The human recombinant ELAC1 is produced in Escherichia coli as a single, non-glycosylated polypeptide chain. It contains 386 amino acids and has a molecular mass of approximately 42.4 kDa. The recombinant protein is fused to a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques .
ELAC1 is involved in the maturation of tRNA molecules, which are essential for protein synthesis. By removing the 3’-trailer from precursor tRNA, ELAC1 ensures that tRNA molecules are properly processed and functional. This activity is vital for the accurate translation of genetic information from mRNA to proteins .
ELAC1 is expressed in various tissues, including lymphoid tissue, bone marrow, testis, and skeletal muscle. It is involved in several biological processes such as cell proliferation, innate immune response, protein ubiquitination, and spermatid development . The enzyme’s activity is crucial for maintaining cellular functions and ensuring the proper development and differentiation of cells.
Mutations or dysregulation of ELAC1 can lead to various diseases and conditions. For example, ELAC1 has been associated with femoral vein thrombophlebitis, a condition characterized by inflammation and clot formation in the femoral vein . Understanding the function and regulation of ELAC1 can provide insights into the molecular mechanisms underlying these conditions and potentially lead to the development of targeted therapies.
The recombinant ELAC1 protein is typically stored at 4°C if it will be used within 2-4 weeks. For longer storage periods, it is recommended to store the protein frozen at -20°C with the addition of a carrier protein such as human serum albumin (HSA) or bovine serum albumin (BSA) to prevent degradation. It is important to avoid multiple freeze-thaw cycles to maintain the protein’s stability and activity .