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Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid.
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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.
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.
Tryptophanyl-tRNA synthetase expression is up-regulated in patients with rheumatoid arthritis.
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 (zeige TBX15 Antikörper)/WARS2 (zeige WARS2 Antikörper), STAB1 (zeige STAB1 Antikörper), PIGC (zeige PIGC Antikörper), ZNRF3 (zeige ZNRF3 Antikörper), GRB14 (zeige GRB14 Antikörper))
Indoleamine2,3-dioxygenase and tryptophanyl-tRNA synthetase may play critical roles in the immune pathogenesis of chronic kidney disease.
Naturally occurring fragments of the two proteins involved in translation, TyrRS (zeige Yars Antikörper) and TrpRS, have opposing activities on angiogenesis.
Tryptophanyl-tRNA synthetase down-regulation by hypoxia may be a factor responsible for low TrpRS in pancreatic tumors with high metastatic ability.
Mini-tryptophanyl-tRNA synthetase inhibited ischemic angiogenesis in rats.
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.
Low tryptophanyl-tRNA synthetase is associated with recurrence in colorectal cancer.
a VE-cadherin (zeige CDH5 Antikörper)-dependent pathway may link T2-TrpRS to inhibition of new blood vessel formation
TrpRS plays a role in protecting against neurodegeneration is suggested, providing an insight into the pathogenesis and a possible treatment of neurodegenerative diseases.
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. Two forms of tryptophanyl-tRNA synthetase exist, a cytoplasmic form, named WARS, and a mitochondrial form, named WARS2. Tryptophanyl-tRNA synthetase (WARS) catalyzes the aminoacylation of tRNA(trp) with tryptophan and is induced by interferon. Tryptophanyl-tRNA synthetase belongs to the class I tRNA synthetase family. Four transcript variants encoding two different isoforms have been found for this gene.
, interferon-induced protein 53
, tryptophan tRNA ligase 1, cytoplasmic
, tryptophan--tRNA ligase, cytoplasmic
, tryptophanyl-tRNA synthetase, cytoplasmic
, tryptophanyl-tRNA synthetase
, Tryptophanyl-tRNA synthetase, cytoplasmic
, tryptophanyl-tRNA synthetase II
, tryptophan-tRNA synthetase