>Heat-Shock Protein (HSP)
Heat-Shock Protein (HSP)
Sino Biological provides quality reagents: heat-shock protein (HSP) recombinant proteins, anti-HSP antibodies, ELISA kits, and ORF cDNA clones for research.
Heat-Shock Protein Products
Please click the molecular formulas to find products that you are interested.
* Being developed. Tell us your requirement so that the products of interest be placed on the priority list.
Heat-Shock Protein (HSP) Background
Heat-shock proteins are a class of proteins which are expressed at high levels when cells are exposed to a sudden temperature jump or other stress, including oxidative stress, nutritional deficiencies (e. g., glucose deprivation), infection, exposure to chemicals, UV light, etc. Heat-shock proteins are found in almost all living organisms, and several families of these proteins are highly conserved from bacteria to human cells. Heat shock proteins are named according to their molecule weight, e.g., Hsp60, Hsp70, Hsp90.
Heat shock proteins function as intracellular chaperones for other proteins. Heat shock proteins stabilize unstable proteins, prevent unwanted protein aggregation, and mediate correct folding, assembly of proteins into oligomeric structures, transport to subcellular compartments, or controlled switching between active and inactive conformational states. Heat shock proteins do not function during cellular stress but also under normal physiological conditions. They serve as monitors of the cell’s proteins. Some examples of their role as "monitors" are that they carry old proteins to the cell's "recycling bin" (proteasome) and they help newly synthesized proteins fold properly.
Heat shock proteins appear to serve a significant cardiovascular role. A substantial literature describes the induction of Hsp70 by ischemia, the potential role of Hsp70 in ischemic preconditioning, and an inverse correlation between expression of Hsp70 induced by ischemic or thermal preconditioning and infarct size in animal models. In addition to Hsp70, Hsp27 can protect primary cardiomyocytes against ischemic damage. Hsp90 binds both endothelial nitric oxide synthase and soluble guanylate cyclase which in turn are involved in vascular relaxation. Hsp20 appears significant in development of the smooth muscle phenotype during development. Hsp20 also serves a significant role in preventing platelet aggregation, cardiac myocyte function and prevention of apoptosis after ischemic injury, and skeletal muscle function and muscle insulin response.
Heat-Shock Protein (HSP) Related Studies
- Benjamin IJ, et al. (1998) Stress (heat shock) proteins: molecular chaperones in cardiovascular biology and disease. Circ Res. 83(2):117-32.
- Xiao X, et al. (1999) Stress-response proteins in cardiovascular disease. Am J Hum Genet. 64(3):685-90.
- Fan GC, et al. (2005) Novel cardioprotective role of a small heat-shock protein, Hsp20, against ischemia/reperfusion injury. Circulation. 111(14):1792-9.
- Antonova G, et al. (2007) Functional significance of hsp90 complexes with NOS and sGC in endothelial cells. Clin Hemorheol Microcirc. 37(1-2):19-35.