Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in linking amino acids with nucleotide triplets contained in tRNAs, aminoacyl-tRNA synthetases are thought to be among the first proteins that appeared in evolution. Tyrosyl-tRNA synthetase (TYRRS, or YARS) belongs to the class I tRNA synthetase family. Cytokine activities have also been observed for the human tyrosyl-tRNA synthetase, after it is split into two parts, an N-terminal fragment that harbors the catalytic site and a C-terminal fragment found only in the mammalian enzyme. The N-terminal fragment (Mini-TyrRA) is an interleukin-8-like cytokine, whereas the released C-terminal fragment is an EMAP II-like cytokine.

Human YARS N-terminal fragment (Mini-TyrRA) cDNA (2 – 364 aa, derived from BC016689) was constructed with codon optimization and expressed with a small T7-His-TEV cleavage site Tag (29aa) fusion at its N-terminal. This protein is expressed in E.coli as inclusion bodies. The final product was refolded using our unique “temperature shift inclusion body refolding” technology and chromatographically purified.

1. May be used for in vitro Mini-YARS protein mediated interleukine-8 like activities regulation study with this protein as either coating matrix protein or soluble factor.

2. May be used for Mini-YARS protein – protein interaction assay.

3. As Enzymatic substrate for various proteases.

4. May be used for specific antibody production.