Recombinant Human EEF1E1 protein(Met1-His174), His-tagged

• Cat.No.: EEF1E1-131H
• Product Overview: Recombinant Human EEF1E1 (NP_004271.1) (Met1-His174) was expressed in E. coli with a polyhistide tag at the N-terminus.

Specification

• Species: Human
• Source: E.coli
• Tag: His
• Protein Length: Met1-His174
• Form: Lyophilized from sterile PBS, 10% Glycerol, pH 7.4. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
• Molecular Mass: The recombinant human EEF1E1 consists of 189 amino acids and predicts a molecular mass of 21.6 KDa. It migrates as an approximately 19-24 KDa band in SDS-PAGE under reducing conditions.
• Purity: > 85 % as determined by SDS-PAGE
• Storage: Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: It is recommended that sterile water be added to the vial to prepare a stock solution of 0.2 ug/ul. Centrifuge the vial at 4°C before opening to recover the entire contents.

Gene Information

• Gene Name: EEF1E1 eukaryotic translation elongation factor 1 epsilon 1 [ Homo sapiens ]
• Official Symbol: EEF1E1
• Synonyms: EEF1E1; eukaryotic translation elongation factor 1 epsilon 1; P18; eukaryotic translation elongation factor 1 epsilon-1; AIMP3; aminoacyl tRNA synthetase complex interacting multifunctional protein 3; ARS-interacting multifunctional protein 3; multisynthase complex auxiliary component p18; p18 component of aminoacyl-tRNA synthetase complex; aminoacyl tRNA synthetase complex-interacting multifunctional protein 3
• Gene ID: 9521
• mRNA Refseq: NM_001135650
• Protein Refseq: NP_001129122
• MIM: 609206
• UniProt ID: O43324

Case Study

Case 1: Kang T, et al. J Mol Biol. 2012

AIMP3/p18 facilitates Met-tRNA transfer from methionyl-tRNA synthetase (MRS) to eIF2γ for translation initiation, enhancing protein synthesis via the multisynthetase complex (MSC). Its selective binding to Met-charged tRNA and recruitment of eIF2γ highlights AIMP3’s role in regulating mRNA translation, offering insights into MSC-driven translational control mechanisms and potential therapeutic targets for protein synthesis disorders.

Fig1. Interaction between AIMP3 and Met was determined by the filter-binding assay.

Fig2. HeLa cells were transfected with si-control and si-AIMP3.

Case 2: Kim C, et al. Aging Cell. 2019

Hypoxia suppresses AIMP3 expression to delay stem cell senescence by reducing p16INK4a and enhancing MSC proliferation. AIMP3 overexpression disrupts mitochondrial respiration, inhibits autophagy, and accelerates aging via HIF1α downregulation and Notch3 activation, revealing metabolic-autophagy crosstalk as a therapeutic target for aging-related tissue regeneration and stem cell-based therapies.

Fig1. The suppression of HIF1α induced AIMP3 under hypoxia at p5, whereas HIF1α overexpression under normoxia significantly repressed AIMP3.

Fig2. The suppression Notch3 expression downregulated AIMP3, FIH1, and p16INK4a in the hpMSCs under hypoxia.

Application

1. Therapeutic Potential of Recombinant EEF1E1 Protein in Aging and Regenerative Medicine Recombinant EEF1E1 (AIMP3) protein, a key regulator of stem cell senescence and protein synthesis, holds therapeutic promise for aging-related disorders and tissue regeneration. By modulating mitochondrial respiration and autophagy, recombinant EEF1E1 can counteract hypoxia-induced delays in stem cell aging, as demonstrated in human placenta-derived mesenchymal stem cells (hpMSCs). Its ability to suppress p16INK4a expression and enhance MSC proliferation positions it as a novel tool for rejuvenating aged stem cells and improving regenerative therapies. 2. Mechanistic Insights and Preclinical Applications Studies reveal that recombinant EEF1E1 disrupts senescence pathways by interacting with HIF1α and Notch3 signaling. In hypoxic conditions, EEF1E1 downregulation preserves MSC function, while its overexpression accelerates aging by impairing metabolic-autophagy balance. Preclinical models, including AIMP3-overexpressing mice, confirm its role in reducing stem cell viability and differentiation capacity, highlighting its potential as a biomarker or therapeutic target for age-related tissue degeneration and metabolic disorders. 3. Challenges and Future Directions Despite its promise, recombinant EEF1E1 faces challenges in delivery and stability. Innovations such as nanoparticle-based delivery systems or CRISPR-mediated gene editing could enhance its bioavailability and specificity. Combining EEF1E1-targeted therapies with autophagy modulators or metabolic enhancers may amplify anti-aging effects. Further research into its dual role in protein synthesis and senescence regulation could unlock precision interventions for aging and degenerative diseases.

Fig1. Schematic diagram describing the regulation of AIMP3/p18 and the mechanism by which AIMP3/p18 controls cellular senescence. (Seunghee Lee, 2014)