Recombinant Human Tyrosyl tRNA synthetase/TyrRS protein is a Human Full Length protein, in the 1 to 528 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
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Tyrosine--tRNA ligase that 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) (Probable) (PubMed:25533949). Also acts as a positive regulator of poly-ADP-ribosylation in the nucleus, independently of its tyrosine--tRNA ligase activity (PubMed:25533949). Activity is switched upon resveratrol-binding: resveratrol strongly inhibits the tyrosine--tRNA ligase activity and promotes relocalization to the nucleus, where YARS1 specifically stimulates the poly-ADP-ribosyltransferase activity of PARP1 (PubMed:25533949).
YARS, YARS1, Tyrosyl-tRNA synthetase, TyrRS
Recombinant Human Tyrosyl tRNA synthetase/TyrRS protein is a Human Full Length protein, in the 1 to 528 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.316% Tris HCl, 0.0154% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
ab107141 is purified using conventional chromatography techniques.
Tyrosine--tRNA ligase that 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) (Probable) (PubMed:25533949). Also acts as a positive regulator of poly-ADP-ribosylation in the nucleus, independently of its tyrosine--tRNA ligase activity (PubMed:25533949). Activity is switched upon resveratrol-binding: resveratrol strongly inhibits the tyrosine--tRNA ligase activity and promotes relocalization to the nucleus, where YARS1 specifically stimulates the poly-ADP-ribosyltransferase activity of PARP1 (PubMed:25533949).
Belongs to the class-I aminoacyl-tRNA synthetase family.
Previously labelled as Tyrosyl tRNA synthetase
Tyrosyl tRNA synthetase also known as TyrRS is an enzyme responsible for charging tRNA molecules with the amino acid tyrosine. This process known as aminoacylation is essential for accurate translation of the genetic code during protein synthesis. TyrRS has a molecular weight of approximately 58 kDa. It is expressed in various tissues playing a significant role in both cytoplasmic and mitochondrial protein synthesis in eukaryotes.
TyrRS plays an important role in ensuring the fidelity of protein translation within cells. It facilitates the correct pairing of tRNA^Tyr with its corresponding tyrosine amino acid contributing to the accuracy of protein production. This enzyme is part of the aminoacyl-tRNA synthetase complex a multi-enzyme complex that catalyzes the attachment of specific amino acids to their appropriate tRNA molecules an important step in the translation process.
TyrRS is involved in the protein synthesis pathway where it functions alongside other aminoacyl-tRNA synthetases to help maintain the genetic code's accuracy. Additionally TyrRS is implicated in the aminoacyl-tRNA biosynthesis pathway connecting its activity with enzymes responsible for similar processes. It works closely with related enzymes such as phenylalanyl-tRNA synthetase (PheRS) and tryptophanyl-tRNA synthetase (TrpRS) through these pathways ensuring coordinated protein synthesis.
TyrRS has been connected to certain neurodegenerative diseases and cancer. Mutations in the TYRRS gene have been associated with Charcot-Marie-Tooth disease a hereditary neuropathy. The enzyme's altered function in this context may lead to compromised protein synthesis. Additionally aberrant TyrRS expression has been observed in some types of cancer where it interacts with proteins like angiogenin to potentially promote tumor growth. These connections highlight the enzyme's potential role in disease progression and pathogenesis.
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15% SDS-PAGE showing ab107141 (3 μg) at approximately 61.3 kDa.
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