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.
Product Name:
HSP70
>Also Known As:
HSPA1A; HSP72; HSPA1; HSP70I; HSP70-1; HSP70-1A
>Catalog No.:
K1300
>Size:
25 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 Datasheet， MSDS
>NCBI RefSeq:
NM_005345
>Image(s):
N/A
>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 PSI-7977 18474941
