Heat Shock Protein Resources
 The family of heat shock proteins was initially characterized as a highly conserved battery of genes whose expression could be induced by heat shock. 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.
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.
Product Listings
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Online Reference Tools
- Cell Stress Society International
- Heat Shock Protein Gene Table
- Includes links to Entrez & SwissProt entries, and related products
- Tutorial: Heat Shock Proteins and the Stress Response
- The Hsp basics in a 45 minute narrated slide show
- Citation Database
- Find citations for Assay Designs™ and Stressgen® products
- Heat Shock Research Portal
- Articles, jobs, lab registry, news, forum - updated daily
- Heat shock protein - Wikipedia, the free encyclopedia
- Heat shock proteins (HSPs) are a group of proteins whose expression is increased when the cells are exposed to elevated temperatures or other stress...
- Chaperone - Wikipedia, the free encyclopedia
- Chaperones are proteins that assist the non-covalent folding/unfolding and the assembly/disassembly of other macromolecular structures,...
- Cell Stress links
- Web links to additional cell stress resources sponsored by Cell Stress Society International.
- Molecular Chaperone Club
- Club website that focuses on annual meeting held in Warwich, Oxford, Cambridge, and other UK cities; publications; scientific membership.
- Hsp90 website
- A web site for the community of scientists interested in the Hsp90 molecular chaperone machine.
- Picard laboratory
- Features a table of interations for Hsp90 and related molecules.
- Chaperome.org site
- Open forum website focused on the chaperone community. Includes basic biology information on chaperones.
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New Products
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Published in the Human Protein Atlas
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Posters
Click here to request a copy of the posters below.
 
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Literature
 Reference Guide: Heat Shock Proteins and the Cellular Stress Response
This comprehensive guide to heat shock proteins (Hsps) focuses on the function of Hsps alone and in complexes as molecular chaperones. This compilation includes a comprehensive review by Dr. William J. Welch of the major Hsp families, their associated co-chaperones, and their function in the context of the cellular response to stress.
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 Heat Shock Proteins Tech Flier
Not all recombinant proteins are created equal. Stressgen brand recombinant human and bacterial Hsp40 (DnaJ) and Hsp70 (DnaK) proteins have been shown to retain ATPase activity, and are suitable for use in luciferase folding assays. Lot-to-lot consistency ensures you get reproducible results over time. Download the technical bulletin to learn mor. Download PDF
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The family of heat shock proteins was initially characterized as a highly conserved battery of genes whose expression could be induced by heat shock. 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.
