Heat Shock Protein Assays
 | | | Depending on the level of stress, injured cells may undergo either necrosis or apoptosis. Under extreme stress conditions, when there is diminution in regulated activation of apoptotic pathways, cells undergo necrosis. At lower stress levels, cells activate their apoptotic machinery. However, at sub-lethal stress levels, cells may attempt to survive and activate a stress response system that includes a rapid induction of heat shock proteins (Hsp). Hsp interact with diverse protein substrates and assist in their folding and in the elimination of any misfolded or damaged molecules. They are transiently expressed during cell cycle to prevent differentiating cells from undergoing apoptosis. Many tumor cells have constitutively elevated levels of Hsp that impart protection against cytotoxic agents, thereby raising the apoptosis threshold of these cells. This abnormal expression of Hsp may lead to multi-drug resistance in aggressively growing tumors. Many Hsp, including Hsp27 and Hsp70, have been shown to block apoptosis. Hsp can also allow cancerous cells to escape the immunosurveillance mediated by death ligands and can render these cells resistant to chemotherapy. Hence, Hsp are fast becoming new targets for therapeutic interventions.
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| PhosphoDetect™ Hsp27 (pSer78/82) ELISA Kit |
96-well plate |
96 Tests |
0.1-10 ng/ml |
4.5 h |
Cell lysates |
CBA078 |
| Hsp27 ELISA Kit |
96-well plate |
96 Tests |
0.02-1 ng/ml |
3.5 h |
Cell lysates, plasma, serum, tissue extracts |
QIA119 |
| Hsp90a ELISA Kit |
96-well plate |
96 Tests |
0.3 - 20 ng/ml |
4 h |
Cell lysates, tissue extracts and biological fluids |
CBA057 |
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