Chaperone proteins and heat shock proteins are evolutionarily conserved proteins that work in protecting cells from oxidative and heat stresses. Notable members include Clusterin (CLU), Hsp70 and Hsp 60. Clusterin, a Golgi chaperone is known to protect cells from apoptosis. Hsp70 binds to partially unfolded proteins and allows them to refold. It also blocks the binding of procaspase-9 to the apoptosome, inhibiting progression of apoptosis. Mitochondrial protein Hsp60 is involved with proper folding of imported proteins. In investigating these proteins and related processes, ready-to-use ELISA kits may prove to be convenient and valuable tools.