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Key Documents

G8046

Sigma-Aldrich

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

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

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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Storage Class

10 - Combustible liquids

wgk_germany

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


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
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
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
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
Hui-Zhong Zhang et al.
World journal of gastroenterology, 13(30), 4126-4130 (2007-08-19)
To investigate the expression and significance of G3BP and RhoC proteins in esophageal squamous carcinoma (ESC). The expression of G3BP and Rhoc proteins in 80 cases of ESC was detected by immunohistochemistry. The relationship was studied between the expression of

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