Heat Shock Protein 70, human recombinant

A chaperone protein that assists protein folding
Catalog #: 4859 | abID:

Product Details

Alternate Name Human Heat Shock Protein 70, Heat Shock Protein 70
Gene Symbol HSPA1A/1B
Gene ID 3303
Accession # P08107
Source E. coli
Appearance Lyophilized protein
Physical Form Description Lyophilized from 41 mM Tris, pH 8 containing 81 mM NaCl.
Molecular Weight 70.0 kDa
Purity by SDS-PAGE ≥98%
Purity by ≥98%
Endotoxin Level <0.1 ng/μg
Reconstitution Instructions Reconstitute in H₂O (solubility > 40 mg/ml), aliquot and store at -80 °C
Handling Centrifuge the vial prior to opening.
Storage Conditions -20°C
Shipping Conditions Gel Pack
USAGE For Research Use Only! Not to be used in humans

Details

HSP70 and HSP90 are molecular chaperones expressed constitutively under normal conditions to maintain protein homeostasis and are induced upon environmental stress. Both HSP70 and HSP90 are able to interact with unfolded proteins to prevent irreversible aggregation and catalyze the refolding of their substrates in an ATP- and co-chaperone-dependent manner. HSP70 has a broad range of substrates including newly synthesized and denatured proteins, while HSP90 tends to have a more limited subset of substrates, most of which are signaling molecules. HSP70 and HSP90 often function collaboratively in a multi-chaperone system, which requires a minimal set of co-chaperones: HSP40, Hop, and p23. The co-chaperones either regulate the intrinsic ATPase activity of the chaperones or recruit chaperones to specific substrates or subcellular compartments. When the ubiquitin ligase CHIP associates with the HSP70/HSP90 complex as a cofactor, the unfolded substrates are subjected to degradation by the proteasome. The biological functions of HSP70/HSP90 extend beyond their chaperone activity. They are essential for the maturation and inactivation of nuclear hormones and other signaling molecules. They also play a role in vesicle formation and protein trafficking.


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Jeffrey A. Mosenson et al.  Mutant HSP70 Reverses Autoimmune Depigmentation in Vitiligo. Science Translational Medicine, Feb 2013; 5: 174ra28.
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