YARS Human; Tyrosyl-tRNA Synthetase Human Recombinant; Tyrosyl-tRNA synthetase cytoplasmic; Tyrosyl--tRNA ligase; TyrRS; YARS; YRS; YTS; CMTDIC

For Research Use Only. Not for use in diagnostic procedures.

E Coli

Greater than 90.0% as determined by SDS-PAGE.

YARS protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.
Sterile Filtered colorless solution.

Store at 4 degree C if entire vial will be used within 2-4 weeks. Store, frozen at -20 degree C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

Small volumes of YARS recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Description: YARS produced in E Coli is a single, non-glycosylated polypeptide chain containing 548 amino acids (1-528 a.a.) and having a molecular mass of 61.3kDa.YARS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Introduction: Tyrosyl-tRNA synthetase (YARS) is a member of the class I tRNA synthetase family. YARS is a vital enzyme which catalyzes the aminoacylation of tRNATrp with tryptophan, a critical function of the cell's protein synthesis machinery. Expression of YARS is highly stimulated in human cells by the addition of IFN-gamma.

ENZYMES; Enzymes; Synthetase

59,143 Da

tyrosyl-tRNA synthetase

tyrosine--tRNA ligase, cytoplasmic; tyrosine tRNA ligase 1, cytoplasmic; tyrosyl--tRNA ligase; tyrosyl-tRNA synthetase, cytoplasmic

Tyrosine--tRNA ligase, cytoplasmic

TyrRS??[Similar Products]

SYYC_HUMAN

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 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 is an interleukin-8-like cytokine, whereas the released C-terminal fragment is an EMAP II-like cytokine. [provided by RefSeq, Jul 2008]

YARS: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr- AMP and then transferred to the acceptor end of tRNA(Tyr). Defects in YARS are the cause of Charcot-Marie-Tooth disease dominant intermediate type C (CMTDIC). CMTDIC is a form of Charcot-Marie-Tooth disease characterized by clinical and pathologic features intermediate between demyelinating and axonal peripheral neuropathies, and motor median nerve conduction velocities ranging from 25 to 45 m/sec. Belongs to the class-I aminoacyl-tRNA synthetase family.

Protein type: EC 6.1.1.1; Ligase

Chromosomal Location of Human Ortholog: 1p35.1

Cellular Component: extracellular space; cytoplasm; cytosol; nucleus

Molecular Function: signal transducer activity; tyrosine-tRNA ligase activity; ATP binding; tRNA binding; isoleucine-tRNA ligase activity; interleukin-8 receptor binding

Biological Process: isoleucyl-tRNA aminoacylation; tyrosyl-tRNA aminoacylation; tRNA aminoacylation for protein translation; apoptosis; gene expression; signal transduction

Disease: Charcot-marie-tooth Disease, Dominant Intermediate C

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