Recombinant Human Tryptophanyl tRNA synthetase/WRS protein is a Human Full Length protein, in the 1 to 471 aa range, expressed in Escherichia coli, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, HPLC.
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Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application HPLC | Reactivity Reacts | Dilution info - | Notes - |
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Catalyzes the attachment of tryptophan to tRNA(Trp) in a two-step reaction: tryptophan is first activated by ATP to form Trp-AMP and then transferred to the acceptor end of the tRNA(Trp). Isoform 1. Has no angiostatic activity. T2-TrpRS. Possesses an angiostatic activity but has no aminoacylation activity (PubMed:11773625, PubMed:11773626, PubMed:14630953). Inhibits fluid shear stress-activated responses of endothelial cells (PubMed:14630953). Regulates ERK, Akt, and eNOS activation pathways that are associated with angiogenesis, cytoskeletal reorganization and shear stress-responsive gene expression (PubMed:14630953). Isoform 2. Has an angiostatic activity.
IFI53, WARS, WRS, WARS1, Interferon-induced protein 53, Tryptophanyl-tRNA synthetase, IFP53, TrpRS, hWRS
Recombinant Human Tryptophanyl tRNA synthetase/WRS protein is a Human Full Length protein, in the 1 to 471 aa range, expressed in Escherichia coli, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, HPLC.
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.32% Tris HCl, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
Purity is determined by SEC-HPLC and reducing SDS-PAGE.
Catalyzes the attachment of tryptophan to tRNA(Trp) in a two-step reaction: tryptophan is first activated by ATP to form Trp-AMP and then transferred to the acceptor end of the tRNA(Trp).
Belongs to the class-I aminoacyl-tRNA synthetase family.
Proteolytic cleavage generates 2 forms; T1-TrpRS and T2-TrpRS.
Previously labelled as Tryptophanyl tRNA synthetase.
Tryptophanyl tRNA synthetase also known as WRS or TrpRS is an enzyme responsible for attaching tryptophan to its corresponding tRNA during protein synthesis. This enzyme is approximately 53 kDa in mass. It ensures the accurate translation of the genetic code in mRNA into proteins by catalyzing the esterification of tryptophan to the tRNA^Trp. WRS is mostly found in the cytoplasm of cells across various tissues contributing to its role in protein biosynthesis.
WRS is involved in the important process of protein translation ensuring fidelity in the genetic code transfer from RNA to protein. As part of the aminoacyl-tRNA synthetases family WRS helps in maintaining the overall function and stability of the translational apparatus. It is not typically known to be part of any larger protein complex. In addition to its core function in protein synthesis WRS possesses non-canonical roles related to immune response regulation and angiogenesis.
WRS plays key roles in the aminoacyl-tRNA biosynthesis and mTOR signaling pathways. These pathways are essential for regulating protein synthesis and cell growth. In the mTOR pathway WRS's function relates to its interaction with proteins involved in cell growth and proliferation. Its roles within these pathways highlight its influence on cellular homeostasis and protein regulation interacting closely with other synthetases and transcription factors.
WRS has associations with certain cancers and autoimmune disorders. Abnormal expression of WRS is observed in various cancer types reflecting its contribution to dysregulated protein synthesis and cell growth. Additionally WRS has been linked to autoimmune diseases like dermatomyositis where its immune-regulatory roles become compromised. In these conditions WRS's interactions with proteins such as interferons illustrate its importance in the pathophysiology of inflammation and immune response.
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