Product Pathways - Translational Control
LysRS Antibody #5341
PhosphoSitePlus® protein, site, and accession data: KARS
| Applications | Reactivity | Sensitivity | MW (kDa) | Source |
|---|---|---|---|---|
| W IP | H M R | Endogenous | 75 | Rabbit |
Applications Key:
W=Western Blotting
IP=Immunoprecipitation
Reactivity Key:
H=Human
M=Mouse
R=Rat
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Protocols
Specificity / Sensitivity
LysRS Antibody detects the endogenous levels of total LysRS protein.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Glu325 of human LysRS protein. Antibodies were purified by protein A and peptide affinity chromatography.
Background
Lysyl-tRNA synthetase (LysRS) is a multifunctional protein that has both regular and mitochondrial forms. The regular form of LysRS belongs to a family of aminoacyl-tRNA synthetases (aaRSs) that catalyze amino acid attachment to its cognate tRNA. In mammalian systems, LysRS forms a multisystem complex (MSC) with several other aaRSs (1-3). In addition to its conventional function, LysRS regulates diadenosine tetraphosphate (Ap4A) production (3). Cellular and metabolic stress increases the level of Ap4A, which functions as a cellular alarm system (3-5). Following FcεRI aggregation in mast cells, MAPK/Erk kinase (MEK) phosphorylates LysRS at Ser207 (5). Serine phosphorylation of LysRS leads to the release of LysRS from MSC and its translocation into the nucleus (5), as well as increased synthesis of Ap4A (5,6). LysRS binds to microphthalmia transcription factor (MITF) and MITF repressor Hint-1. Upon binding of Ap4A, Hint-1 is released from the complex that in turn allows the transcription of MITF-responsive genes (5-7). LysRS is also involved in HIV viral assembly through incorporation into HIV-1 virions via an interaction with HIV-1 Gag (8). Research studies have shown that in the presence of mutant Cu,Zn-superoxide dismutase (SOD1), mitochondrial LysRS tends to be misfolded and degraded by proteasomal degradation, contributing to mitochondrial dysfunction in Amyotrophic Lateral Sclerosis (ALS) (9). LysRS is also secreted and has cytokine-like functions (10). LysRS was also found to be an autoantigen in autoimmune responses (11).
- SzymaĆski, M. et al. (2000) Acta Biochim Pol 47, 821-34.
- Bandyopadhyay, A.K. and Deutscher, M.P. (1971) J Mol Biol 60, 113-22.
- Wahab, S.Z. and Yang, D.C. (1985) J Biol Chem 260, 5286-9.
- Yannay-Cohen, N. et al. (2009) Mol Cell 34, 603-11.
- Lee, Y.N. and Razin, E. (2005) Mol Cell Biol 25, 8904-12.
- Lee, Y.N. et al. (2004) Immunity 20, 145-51.
- Nechushtan, H. and Razin, E. (2002) Mol Immunol 38, 1177-80.
- Kovaleski, B.J. et al. (2006) J Biol Chem 281, 19449-56.
- Kawamata, H. et al. (2008) J Biol Chem 283, 28321-8.
- Park, S.G. et al. (2005) Proc Natl Acad Sci USA 102, 6356-61.
- Linke, A.T. et al. (2001) Clin Exp Immunol 126, 173-9.
Application References
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For Research Use Only. Not For Use In Diagnostic Procedures.