|Application ||WB, IHC-P, E|
|Calculated MW||58777 Da|
|Other Names||Serine--tRNA ligase, cytoplasmic, Seryl-tRNA synthetase, SerRS, Seryl-tRNA(Ser/Sec) synthetase, SARS, SERS|
|Target/Specificity||This SARS antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 133-161 amino acids from the N-terminal region of human SARS.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||SARS Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Catalyzes the attachment of serine to tRNA(Ser) in a two-step reaction: serine is first activated by ATP to form Ser- AMP and then transferred to the acceptor end of tRNA(Ser) (PubMed:22353712, PubMed:24095058, PubMed:9431993, PubMed:26433229, PubMed:28236339). Is probably also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec) (PubMed:9431993, PubMed:26433229, PubMed:28236339). In the nucleus, binds to the VEGFA core promoter and prevents MYC binding and transcriptional activation by MYC (PubMed:24940000). Recruits SIRT2 to the VEGFA promoter, promoting deacetylation of histone H4 at 'Lys-16' (H4K16). Thereby, inhibits the production of VEGFA and sprouting angiogenesis mediated by VEGFA (PubMed:19423848, PubMed:19423847, PubMed:24940000).|
|Cellular Location||Cytoplasm. Nucleus. Note=Predominantly cytoplasmic, but a minor proportion is also found in the nucleus|
Provided below are standard protocols that you may find useful for product applications.
Seryl-tRNA synthetase belongs to the class II amino-acyl tRNA family. This enzyme catalyzes the transfer of L-serine to tRNA (Ser) and is related to bacterial and yeast counterparts.
Shimada,N., J. Biol. Chem. 276 (50), 46770-46778 (2001)
Shah,Z.H., Hum. Mutat. 17 (5), 433-434 (2001)
Heckl,M., FEBS Lett. 427 (3), 315-319 (1998)