Recombinant Human Tryptophan--tRNA ligase, cytoplasmic(WARS)

Code CSB-BP025965HU
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Source Baculovirus
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Code CSB-EP025965HU-B
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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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Product Details

Purity >85% (SDS-PAGE)
Target Names WARS
Uniprot No. P23381
Alternative Names Gamma 2; GAMMA-2; Gamma2; hWRS; IFI 53; IFI53; IFP 53; IFP53; Interferon induced protein 53; Interferon-induced protein 53; SYWC_HUMAN; T2-TrpRS; TrpRS; Tryptophan tRNA ligase; cytoplasmic; Tryptophan tRNA ligase 1 cytoplasmic; Tryptophan tRNA ligase; Tryptophan--tRNA ligase; Tryptophanyl tRNA synthetase ; Tryptophanyl tRNA synthetase cytoplasmic; WARS; WARS protein; WRS
Species Homo sapiens (Human)
Expression Region 2-471
Target Protein Sequence PNSEPASLL ELFNSIATQG ELVRSLKAGN ASKDEIDSAV KMLVSLKMSY KAAAGEDYKA DCPPGNPAPT SNHGPDATEA EEDFVDPWTV QTSSAKGIDY DKLIVRFGSS KIDKELINRI ERATGQRPHH FLRRGIFFSH RDMNQVLDAY ENKKPFYLYT GRGPSSEAMH VGHLIPFIFT KWLQDVFNVP LVIQMTDDEK YLWKDLTLDQ AYSYAVENAK DIIACGFDIN KTFIFSDLDY MGMSSGFYKN VVKIQKHVTF NQVKGIFGFT DSDCIGKISF PAIQAAPSFS NSFPQIFRDR TDIQCLIPCA IDQDPYFRMT RDVAPRIGYP KPALLHSTFF PALQGAQTKM SASDPNSSIF LTDTAKQIKT KVNKHAFSGG RDTIEEHRQF GGNCDVDVSF MYLTFFLEDD DKLEQIRKDY TSGAMLTGEL KKALIEVLQP LIAEHQARRK EVTDEIVKEF MTPRKLSFDF Q
Protein Length Full Length of Mature Protein
Tag Info The following tags are available.
N-terminal His-tagged
Tag-Free
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
Protein 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
Isoform 1, isoform 2 and T1-TrpRS have aminoacylation activity while T2-TrpRS lacks it. Isoform 2, T1-TrpRS and T2-TrpRS possess angiostatic activity whereas isoform 1 lacks it. T2-TrpRS inhibits fluid shear stress-activated responses of endothelial cells. Regulates ERK, Akt, and eNOS activation pathways that are associated with angiogenesis, cytoskeletal reorganization and shear stress-responsive gene expression.
Gene References into Functions
  1. Based on these results, secretion of full-length tryptophanyl-tRNA synthetase appears to work as a primary defence system against infection, acting before full activation of innate immunity. PMID: 27748732
  2. findings establish WARS as a gene whose mutations may cause distal hereditary motor neuropathy and alter canonical and non-canonical functions of tryptophanyl-tRNA synthetase. PMID: 28369220
  3. Overexpression of WARS predicts no recurrence and good survival for triple-negative breast cancer patients. PMID: 26209610
  4. Tryptophanyl-tRNA synthetase expression is up-regulated in patients with rheumatoid arthritis. PMID: 24515434
  5. Genes within recently identified loci associated with waist-hip ratio (WHR) exhibit fat depot-specific mRNA expression, which correlates with obesity-related traits. Adipose tissue (AT) mRNA expression of 6 genes (TBX15/WARS2, STAB1, PIGC, ZNRF3, GRB14) PMID: 23670221
  6. Indoleamine2,3-dioxygenase and tryptophanyl-tRNA synthetase may play critical roles in the immune pathogenesis of chronic kidney disease. PMID: 23651343
  7. Naturally occurring fragments of the two proteins involved in translation, TyrRS and TrpRS, have opposing activities on angiogenesis. PMID: 21442253
  8. Tryptophanyl-tRNA synthetase down-regulation by hypoxia may be a factor responsible for low TrpRS in pancreatic tumors with high metastatic ability. PMID: 21926542
  9. Mini-tryptophanyl-tRNA synthetase inhibited ischemic angiogenesis in rats. PMID: 20963594
  10. Tryptophanyl-tRNA synthetase is a multidomain protein exhibiting excellent allosteric communication, and this research has provided valuable structural as well as functional insights into the protein. PMID: 19768679
  11. Low tryptophanyl-tRNA synthetase is associated with recurrence in colorectal cancer. PMID: 19900940
  12. In this study, we show that a recombinant form of a COOH-terminal fragment of TrpRS is a potent antagonist of vascular endothelial growth factor-induced angiogenesis in a mouse model and of naturally occurring retinal angiogenesis in the neonatal mouse PMID: 11773625
  13. Thus, protein synthesis may be linked to the regulation of angiogenesis by a natural fragment of TrpRS PMID: 11773626
  14. Recognition by tryptophanyl-tRNA synthetases of discriminator base on tRNATrp from three biological domains PMID: 11834741
  15. The recently discovered antiangiogenic and cell-signaling activities of tryptophanyl-tRNA synthetase bioactive fragments are discussed in this review. PMID: 12416978
  16. TrpRS may have a role in the maintenance of vascular homeostasis PMID: 14630953
  17. results suggest that mammalian and bacterial tryptophanyl-tRNA synthetase might use different mechanisms to recognize the substrate and modeling studies indicate that transfer RNA binds with the dimeric enzyme PMID: 14660560
  18. A crystal structure of human tryptophanyl-tRNA synthetase was solved at 2.1 A with a tryptophanyl-adenylate bound at the active site PMID: 14671330
  19. May play an important role in the intracellular regulation of protein synthesis under conditions of oxidative stress. PMID: 15628863
  20. These crystals captured two conformations of the human tryptophanyl-tRNA synthetase and tRNATrp complex, which are nearly identical with respect to the protein and a bound tryptophan. PMID: 16724112
  21. The first crystal structure of human tryptophanyl-tRNA synthetase (hTrpRS) in complex with tRNA(Trp) and Trp which, together with biochemical data, reveals the molecular basis of a novel tRNA binding and recognition mechanism. PMID: 16798914
  22. Results provide the first evidence of the involvement of heme in regulation of TrpRS aminoacylation activity. PMID: 17877375
  23. the annexin II-S100A10 complex, which regulates exocytosis, forms a ternary complex with TrpRS. PMID: 17999956
  24. Analysis of the molecular basis of the mechanisms of the substrate recognition and the activation reaction by tryptophanyl-tRNA synthetase. PMID: 18180246
  25. Indoleamine 2,3-dioxygenase (IDO)-expression in antigen-presenting cells (APCs) may control autoimmune responses by depleting the available tryptophan, whereas tryptophanyl-tRNA synthetase (TTS) may counteract this effect PMID: 19363598

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Subcellular Location Cytoplasm.
Protein Families Class-I aminoacyl-tRNA synthetase family
Database Links

HGNC: 12729

OMIM: 191050

KEGG: hsa:7453

STRING: 9606.ENSP00000347495

UniGene: Hs.497599

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