Recombinant Human Tyrosine--tRNA ligase, Cytoplasmic domain (YARS1)

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Code CSB-EP026245HU
Size $224
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Product Details

Greater than 90% as determined by SDS-PAGE.
Target Names
Uniprot No.
Research Area
Alternative Names
CMTDIC; SYYC_HUMAN; Tyrosine tRNA ligase, cytoplasmic; Tyrosine tRNA ligase 1, cytoplasmic; Tyrosyl tRNA synthetase; Tyrosyl--tRNA ligase; Tyrosyl-tRNA synthetase, cytoplasmic; TyrRS; yars; YRS; YTS
Homo sapiens (Human)
Expression Region
Target Protein Sequence
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
Protein Length
Full Length of Mature Protein
Tag Info
N-terminal GST-tagged
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Tris-based buffer,50% glycerol
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
3-7 business days
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.

Recombination of a plasmid encoding the Human YARS1 protein (2-528aa) is the first step during the production the recombinant Human YARS1 protein. The constructed plasmid is introduced into e.coli cells. e.coli cells that can survive in the presence of a specific antibiotic are selected to be cultured for the induction of protein expression. The protein is equipped with a N-terminal GST tag. After expression, affinity purification is used to isolate and purify the recombinant Human YARS1 protein from the cell lysate. Denaturing SDS-PAGE is then applied to resolve the resulting recombinant Human YARS1 protein. Its purity exceeds 90%.

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Target Background

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).
Gene References into Functions
  1. conclusion is further supported by a positive correlation across brain regions between TyrRS expression and arginine-accelerated KTP production. PMID: 29289698
  2. Platelet replenishment by YRS(ACT) is independent of thrombopoietin (TPO), as evidenced by expansion of the megakaryocytes from induced pluripotent stem cell-derived hematopoietic stem cells from a patient deficient in TPO signaling. PMID: 30104364
  3. These YARS variants occur in the catalytic domain and the C-terminal domain, respectively. Mutations in YARS have been previously associated with an autosomal dominant form of Charcot-Marie-Tooth (CMT); our findings suggest the disease spectrum associated with YARS dysregulation is broader than peripheral neuropathy. PMID: 27633801
  4. Studied the structural effect of three Charcot-Marie-Tooth disease-causing mutations in tyrosyl-tRNA synthetase. The mutations do not induce changes in protein secondary structures, or shared effects on oligomerization state and stability. However, all mutations provide access to a surface masked in the wild-type enzyme, and that access correlates with protein misinteraction. PMID: 28531329
  5. Data show that the internal deletion of tyrosyl-tRNA synthetase TyrRSDeltaE2-4 splice variants (SVs) gave an alternative, neomorphic dimer interface 'orthogonal' to that of native TyrRS. PMID: 26773056
  6. Expression of CMT-mutant tyrosyl-tRNA synthetase in Drosophila impairs protein translation. PMID: 26138142
  7. Computational modeling of molecular dynamics of G41R mutant form of human tyrosyl-tRNA synthetase, assosiated with Charcot-Marie-Tooth neuropathy has been presented. PMID: 27025069
  8. the association of rare YARS variant with late-onset autosomal dominant Charcot-Marie-Tooth neuropathy PMID: 24354524
  9. This study presents genetic evidence for common mutant-specific interactions between two CMT-associated aminoacyl-tRNA synthetases, lending support for a shared mechanism responsible for the synthetase-induced peripheral neuropathies. PMID: 24807208
  10. rhTyrRS promotes migration and aggregation of megakaryocytes to the bone marrow niche PMID: 24907514
  11. nuclear-localized TyrRS activates transcription factor E2F1 to upregulate the expression of DNA damage repair genes such as BRCA1 and RAD51. PMID: 25284223
  12. A major difference between the first- and second-generation tRNA synthetases (RSs) is that the second-generation RSs have an active site more compatible with tyrosine binding. PMID: 24611875
  13. The full length tyrosyl-tRNA synthetase lacks its cytokine activity because of the interactions between N-terminal and the C-terminal modules, which protect the ELR cytokine motif. PMID: 23334919
  14. Nuclear import of TyrRS is regulated by tRNA(Tyr). PMID: 22291016
  15. Dominant Intermediate Charcot-Marie-Tooth disorder is not due to a catalytic defect in tyrosyl-tRNA synthetase. PMID: 21732632
  16. Expression of tyrosyl-tRNA synthetase (YARS) DI-CMTC associated mutations (G41R, E196K,153-156delVKQV)in Drosophila leads to neuronal dysfunction. PMID: 19561293
  17. role in catalyzing tyrosyl-adenylate formation PMID: 11856731
  18. replacement of second lysine in KMSKS signature sequence by potassium PMID: 11927599
  19. role in inducing angiogenesis PMID: 11956181
  20. the KMSSS sequence in human tyrosyl-tRNA synthetase stabilizes the transition state for the tyrosine activation reaction by interacting with the pyrophosphate moiety of ATP PMID: 12016229
  21. The recently discovered proangiogenic role of a tyrosyl-tRNA synthetase fragment that stimulates immune cells and links translation to a major cell-signaling pathway is discussed in this review. PMID: 12416978
  22. The structure of human mini-TyrRS containing both the catalytic & the anticodon recognition domains, is reported to a resolution of 1.18 A. The spatial disposition of the anticodon recognition domain relative to the catalytic domain is unique. PMID: 12427973
  23. identification of two heterozygous missense mutations (G41R and E196K) and one de novo deletion (153-156delVKQV) in tyrosyl-tRNA synthetase (YARS) in three unrelated families affected with dominant intermediate Charcot-Marie-Tooth neuropathy PMID: 16429158
  24. Mutating a conserved tyrosine (Y341) that tethers a critical ELR motif in TyrRS resulted in subtle opening of the structure, and activation of cytokine functions, proving the possibility of constitutive gain-of-function mutations in tRNA ligases. PMID: 18096501
  25. Human tyrosyl-tRNA synthetase, where a catalytic-domain surface helix, next to the active site, was recruited for interleukin-8-like cytokine signaling. PMID: 19477417

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Involvement in disease
Charcot-Marie-Tooth disease, dominant, intermediate type, C (CMTDIC)
Subcellular Location
Protein Families
Class-I aminoacyl-tRNA synthetase family
Database Links

HGNC: 12840

OMIM: 603623

KEGG: hsa:8565

STRING: 9606.ENSP00000362576

UniGene: Hs.213264

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