Related Product Information for anti-AIMP2 antibody
AIMP2 is an important component for association of ARS multi-complex. AIMP2 is a potent tumor suppressor. AIMP2 inhibit cmyc activity in TGF-beta signaling, link c-lAP1 to TRAF2 by TNF-alpha stimulation and activation p53 under DNA damaged condition.
References
1. Chemical suppression of an oncogenic splicing variant of AIMP2 induces tumour regression. Hee Sook LEE et al., Biochem. J. Vol.454, 411-416, 2013. 2. Splicing variant of AIMP2 as an effective target against chemoresistant ovarian cancer. Jin Woo Choi et al., Journal of Molecular Cell Biology, Vol.4, 164-173, 2012. 3. Cancer-Associated Splicing Variant of Tumor Suppressor AIMP2/p38: Pathological Implication in Tumorigenesis. Jin Woo Choi et al., PLoS Genetics, Vol.7, Issue 3, e1001351, 2011. 4. AIMP2/p38 promotes TNF-alpha-dependent apoptosis via ubiquitin-mediated degradation of TRAF2. Jinwoo Choi et al, J. Cell Sci, Vol.122, 2710-2715, 2009. 5. Multi-directional tumor suppressive activity of AIMP2/p38 and the enhanced susceptibility of AIMP2heterozygous mice to multi-organ carcinogenesis. Jinwoo Choi et al., Carcinogenesis, Vol.30, 1638-1644, 2009. 6. AIMP2/p38, the scaffold for multi-tRNA synthetase complex, responds to genotoxic stresses via p53. Jung Min Han et al., PNAS, Vol.105, 11206-11211, 2008. 7. Accumulation of the Authentic Parkin Substrate AminoacyltRNA Synthetase Cofactor, p38/JTV-1, Leads to Catecholaminergic Cell Death. Han Seok Ko et al., The Journal of Neuroscience, Vol.25(35), 7968-7978, 2005. 8. Downregulation of FUSE-binding protein and c-myc by tRNA synthetase cofactor p38 is required for lung cell differentiation. Min Jung Kim et al., NATURE GENETICS, Vol.34(3), 2003. 9. Solution structure and p43 binding of the p38 leucine zipper motif: coiled-coil interactions mediate the association between p38 and p43. Hee-Chul Ahn et al., FEBS Letters, Vol.542, 119-124, 2003. 10. p38 is essential for the assembly and stability of macromolecular tRNA synthetase complex: Implications for its physiological significance. Jin Young Kim et al., PNAS, Vol.99(12), 7912-7916, 2002.