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AB123193

Recombinant Human G3BP2 protein (His tag N-Terminus)

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(1 Publication)

Recombinant Human G3BP2 protein (His tag N-Terminus) is a Human Full Length protein, in the 1 to 449 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.

View Alternative Names

KIAA0660, G3BP2, Ras GTPase-activating protein-binding protein 2, G3BP-2, GAP SH3 domain-binding protein 2

1 Images
SDS-PAGE - Recombinant Human G3BP2 protein (His tag N-Terminus) (AB123193)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human G3BP2 protein (His tag N-Terminus) (AB123193)

SDS-PAGE analysis of Recombinant Human G3BP2 protein (ab123193), under reducing conditions. Proteins visualized by coomassie blue stain.

Lane 1 : Molecular Weight Standards

Lane 2 : 3 μg Recombinant Human G3BP2 protein

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

Q9UN86

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 30% Glycerol (glycerin, glycerine), 1.17% Sodium chloride, 0.32% Tris HCl, 0.03% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.002% PMSF

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMGSHMVMEKPSPLLVGREFVRQYYTLLNKAPEYLHRFYGRNSSYVHGGVDASGKPQEAVYGQNDIHHKVLSLNFSECHTKIRHVDAHATLSDGVVVQVMGLLSNSGQPERKFMQTFVLAPEGSVPNKFYVHNDMFRYEDEVFGDSEPELDEESEDEVEEEQEERQPSPEPVQENANSGYYEAHPVTNGIEEPLEESSHEPEPEPESETKTEELKPQVEEKNLEELEEKSTTPPPAEPVSLPQEPPKPRVEAKPEVQSQPPRVREQRPRERPGFPPRGPRPGRGDMEQNDSDNRRIIRYPDSHQLFVGNLPHDIDENELKEFFMSFGNVVELRINTKGVGGKLPNFGFVVFDDSEPVQRILIAKPIMFRGEVRLNVEEKKTRAARERETRGGGDDRRDIRRNDRGPGGPRGIVGGGMMRDRDGRGPPPRGGMAQKLGSGRGTGQMEGRFTGQRR","proteinLength":"Full Length","predictedMolecularWeight":"53.3 kDa","actualMolecularWeight":null,"aminoAcidEnd":449,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q9UN86","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Specifications

Form

Liquid

Additional notes

ab123193 is purified using conventional chromatography techniques.

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General info

Function

Scaffold protein that plays an essential role in cytoplasmic stress granule formation which acts as a platform for antiviral signaling (PubMed : 23279204, PubMed : 32302570, PubMed : 32302571, PubMed : 32302572). Plays an essential role in stress granule formation (PubMed : 27022092, PubMed : 32302570, PubMed : 32302571, PubMed : 32302572, PubMed : 35977029). Stress granules are membraneless compartments that store mRNAs and proteins, such as stalled translation pre-initiation complexes, in response to stress (PubMed : 32302570, PubMed : 32302571, PubMed : 32302572). Promotes formation of stress granules phase-separated membraneless compartment by undergoing liquid-liquid phase separation (LLPS) upon unfolded RNA-binding : functions as a molecular switch that triggers RNA-dependent LLPS in response to a rise in intracellular free RNA concentrations (By similarity).

Post-translational modifications

(Microbial infection) Cleaved by foot-and-mouth disease virus leader protease; this cleavage suppresses the formation of cytoplasmic stress granules.

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Product protocols

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Target data

Scaffold protein that plays an essential role in cytoplasmic stress granule formation which acts as a platform for antiviral signaling (PubMed : 23279204, PubMed : 32302570, PubMed : 32302571, PubMed : 32302572). Plays an essential role in stress granule formation (PubMed : 27022092, PubMed : 32302570, PubMed : 32302571, PubMed : 32302572, PubMed : 35977029). Stress granules are membraneless compartments that store mRNAs and proteins, such as stalled translation pre-initiation complexes, in response to stress (PubMed : 32302570, PubMed : 32302571, PubMed : 32302572). Promotes formation of stress granules phase-separated membraneless compartment by undergoing liquid-liquid phase separation (LLPS) upon unfolded RNA-binding : functions as a molecular switch that triggers RNA-dependent LLPS in response to a rise in intracellular free RNA concentrations (By similarity).
See full target information G3BP2
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Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Nature communications 14:3016 PubMed37230995

2023

Decoding protein methylation function with thermal stability analysis.

Applications

Unspecified application

Species

Unspecified reactive species

Cristina Sayago,Jana Sánchez-Wandelmer,Fernando García,Begoña Hurtado,Vanesa Lafarga,Patricia Prieto,Eduardo Zarzuela,Pilar Ximénez-Embún,Sagrario Ortega,Diego Megías,Oscar Fernández-Capetillo,Marcos Malumbres,Javier Munoz
View all publications
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