EEF1B2 Human
Description
EEF1B2 Human Recombinant fused with an 8 amino acid His tag at C-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 233 amino acids (1-225 a.a.) and having a molecular mass of 25.8kDa. The EEF1B2 is purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
Eukaryotic Translation Elongation Factor 1 Beta 2 (EEF1B2) is a protein-coding gene that plays a crucial role in the elongation step of translation. This protein is involved in the transfer of aminoacylated tRNAs to the ribosome, facilitating the synthesis of proteins. The human recombinant form of EEF1B2 is produced using recombinant DNA technology, which allows for the expression of the protein in a host organism, such as E. coli.
The EEF1B2 gene is located on chromosome 2 and encodes a protein that is approximately 25.8 kDa in size . The protein consists of 233 amino acids and includes a guanine nucleotide exchange factor domain, which is essential for its function in translation elongation . The human recombinant form of EEF1B2 is often fused with an 8 amino acid His tag at the C-terminus to facilitate purification .
EEF1B2 functions as a guanine nucleotide exchange factor (GEF) for Eukaryotic Translation Elongation Factor 1 Alpha (EEF1A). It mediates the exchange of GDP for GTP on EEF1A, which is necessary for the proper functioning of the elongation cycle during protein synthesis . This process ensures the accurate and efficient addition of amino acids to the growing polypeptide chain.
The activity of EEF1B2 is critical for maintaining the fidelity and efficiency of protein synthesis. Dysregulation of EEF1B2 has been associated with various diseases, including autosomal recessive non-syndromic intellectual disability and Alacrima, Achalasia, and Impaired Intellectual Development Syndrome . Additionally, EEF1B2 is frequently overexpressed in human cancer cells, highlighting its potential role in tumorigenesis .
The human recombinant form of EEF1B2 is used in various research applications, including studies on protein synthesis, translation regulation, and cancer biology. The recombinant protein is typically expressed in E. coli and purified using chromatographic techniques to ensure high purity and activity . It is available in different sizes and formulations, making it suitable for a wide range of experimental setups.
