Species : |
Human |
Source : |
E.coli |
Tag : |
His |
Protein Length : |
3-528 a.a. |
Description : |
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. |
Conjugation : |
HIS |
Form : |
Lyophilised:reconstitution with 135 μl distilled water. |
Storage buffer : |
Preservative: NoneConstituents: 0.5% Trehalose, 6M Urea, 100mM Sodium hydrogen phosphate, 10mM Sodium chloride, pH 4.5 |
Storage : |
Shipped at 4°C. Upon delivery aliquot and store at -80oC. Avoid freeze / thaw cycles. |
Sequences of amino acids : |
DAPSPEEKLHLITRNLQEVLGEEKLKEILKERELKIYWGT ATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYL DNMKAPWELLELRVSYYENVIKAMLESIGVPLEKLKFI KGTDYQLSKEYTLDVYRLSSVVTQHDSKKAGAEVVKQVEH PLLSGLLYPGLQALDEEYLKVDAQFGGIDQRKIFTFAE KYLPALGYSKRVHLMNPMVPGLTGSKMSSSEEESKIDL LDRKEDVKKKLKKAFCEPGNVENNGVLSFIKHVLFPLKSEFVILRDEKWGGNKTYTAYVDLEKDFAAEVVHPGDLKNS VEVALNKLLDPIREKFNTPALKKLASAAYPDPSKQKPM AKGPAKNSEPEEVIPSRLDIRVGKIITVEKHPDADSLY VEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKP QKMRGVESQGMLLCASIEGINRQVEPLDPPAGSAPGEH VFVKGYEKGQPDEELKPKKKVFEKLQADFKISEECIAQ WKQTNFMTKLGSISCKSLKGGNIS |
Sequence Similarities : |
Belongs to the class-I aminoacyl-tRNA synthetase family.Contains 1 tRNA-binding domain. |