Molecular Chaperones / Heat Shock Proteins

HSPs [HSP90, HSP70/40, HSP60/10, GroEL/ES & more]
Heme Oxygenases
Small HSPs [Crystallin, HSP20, HSP25, HSP27 & more]
Co-Chaperones & HSP-interacting Proteins
HSF
Mitochondrial HSPs [Mortalin, Grp75]
ER Stress [ERp57, ERp72, Grp94, Calnexin, Calnexin & more]
Neurodegenerative Diseases
Clusterin
More Stress & HSPs

All Stress & HSPs

Heat Shock Protein Chaperone Complexes - Wallchart

Heat Shock Proteins & the Cellular Stress Response Catalog

HSP70/HSP40 Complexes - Technical Brief

HSP90 - Scientific Review

All new literature pieces

HSP90α (human), ELISA Kit

Most sensitive, rapid ELISA kit for highly specific, quantitative detection of human HSP90α

• Reproducible – less than 10% variation between assays
• Sensitive – detect as little as 50 pg/ml of human HSP90α
• Higher throughput – test up to 40 samples in duplicate in just 3 hours
• Quantitative – obtain precise, statistically significant results, facilitating comparison of data between multiple experiments

[pSer³²⁶]HSF1 ELISA kit

Sensitive, ELISA kit for this key transcription factor for heat shock protein (chaperone) research.

• Sensitive - measure pg/ml of HSF1 and use less precious sample compared to Western blot
• Time Saving - results from up to 40 samples in duplicate in just 3 hours
• Convenient - ready-to-use liquid color-coded reagents and pre-coated plate

The family of heat shock proteins (HSPs) was initially characterized as a highly conserved battery of genes whose expression could be induced by heat shock. HSPs play a prominent role in many of the cell’s most basic processes. Many heat shock protein family members are now known to function constitutively as molecular chaperones, stabilizing and assisting in the trafficking of nascent peptides during normal growth. Under stressful conditions such as heat shock or hypoxia, increased expression of heat shock proteins protects the cell by stabilizing unfolded or misfolded peptides, giving the cell time to repair or re-synthesize damaged proteins. Their general role as molecular chaperones, protectors of the proteome, is now central to many areas of active research including aging, neurodegeneration, signaling, immunology and cancer.

Many heat shock proteins function together in co-chaperone complexes, such as HSP70/HSP40 (bacterial DnaK/DnaJ) that along with GrpE acts as an ATP-regulated shuttle complex for newly synthesized proteins. Many of these nascent peptides are delivered to HSP90-containing complexes, which play a critical role in the stabilization and activation of key signaling kinases and hormone receptors. The HSP60/HSP10 complex (bacterial GroEL/GroES) forms an alternative protein folding mechanism in the mitochondria. Small heat shock proteins including HSP27 and the crystallins form large oligomeric complexes that function to prevent protein aggregation.