Heat Shock Proteins & Chaperones

Heat shock proteins (HSPs) are important molecular chaperones that regulate protein folding. Their name comes from their original discovery as genes and proteins that increase their expression under elevated temperatures, mediated by transcription factors known as the heat shock factors. However, HSP expression also increases due to other sources of cellular stress, including osmotic stress, oxidative stress, and the unfolded protein response, mediated by the ATF family of transcription factors. HSPs assist in the folding and maintenance of newly translated proteins, the refolding of denatured proteins, and the further unfolding of misfolded or destabilized proteins to assist in their degradation. HSP nomenclature defines families by their molecular weight: HSP90 (81 to 99 kD), HSP70 (65 to 80 kD), HSP60 (55 to 64 kD), HSP40 (35 to 54 kD), and small HSPs (<34 kD). Other chaperone cofactors (such as chaperonins, torsin family members, and prefoldin subunits) are also directly involved in protein folding. HSP expression and function can be dysregulated during pathophysiological processes such as carcinogenesis and cardiovascular disease.

QIAGEN provides a broad range of assay technologies for heat shock protein and chaperone research that enables analysis of gene expression and regulation, epigenetic modification, genotyping, and signal transduction pathway activation. Solutions optimized for heat shock protein and chaperone studies include PCR array, miRNA, siRNA, mutation analysis, pathway reporter, chromatin IP, DNA methylation, and protein expression products.