G3BP2 Human

GTPase Activating Protein (SH3 domain) Binding Protein 2 Human Recombinant
Cat. No.
BT24274
Source
Escherichia Coli.
Synonyms
Ras GTPase-activating protein-binding protein 2, G3BP-2, GAP SH3 domain-binding protein 2, G3BP2, KIAA0660.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 90% as determined by SDS-PAGE.
Usage
THE BioTeks products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

G3BP2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 473 amino acids (1-449) and having a molecular mass of 53.3kDa.
G3BP2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Ras GTPase-activating protein-binding protein 2 (G3BP2), primarily found at the plasma membrane and within endocytic compartments, regulates a rapid endocytic recycling pathway. G3BP2 is thought to function as a scaffold protein potentially involved in mRNA transport.
Description
Recombinant human G3BP2, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 473 amino acids (residues 1-449) with a molecular weight of 53.3 kDa. This protein includes a 24 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic techniques.
Physical Appearance
Clear, sterile, and filtered solution.
Formulation
The G3BP2 solution (1 mg/ml) is supplied in a buffer containing 20 mM Tris-HCl (pH 8.0), 30% glycerol, 0.2 M NaCl, 2 mM DTT, and 0.1 mM PMSF.
Stability
For short-term storage (up to 2-4 weeks), store the solution at 4°C. For extended periods, store frozen at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Repeated freezing and thawing should be avoided.
Purity
Purity exceeds 90% as assessed by SDS-PAGE.
Synonyms
Ras GTPase-activating protein-binding protein 2, G3BP-2, GAP SH3 domain-binding protein 2, G3BP2, KIAA0660.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMVMEKP SPLLVGREFV RQYYTLLNKA PEYLHRFYGR NSSYVHGGVD ASGKPQEAVY GQNDIHHKVL SLNFSECHTK IRHVDAHATL SDGVVVQVMG LLSNSGQPER KFMQTFVLAP EGSVPNKFYV HNDMFRYEDE VFGDSEPELD EESEDEVEEE QEERQPSPEP VQENANSGYY EAHPVTNGIE EPLEESSHEP EPEPESETKT EELKPQVEEK NLEELEEKST TPPPAEPVSL PQEPPKPRVE AKPEVQSQPP RVREQRPRER PGFPPRGPRP GRGDMEQNDS DNRRIIRYPD SHQLFVGNLP HDIDENELKE FFMSFGNVVE LRINTKGVGG KLPNFGFVVF DDSEPVQRIL IAKPIMFRGE VRLNVEEKKT RAARERETRG GGDDRRDIRR NDRGPGGPRG IVGGGMMRDR DGRGPPPRGG MAQKLGSGRG TGQMEGRFTG QRR.

Product Science Overview

Introduction

GTPase Activating Protein (SH3 domain) Binding Protein 2 (G3BP2) is a member of the G3BP family, which also includes G3BP1. These proteins are known for their role in various cellular processes, including stress granule formation, RNA metabolism, and signal transduction. G3BP2 is encoded by the G3BP2 gene located on human chromosome 4. The protein is highly expressed in the small intestine and brain .

Structure and Function

G3BP2 is an RNA-binding protein that interacts with the SH3 domain of Ras-GTPase activating protein (Ras-GAP) in serum-stimulated cells . The protein consists of several domains, including an NTF2-like domain, an RNA recognition motif (RRM), and an acidic C-terminal region. These domains facilitate its interactions with various cellular components and its involvement in multiple cellular pathways.

One of the key functions of G3BP2 is its role in the formation of stress granules (SGs). Stress granules are membraneless organelles that form in response to cellular stress and serve as storage sites for mRNAs and proteins . G3BP2 promotes the assembly of these granules through liquid-liquid phase separation (LLPS), a process driven by the interaction of its RNA-binding domains with unfolded RNA .

Biological Significance

G3BP2 plays a crucial role in the regulation of mRNA stability and translation. It acts as a molecular switch that triggers RNA-dependent LLPS in response to increased intracellular RNA concentrations . This function is essential for the formation of stress granules, which help cells survive under stress conditions by sequestering and protecting mRNAs.

In addition to its role in stress granule formation, G3BP2 is involved in various signaling pathways. It interacts with the Ras signaling pathway, although the exact nature of this interaction is still under investigation . G3BP2 also participates in the innate immune response by promoting the activity of cGAS and RIG-I, two key components of the antiviral defense mechanism .

Clinical Relevance

G3BP2 has been implicated in several diseases, including cancer, neurodevelopmental disorders, and viral infections. Its role in stress granule formation and RNA metabolism makes it a potential target for therapeutic interventions. For example, modulating G3BP2 activity could help enhance the antiviral response or mitigate the effects of cellular stress in diseases such as cancer .

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