TARS Human
Description
TARS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
GSCFFLPKGA YIYNALIEFI RSEYRKRGFQ EVVTPNIFNS RLWMTSGHWQ HYSENMFSFE VEKELFALKP MNCPGHCLMF DHRPRSWREL PLRLADFGVL HRNELSGALT GLTRVRRFQQ DDAHIFCAME QIEDEIKGCL DFLRTVYSVF GFSFKLNLST RPEKFLGDIE VWDQAEKQLE NSLNEFGEKW ELNSGDGAFY GPKIDIQIKD AIGRYHQCAT IQLDFQLPIR FNLTYVSHDG DDKKRPVIVH RAILGSVERM IAILTENYGG KWPFWLSPRQ VMVVPVGPTC DEYAQKVRQQ FHDAKFMADI DLDPGCTLNK KIRNAQLAQY NFILVVGEKE KISGTVNIRT RDNKVHGERT ISETIERLQQ LKEFRSKQAE EEF.
Product Science Overview
Threonyl-tRNA synthetase (ThrRS) is an essential enzyme in the process of protein synthesis. It belongs to the family of aminoacyl-tRNA synthetases (aaRSs), which are responsible for the aminoacylation of transfer RNA (tRNA) molecules with their corresponding amino acids. This process is crucial for the accurate translation of genetic information from mRNA into proteins.
Threonyl-tRNA synthetase is a cytoplasmic enzyme encoded by the TARS gene in humans . The primary function of ThrRS is to catalyze the attachment of the amino acid threonine to its corresponding tRNA (tRNA^Thr). This reaction involves the formation of a threonyl-adenylate intermediate, followed by the transfer of threonine to the 3’ end of the tRNA molecule.
The enzyme’s structure is highly conserved across different species, reflecting its fundamental role in cellular biology. ThrRS typically consists of a catalytic domain responsible for the aminoacylation reaction and an anticodon-binding domain that ensures the correct tRNA is recognized and charged with threonine.
Threonyl-tRNA synthetase plays a critical role in maintaining the fidelity of protein synthesis. By ensuring that tRNA molecules are accurately charged with their corresponding amino acids, ThrRS helps prevent errors in the translation process that could lead to the production of dysfunctional proteins.
In addition to its canonical role in translation, ThrRS has been implicated in various cellular processes beyond protein synthesis. For instance, it has been detected extracellularly in autoimmune diseases and has exhibited pro-angiogenetic activity . This suggests that ThrRS may have additional functions in immune regulation and vascular biology.
Human recombinant Threonyl-tRNA synthetase is produced using recombinant DNA technology. This involves cloning the TARS gene into an expression vector, which is then introduced into a suitable host organism, such as Escherichia coli. The host cells are cultured under conditions that promote the expression of the recombinant protein, which is subsequently purified using chromatographic techniques.
Recombinant ThrRS is used in various research applications, including studies on protein synthesis, enzyme kinetics, and the development of therapeutic agents targeting aaRSs. Its availability as a recombinant protein allows for detailed biochemical and structural analyses, which are essential for understanding its function and potential roles in disease.
The study of Threonyl-tRNA synthetase has significant implications for both basic research and clinical applications. In the context of infectious diseases, for example, the enzyme has been explored as a potential therapeutic target for the treatment of parasitic infections such as visceral leishmaniasis . In this case, inhibitors of ThrRS could disrupt protein synthesis in the parasite, leading to its elimination.
Moreover, the involvement of ThrRS in immune responses and angiogenesis highlights its potential as a target for therapeutic intervention in autoimmune diseases and cancer. By modulating the activity of ThrRS, it may be possible to influence these pathological processes and develop novel treatments.
