The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
1/50 - 1/100. Detects a band of approximately 107 kDa (predicted molecular weight: 107 kDa).
1/10 - 1/50.
FunctionCatalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.
Involvement in diseaseCharcot-Marie-Tooth disease 2N
Sequence similaritiesBelongs to the class-II aminoacyl-tRNA synthetase family.
DomainConsists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs. The C-terminal C-Ala domain (residues 756 to 968), along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs. The human domain can be used in vitro to replace the corresponding domain in E.coli.
ab71289 at 1/50 dilution staining AlaRS N - terminal in human hepatocarcinoma tissue section by Immunohistochemistry (Formalin/ PFA fixed paraffin-embedded sections). A peroxidase conjugated secondary antibody was used followed by DAB staining.
References for Anti-AlaRS antibody - N-terminal (ab71289)
has not yet been referenced specifically in any publications.
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