Defective protein homeostasis (proteostasis) is a key driver of many age-related diseases in humans and is recognized as a key element in normal aging. We developed a proteome-wide assay of proteostasis based on the accumulation of SDS-insoluble proteins during normal aging in C. elegans, utilizing mass spectrometry to identify specific insoluble proteins. We hypothesize that this accumulation of dysfunctional protein is a result of failure or decline in capacity of specific nodes in the proteostatic network. Comparison of multiple distinct proteome-wide insoluble protein datasets yielded several hundred proteins which reproducibly appear in the insoluble fraction of old (aged to adult day 7 or greater) C. elegans. Analysis of these age-related insoluble proteins revealed significant enrichment for proteins involved in metabolism, protein folding, and translation. We have created transgenic animals expressing GFP tagged proteins from this set of reproducible age-related insoluble proteins, and are using these strains to investigate the drivers of proteostasis decline with age.