Anti-AlaRS/AARS1 Antibody Picoband® Fluoro647 Conjugated

An aminoacyl-tRNA synthetase (aaRS or ARS), also called tRNA-ligase, is an enzyme that attaches the appropriate amino acid onto its corresponding tRNA. The human alanyl-tRNA synthetase (AARS) belongs to a family of tRNA synthases, of the class II enzymes. Class II tRNA synthases evolved early in evolution and are highly conserved. This is reflected by the fact that 498 of the 968-residue polypeptide human AARS shares 41% identity witht the E.coli protein. tRNA synthases are the enzymes that interpret the RNA code and attach specific aminoacids to the tRNAs that contain the cognate trinucleotide anticodons. They consist of a catalytic domain which interacts with the amino acid acceptor-T psi C helix of the tRNA, and a second domain which interacts with the rest of the tRNA structure.

ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon.

1. Chihade, J. W., Brown, J. R., Schimmel, P. R., Ribas de Pouplana, L. Origin of mitochondria in relation to evolutionary history of eukaryotic alanyl-tRNA synthetase. Proc. Nat. Acad. Sci. 97: 12153-12157, 2000. 2. Guo, M., Chong, Y. E., Beebe, K., Shapiro, R., Yang, X.-L., Schimmel, P. The C-Ala domain brings together editing and aminoacylation functions on one tRNA. Science 325: 744-747, 2009. Note: Erratum: Science 326: 46 only, 2009. 3. Guo, M., Chong, Y. E., Shapiro, R., Beebe, K., Yang, X.-L., Schimmel, P. Paradox of mistranslation of serine for alanine caused by AlaRS recognition dilemma. Nature 462: 808-812, 2009.