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Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Additionally we are shipping Tyrosyl-tRNA Synthetase Antibodies (61) and many more products for this protein.
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Human Yars Protein expressed in Escherichia coli (E. coli) - ABIN667910
Kise, Lee, Park, Fukai, Sengoku, Ishii, Yokoyama, Kim, Nureki: A short peptide insertion crucial for angiostatic activity of human tryptophanyl-tRNA synthetase. in Nature structural & molecular biology 2004
Show all 2 references for ABIN667910
This study showed that show that apoptotic loser cells secrete Tyrosyl-tRNA synthetase, which is best known as a core component of the translational machinery.
Dominant mutations in the tyrosyl-tRNA synthetase gene recapitulate in Drosophila features of human Charcot-Marie-Tooth neuropathy.
Data show that the internal deletion of tyrosyl-tRNA synthetase TyrRSDeltaE2-4 splice variants (SVs (show FGFR2 Proteins)) gave an alternative, neomorphic dimer interface 'orthogonal' to that of native TyrRS.
Expression of CMT-mutant tyrosyl-tRNA synthetase in Drosophila impairs protein translation.
Computational modeling of molecular dynamics of G41R mutant form of human tyrosyl-tRNA synthetase, assosiated with Charcot-Marie-Tooth neuropathy has been presented.
the association of rare YARS variant with late-onset autosomal dominant Charcot-Marie-Tooth neuropathy
nuclear-localized TyrRS activates transcription factor E2F1 (show E2F1 Proteins) to upregulate the expression of DNA damage repair genes such as BRCA1 and RAD51 (show RAD51 Proteins).
A major difference between the first- and second-generation tRNA synthetases (RSs (show GRB10 Proteins)) is that the second-generation RSs (show GRB10 Proteins) have an active site more compatible with tyrosine binding.
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.
Naturally occurring fragments of the two proteins involved in translation, TyrRS and TrpRS (show WARS Proteins), have opposing activities on angiogenesis.
Nuclear import of TyrRS is regulated by tRNA(Tyr (show TYR Proteins)).
Dominant Intermediate Charcot-Marie-Tooth disorder is not due to a catalytic defect in tyrosyl-tRNA synthetase.
Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in linking amino acids with nucleotide triplets contained in tRNAs, aminoacyl-tRNA synthetases are thought to be among the first proteins that appeared in evolution. Tyrosyl-tRNA synthetase belongs to the class I tRNA synthetase family. Cytokine activities have also been observed for the human tyrosyl-tRNA synthetase, after it is split into two parts, an N-terminal fragment that harbors the catalytic site and a C-terminal fragment found only in the mammalian enzyme. The N-terminal fragment is an interleukin-8-like cytokine, whereas the released C-terminal fragment is an EMAP II-like cytokine.
tyrosine--tRNA ligase, cytoplasmic
, tyrosyl--tRNA ligase
, tyrosyl-tRNA synthetase, cytoplasmic
, tyrosyl-tRNA synthetase
, Tyrosyl-tRNA synthetase, cytoplasmic
, tyrosine tRNA ligase 1, cytoplasmic