Eukaryotic translation elongation factor 1 epsilon-1, Aminoacyl tRNA synthetase complex-interacting multifunctional protein 3, Elongation factor p18, Multisynthase complex auxiliary component p18, EEF1E1, AIMP3, P18.
EEF1E1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 194 amino acids (1-174 a.a.) and having a molecular mass of 21.9kDa.
EEF1E1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Eukaryotic translation elongation factor 1 epsilon-1 (EEF1E1) is similar in sequence to the amino-terminal ends of the Beta and Gamma subunits of EF-1. EEF1E1 specifically interacts with MetRS and binds to a large tRNA synthtase complex. This complex catalyzes the ligation of specific amino acids to their corresponding tRNAs. When DNA damage occurs, EEF1E1 moves to the nucleus and interacts with ATM and ATR, leading to p53 activation.
EEF1E1, as produced in E. coli, is a single polypeptide chain that is not glycosylated. It contains 194 amino acids (specifically, amino acids 1 through 174) and has a molecular weight of 21.9 kDa.
A 20 amino acid His-tag is fused to the N-terminus of EEF1E1. Purification is achieved using proprietary chromatographic techniques.
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, freeze the product at -20°C.
Adding a carrier protein (either HSA or BSA) to a final concentration of 0.1% is recommended for long-term storage.
Multiple freeze-thaw cycles should be avoided.
Eukaryotic translation elongation factor 1 epsilon-1, Aminoacyl tRNA synthetase complex-interacting multifunctional protein 3, Elongation factor p18, Multisynthase complex auxiliary component p18, EEF1E1, AIMP3, P18.
MGSSHHHHHH SSGLVPRGSH MAAAAELSLL EKSLGLSKGN KYSAQGERQI PVLQTNNGPS LTGLTTIAAH LVKQANKEYL LGSTAEEKAI VQQWLEYRVT QVDGHSSKND IHTLLKDLNS YLEDKVYLTG YNFTLADILL YYGLHRFIVD LTVQEKEKYL NVSRWFCHIQ HYPGIRQHLS SVVFIKNRLY TNSH.
Eukaryotic Translation Elongation Factor 1 Epsilon 1 (EEF1E1) is a protein-coding gene that plays a crucial role in the process of translation elongation during protein synthesis. This protein is part of the elongation factor-1 (EF-1) complex, which is responsible for the enzymatic delivery of aminoacyl-tRNAs to the ribosome during the elongation phase of translation. The human recombinant form of EEF1E1 is produced using recombinant DNA technology, allowing for its use in various research and therapeutic applications.
The EEF1E1 gene is located on chromosome 6 in humans and encodes a multifunctional protein that localizes to both the cytoplasm and nucleus . The protein is an auxiliary component of the macromolecular aminoacyl-tRNA synthase complex in the cytoplasm. It has been shown to translocate to the nucleus in response to DNA damage, where it plays a positive role in ATM/ATR-mediated p53 activation .
EEF1E1 is involved in the elongation phase of protein synthesis, where it facilitates the GTP-dependent binding of aminoacyl-tRNA to the A-site of the ribosome . This process is essential for the accurate and efficient synthesis of proteins. The protein exists in two isoforms, eEF1A1 and eEF1A2, which share almost identical amino acid sequences but differ in their expression patterns. eEF1A1 is ubiquitously present except in skeletal and cardiac muscle, while eEF1A2 is restricted to the brain, skeletal muscle, heart, and other specific cell types .
EEF1E1 plays a critical role in various cellular processes beyond translation elongation. It is involved in the regulation of transcription, DNA-templated processes, cellular response to epidermal growth factor stimulus, and regulation of chaperone-mediated autophagy . Additionally, EEF1E1 has been implicated in the modulation of the cytoskeleton, exhibiting chaperone-like activity, and controlling cell proliferation and cell death .
Mutations or dysregulation of EEF1E1 have been associated with several diseases, including Retinoschisis 1, X-Linked, Juvenile, and Chromosome 5Q12 Deletion Syndrome . The protein’s role in DNA damage response and its involvement in various signaling pathways make it a potential target for therapeutic interventions in cancer and other diseases.