HSP70

HSP70 a critical chaperone protein that has a high affinity for unfolded polypeptide chains. It binds extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. In cooperation with other chaperones, Hsp70 stabilizes preexistent proteins against aggregation and mediates the folding of newly translated polypeptides in the cytosol as well as within organelles. Hsp70 and Hsp40 recruit some misfolded proteins to the ubiquitin E3 ligase CHIP for ubiquitination.

Additional Information

Product Name: HSP70
Also Known As: HSPA1A; HSP72; HSPA1; HSP70I; HSP70-1; HSP70-1A
Catalog No.: K1301
Size: 100 µg
Molecular Weight: 70 kDa
Species: Human
Source: Bacterial recombinant
Stock: 20 mM Tris, 150 mM NaCl, 2 mM βME, 10% Glycerol
Concentration: See tube label
Quality Assurance: ~90% by SDS-PAGE, see datasheet for gel image
Storage: Store at -80°C; avoid multiple freeze-thaw cycles
PDF Data Sheet: PDF DatasheetMSDS
NCBI RefSeq: NM_005345
Image(s): No
Shipping Method: Dry ice shipping
References: 1. Walerych ., et al. (2009) Oncogene 28: 4284-94
2. Daugaard M, et al. (2007) FEBS Lett. 581: 3702-3710
3. Klucken J, et al.(2006) FASEB J. 20, 2050
4. Freeman BC, et al. (1995) EMBO J 14: 2281-22-92

Details

HSP70 a critical chaperone protein that has a high affinity for unfolded polypeptide chains. It binds extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. In cooperation with other chaperones, Hsp70 stabilizes preexistent proteins against aggregation and mediates the folding of newly translated polypeptides in the cytosol as well as within organelles. Hsp70 and Hsp40 recruit some misfolded proteins to the ubiquitin E3 ligase CHIP for ubiquitination.