K-290

Material Data Sheet

HSP70/HSP40 Glow-Fold Protein Refolding Kit

Price: $475.00
Catalog #: K-290

HSP70/HSP40 Glow-Fold Protein Refolding Kit

Price: 
$475
Quantity: 
1 Kit
Data Sheet: 

Heat shock proteins (HSPs) are a family of highly conserved stress response proteins.  Heat shock proteins function primarily as molecular chaperones by facilitating the folding of other cellular proteins, preventing protein aggregation or targeting improperly folded proteins to specific degradative pathways.  HSP70 function depends on its cycling between two states: ATP-bound and ADP-bound.  ATP-bound HSP70 recognizes stretches of hydrophobic amino acid residues in misfolded or newly synthesized proteins and interacts with them.  This initial binding event is relatively weak and reversible, and so the ATP-bound HSP70 freely binds and release peptides.  However, the presence of a peptide in the binding domain weakly stimulates the latent ATPase activity of HSP70.  Once ATP is hydrolyzed to ADP, the binding pocket of HSP70 is reconfigured into a tight-binding state that clamps down on protein targets and helps to prevent their aggregation.  ATP hydrolysis is stimulated by HSP70 association with “J-domain” class co-chaperones such as HSP40.  These co-chaperones dramatically increase the activity and the functionality of HSP70 in the presence of interacting peptides/proteins.  Eventually ADP is exchanged for an ATP molecule, thus bringing the substrate-binding domain back to its low affinity state.  This releases the bound protein so that it may fold correctly by itself, interact with other chaperone systems to complete folding, or bind again to HSP70.

Literature

References: 

Hartl F.U. & Hayer-Hartl M. (2009)  Nat. Struc. Mol. Biol.  16: 574-581Kampinga H. H. & Craig E.A. (2010)   Nat. Rev. Mol. Cell Biol.  11:  579-592