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Merck

G6046

Sigma-Aldrich

Anti-G3BP antibody produced in rabbit

~1.0 mg/mL, affinity isolated antibody, buffered aqueous solution

Sinónimos:

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

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

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, mouse (predicted), rat (predicted)

concentration

~1.0 mg/mL

technique(s)

indirect immunofluorescence: 2-5 μg/mL using human HeLa cells
western blot: 0.1-0.2 μg/mL using whole extract of human U-2-OS cells

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... G3BP1(10146)
mouse ... G3bp1(27041)
rat ... G3bp1(171092)

General description

G3BP is a RNA-binding protein that contains a RNA binding domain, the RRM-type domain, at the carboxyl-terminal. The N-terminal domain is homologous to nuclear transporter factor 2 (NTF2) and the central domain is rich in acidic residues. The RRM domain is involved in the binding of G3BP to specific RNA sequences. This helps G3BP to function as a CA dinucleotide-specific endoribonuclease. G3BP′s subcellular localization and protein-protein interactions are mediated by the phosphorylation of G3BP at Ser149, near NTF2-like domain. G3BP is found in abundance in many kinds of malignant tumors such as lung, colon, gastric, and breast cancer.

Application

Anti-G3BP antibody produced in rabbit has been used in co-immunoprecipitation assay.
Anti-G3BP antibody produced in rabbit has been used in
  • immunofluorescence analysis
  • immunostaining
  • immunoblotting
  • immunoprecipitation

Biochem/physiol Actions

G3BP (Ras-GTPase-activating protein SH3 domain binding protein 1) is a endoribonuclease that is phosphorylation-dependent and specific to single strand. It cleaves between cytosine and adenine (CA). It binds to the SH3 domain of RasGAP. It forms a link between RasGAP-mediated signaling pathway and RNA turnover. G3BP is required for the assembly of stress granules (SGs), which are involved in the regulation of mRNA metabolism during stress. It may be used as a cytoplasmic SG marker.
Ras-GAP SH3 domain binding protein (G3BP) is overexpressed in many kinds of malignant tumors such as breast, colon, lung and gastric breast cancer. G3BP expression is correlated with lymph node metastasis in breast cancer.

Target description

G3BP 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 in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Preparation Note

In immunoblotting assays, it is highly recommended to dilute the antibody in 5% NFDM (w/v).

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

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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


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Jelke Jan Fros et al.
eLife, 6 (2017-09-30)
Most vertebrate and plant RNA and small DNA viruses suppress genomic CpG and UpA dinucleotide frequencies, apparently mimicking host mRNA composition. Artificially increasing CpG/UpA dinucleotides attenuates viruses through an entirely unknown mechanism. Using the echovirus 7 (E7) model in several
Jelke J Fros et al.
Journal of virology, 86(19), 10873-10879 (2012-07-28)
Chikungunya virus nonstructural protein nsP3 has an essential but unknown role in alphavirus replication and interacts with Ras-GAP SH3 domain-binding protein (G3BP). Here we describe the first known function of nsP3, to inhibit stress granule assembly by recruiting G3BP into
Yan Zheng et al.
Journal of virology, 87(17), 9579-9589 (2013-06-21)
Alphaviruses are enveloped viruses with highly organized structures. The nucleocapsid (NC) core contains a capsid protein lattice enclosing the plus-sense RNA genome, and it is surrounded by a lipid bilayer containing a lattice of the E1 and E2 envelope glycoproteins.
Samuel Solomon et al.
Molecular and cellular biology, 27(6), 2324-2342 (2007-01-11)
Caprin-1 is a ubiquitously expressed, well-conserved cytoplasmic phosphoprotein that is needed for normal progression through the G(1)-S phase of the cell cycle and occurs in postsynaptic granules in dendrites of neurons. We demonstrate that Caprin-1 colocalizes with RasGAP SH3 domain
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

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