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Lysine-tRNA ligase, also known as Lysyl-tRNA synthetase, LysRS, KARS and KIAA0070, belongs to the class-II aminoacyl-tRNA synthetase family. The N-terminal cytoplasmic domain (1-65) is a functional tRNA-binding domain, which is required for nuclear localization, is involved in the interaction with DARS, but has a repulsive role in the binding to EEF1A1. A central domain (208-259) is involved in homodimerization and is required for interaction with HIV-1 GAG and incorporation into virions. KARS catalyzes the specific attachment of an amino acid to its cognate tRNA in a two step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. Defects in KARS are the cause of Charcot-Marie-Tooth disease recessive intermediate type B (CMTRIB).

| Pack Size | Price | USA Warehouse | Global Warehouse | Quantity |
|---|---|---|---|---|
| 5 μg | $112 | 7-10 days | 7-10 days | |
| 10 μg | $183 | 7-10 days | 7-10 days | |
| 20 μg | $292 | 7-10 days | 7-10 days | |
| 50 μg | $545 | 7-10 days | 7-10 days | |
| 100 μg | $792 | 7-10 days | 7-10 days | |
| 200 μg | $1,150 | 7-10 days | 7-10 days | |
| 500 μg | $1,900 | 7-10 days | 7-10 days | |
| 1 mg | $2,730 | 7-10 days | 7-10 days |
| Biological Activity | Activity has not been tested. It is theoretically active, but we cannot guarantee it. If you require protein activity, we recommend choosing the eukaryotic expression version first. |
| Description | Lysine-tRNA ligase, also known as Lysyl-tRNA synthetase, LysRS, KARS and KIAA0070, belongs to the class-II aminoacyl-tRNA synthetase family. The N-terminal cytoplasmic domain (1-65) is a functional tRNA-binding domain, which is required for nuclear localization, is involved in the interaction with DARS, but has a repulsive role in the binding to EEF1A1. A central domain (208-259) is involved in homodimerization and is required for interaction with HIV-1 GAG and incorporation into virions. KARS catalyzes the specific attachment of an amino acid to its cognate tRNA in a two step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. Defects in KARS are the cause of Charcot-Marie-Tooth disease recessive intermediate type B (CMTRIB). |
| Species | Human |
| Expression System | HEK293 Cells |
| Tag | C-6xHis |
| Accession Number | Q15046 |
| Synonyms | Lysyl-tRNA Synthetase,LysRS,Lysine--tRNA Ligase,KIAA0070,KARS |
| Amino Acid | Ala2-Val597 |
| Construction | Ala2-Val597 |
| Protein Purity | Greater than 95% as determined by reducing SDS-PAGE. (QC verified) |
| Molecular Weight | 70-90 KDa (reducing condition) |
| Endotoxin | < 0.1 ng/µg (1 EU/µg) as determined by LAL test. |
| Formulation | Supplied as a 0.2 μm filtered solution of 20 mM Tris-HCl, 100 mM NaCl, 1 mM DTT, 20% Glycerol, pH 8.0. |
| Stability & Storage | Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots. |
| Shipping | Shipping with blue ice. |
| Research Background | Lysine-tRNA ligase, also known as Lysyl-tRNA synthetase, LysRS, KARS and KIAA0070, belongs to the class-II aminoacyl-tRNA synthetase family. The N-terminal cytoplasmic domain (1-65) is a functional tRNA-binding domain, which is required for nuclear localization, is involved in the interaction with DARS, but has a repulsive role in the binding to EEF1A1. A central domain (208-259) is involved in homodimerization and is required for interaction with HIV-1 GAG and incorporation into virions. KARS catalyzes the specific attachment of an amino acid to its cognate tRNA in a two step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. Defects in KARS are the cause of Charcot-Marie-Tooth disease recessive intermediate type B (CMTRIB). |
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