Involved in ATP binding, has serine-tRNA ligase activity and involved in seryl-tRNA aminoacylation. The 3 substrates of this enzyme are ATP, L-serine, and tRNA(Ser), whereas its 3 products are AMP, diphosphate, and L-seryl-tRNA(Ser). This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-serine:tRNASer ligase (AMP-forming). Other names in common use include seryl-tRNA synthetase, SerRS, seryl-transfer ribonucleate synthetase, seryl-transfer RNA synthetase, seryl-transfer ribonucleic acid synthetase, and serine translase. This enzyme participates in glycine, serine and threonine metabolism and aminoacyl-trna biosynthesis.
Background References
1. Gaudet P et al. Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12:449-462 (2011).
Western blot analysis of SARS2 on Zebrafish tissue lysate. Proteins were transferred to a PVDF membrane and blocked with 5% BSA in PBS for 1 hour at room temperature. The primary antibody (ER1902-38, 1/500) was used in 5% BSA at room temperature for 2 hours. Goat Anti-Rabbit IgG - HRP Secondary Antibody (HA1001) at 1:5,000 dilution was used for 1 hour at room temperature.
IF staining of SARS2 in Zebrafish tissue(green). The nuclear counter stain is DAPI (blue). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS.
Immunohistochemical analysis of paraffin-embedded Zebrafish tissue using anti-SARS2 antibody. Counter stained with hematoxylin.
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