GARS Human
Description
GARS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
Glycyl-tRNA synthetase (GARS) is an essential enzyme involved in protein synthesis. It catalyzes the attachment of glycine to its corresponding tRNA molecule, a crucial step in the translation of genetic information into proteins. The human recombinant form of this enzyme is produced through recombinant DNA technology, allowing for its use in various research and therapeutic applications.
GARS belongs to the class II aminoacyl-tRNA synthetases, characterized by their unique structural motifs and mechanisms of action. The enzyme is composed of 685 amino acids and has a molecular weight of approximately 77.5 kDa . It features several highly conserved regions, including the class II synthetase motif and an N-terminal region similar to those found in other synthetases .
The primary function of GARS is to ensure the accurate translation of genetic information by catalyzing the esterification of glycine to its cognate tRNA. This process is vital for maintaining the fidelity of protein synthesis, as it ensures that the correct amino acid is incorporated into the growing polypeptide chain .
GARS plays a critical role in cellular metabolism and protein synthesis. It is ubiquitously expressed in all cells, reflecting its essential function in maintaining cellular homeostasis. The enzyme’s activity is tightly regulated to ensure the proper balance of aminoacyl-tRNA molecules required for efficient protein synthesis .
In addition to its primary role in translation, GARS has been implicated in various cellular processes, including signal transduction and stress response. Recent studies have shown that GARS can bind to specific RNA structures, such as the Internal Ribosome Entry Site (IRES) elements of certain viruses, to facilitate cap-independent translation initiation . This moonlighting function highlights the enzyme’s versatility and importance in cellular physiology .
Mutations in the GARS gene have been associated with several neurological disorders, including Charcot-Marie-Tooth disease type 2D (CMT2D) and distal hereditary motor neuropathy type V (dHMN-V). These conditions are characterized by progressive muscle weakness and atrophy, reflecting the critical role of GARS in maintaining neuronal function .
The human recombinant form of GARS is used in various research applications to study its structure, function, and role in disease. It is also employed in the development of potential therapeutic strategies for treating GARS-related disorders.
