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Merck
CN

HPA018425

Anti-G3BP2 antibody produced in rabbit

Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution

别名:

Anti-G3BP-2, Anti-GAP SH3 domain-binding protein 2, Anti-Ras GTPase-activating protein-binding protein 2

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关于此项目

UNSPSC Code:
12352203
NACRES:
NA.41
Human Protein Atlas Number:
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产品名称

Anti-G3BP2 antibody produced in rabbit, Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

product line

Prestige Antibodies® Powered by Atlas Antibodies

form

buffered aqueous glycerol solution

species reactivity

human

enhanced validation

orthogonal RNAseq
independent
Learn more about Antibody Enhanced Validation

technique(s)

immunohistochemistry: 1:50-1:200

immunogen sequence

KNLEELEEKSTTPPPAEPVSLPQEPPKPRVEAKPEVQSQPPRVREQRPRERPGFPPRGPRPGRGDMEQNDS

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Quality Level

Gene Information

human ... G3BP2(9908)

Immunogen

Ras GTPase-activating protein-binding protein 2 recombinant protein epitope signature tag (PrEST)

Other Notes

Corresponding Antigen APREST73970

Physical form

Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide

Legal Information

Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany

Application

Anti-G3BP2 antibody produced in rabbit, a Prestige Antibody, is developed and validated by the Human Protein Atlas (HPA) project . Each antibody is tested by immunohistochemistry against hundreds of normal and disease tissues. These images can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. The antibodies are also tested using immunofluorescence and western blotting. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit sigma.com/prestige.

Biochem/physiol Actions

GAP SH3 domain-binding protein-2 (G3BP2) is identified as a gene for predicting the presence of lymph node metastasis in primary oral squamous cell carcinoma. G3BP2 is a negative modulator of p53 function. Depletion of G3BP2 leads to up-regulation of p53 and its overexpression leads to the cytoplasmic redistribution of p53. G3BP2 binds mechanomediator TWIST1 in the cytoplasm. Loss of G3BP2 leads to nuclear localization of TWIST1 which in response to biomechanical signals induce epithelial-mesenchymal transition, promoting tumor invasion and metastasis. Overexpression of G3BP2 induces formation of cytoplasmic RNA granules called stress granules (SGs). Knockdown of G3BP2 reduces the number of SG-positive cells. During Semliki Forest virus infection, the C-terminal domain of the viral nonstructural protein-3 forms a complex with G3BP2 and inhibits the formation of SGs on viral mRNAs, thus impairing antiviral defense.

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.

Features and Benefits

Prestige Antibodies® are highly characterized and extensively validated antibodies with the added benefit of all available characterization data for each target being accessible via the Human Protein Atlas portal linked just below the product name at the top of this page. The uniqueness and low cross-reactivity of the Prestige Antibodies® to other proteins are due to a thorough selection of antigen regions, affinity purification, and stringent selection. Prestige antigen controls are available for every corresponding Prestige Antibody and can be found in the linkage section.

Every Prestige Antibody is tested in the following ways:
  • IHC tissue array of 44 normal human tissues and 20 of the most common cancer type tissues.
  • Protein array of 364 human recombinant protein fragments.

General description

The gene G3BP2 (GAP SH3 domain-binding protein-2) has been mapped to human chromosome 4q21.1. G3BP2 is ubiquitously expressed and is mainly present in the cytoplasm. However, it is capable of shuttling into the nucleus in cell-cycle dependent manner. G3BP2 include an NTF2 (nuclear transport factor)-like domain and two RNA-binding motifs.

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存储类别

10 - Combustible liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

法规信息

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Weina Wang et al.
Advanced science (Weinheim, Baden-Wurttemberg, Germany), 11(6), e2305068-e2305068 (2023-12-13)
Primary cilia are conserved organelles in most mammalian cells, acting as "antennae" to sense external signals. Maintaining a physiological cilium length is required for cilium function. MicroRNAs (miRNAs) are potent gene expression regulators, and aberrant miRNA expression is closely associated
Fátima Solange Pasini et al.
Acta oncologica (Stockholm, Sweden), 51(1), 77-85 (2011-10-12)
Previous knowledge of cervical lymph node compromise may be crucial to choose the best treatment strategy in oral squamous cell carcinoma (OSCC). Here we propose a set four genes, whose mRNA expression in the primary tumor predicts nodal status in
Amy E Rose et al.
Cancer research, 71(7), 2561-2571 (2011-02-24)
Superficial spreading melanoma (SSM) and nodular melanoma (NM) are believed to represent sequential phases of linear progression from radial to vertical growth. Several lines of clinical, pathologic, and epidemiologic evidence suggest, however, that SSM and NM might be the result
Marc D Panas et al.
Molecular biology of the cell, 23(24), 4701-4712 (2012-10-23)
Dynamic, mRNA-containing stress granules (SGs) form in the cytoplasm of cells under environmental stresses, including viral infection. Many viruses appear to employ mechanisms to disrupt the formation of SGs on their mRNAs, suggesting that they represent a cellular defense against
Ying Sun et al.
Oncogene, 38(24), 4856-4874 (2019-02-26)
Identification of molecular alterations driving breast cancer progression is critical for the development of effective therapy. In this study, we show that the level of α-parvin is elevated in triple-negative breast cancer cells. The depletion of α-parvin from triple-negative breast

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