HSP60 (D6F1) XP ® Rabbit mAb

In both prokaryotic and eukaryotic cells the misfolding and aggregation of proteins during biogenesis and under conditions of cellular stress are prevented by molecular chaperones (1-3). HSP60 has primarily been known as a mitochondrial protein that is important for folding key proteins after import into the mitochondria (4). Research studies have shown that a significant amount of HSP60 is also present in the cytosol of many cells, and that it is induced by stress, inflammatory and immune responses, and autoantibodies correlated with Alzheimer's, coronary artery diseases, MS, and diabetes (5-8). 1.Hartl, F.U. (1996) Nature 381, 571-579. 2.Bukau, B. and Horwich, A.L. (1998) Cell 92, 351-366. 3.Hartl, F.U. and Hayer-Hartl, M. (2002) Science 295, 1852-1858. 4.Jindal, S. et al. (1989) Mol. Cell Biol. 9, 2279-2283. 5.Itoh, H. et al. (2002) Eur. J. Biochem. 269, 5931-5938. 6.Gupta, S. and Knowlton, A.A. J. Cell Mol. Med. 9, 51-58. 7.Deocaris, C.C. et al. (2006) Cell Stress Chaperones 11, 116-128. 8.Lai, H.C. et al. (2007) Am. J. Physiol. Endocrinol. Metab. 292, E292-E297.