAP. Here we show that G3BP colocalizes and physically interacts with RasGAP
Monika Jedrusik-Bode et al.
Journal of cell science, 126(Pt 22), 5166-5177 (2013-09-10)
SIRT6 is a NAD(+)-dependent deacetylase that modulates chromatin structure and safeguards genomic stability. Until now, SIRT6 has been assigned to the nucleus and only nuclear targets of SIRT6 are known. Here, we demonstrate that in response to stress, C. elegans
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