Recombinant Human Tyrosine--tRNA ligase, cytoplasmic (YARS)

Code CSB-YP026245HU
MSDS
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Source Yeast
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Code CSB-EP026245HU-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP026245HU
MSDS
Size Pls inquire
Source Baculovirus
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Code CSB-MP026245HU
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
YARS
Uniprot No.
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
Species
Homo sapiens (Human)
Expression Region
2-528
Target Protein Sequence
GDAPSPEEK LHLITRNLQE VLGEEKLKEI LKERELKIYW GTATTGKPHV AYFVPMSKIA DFLKAGCEVT ILFADLHAYL DNMKAPWELL ELRVSYYENV IKAMLESIGV PLEKLKFIKG TDYQLSKEYT LDVYRLSSVV TQHDSKKAGA EVVKQVEHPL LSGLLYPGLQ ALDEEYLKVD AQFGGIDQRK IFTFAEKYLP ALGYSKRVHL MNPMVPGLTG SKMSSSEEES KIDLLDRKED VKKKLKKAFC EPGNVENNGV LSFIKHVLFP LKSEFVILRD EKWGGNKTYT AYVDLEKDFA AEVVHPGDLK NSVEVALNKL LDPIREKFNT PALKKLASAA YPDPSKQKPM AKGPAKNSEP EEVIPSRLDI RVGKIITVEK HPDADSLYVE KIDVGEAEPR TVVSGLVQFV PKEELQDRLV VVLCNLKPQK MRGVESQGML LCASIEGINR QVEPLDPPAG SAPGEHVFVK GYEKGQPDEE LKPKKKVFEK LQADFKISEE CIAQWKQTNF MTKLGSISCK SLKGGNIS
Protein Length
Full Length of Mature Protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
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.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
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
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
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
Cytoplasm.
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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