HSP70/HSP40 (human) Protein Refolding Kit

CHF 726.00
In stock
AG-44T-0115-KI011 KitCHF 726.00
 
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Product Details
Product Type Kit
Properties
Application Set Compound Screening
Crossreactivity Human
Kit Contains 30μl of 10X HSP70 Solution
30μl of 10X HSP40 Solution
50μl of 10X HSP70 Reaction Buffer
30μl of 10X Mg-ATP Solution
50μl of 10X Glow-Fold™ Substrate Protein
2ml of Luciferin Reagent

NOTE: Kit contains reagents sufficient for 15 x 20μl reactions.
Other Product Data Use: This kit provides a functional in vitro HSP70/HSP40 refolding system. Using the provided substrate protein, the kit can be used to screen for small molecules affecting the efficiency of the refolding process (such as HSP inhibitors). Alternatively, the HSP70/HSP40 complex may be used to test refolding of user-supplied proteins if a functional assay is available.
Declaration Manufactured by Boston Biochem
Shipping and Handling
Shipping DRY ICE
Short Term Storage -20°C
Long Term Storage -80°C
Handling Advice Aliquot to avoid freeze/thaw cycles.
Use/Stability Stable for at least 1 year after receipt when stored at -80°C.
Documents
Manual Download PDF
MSDS No
Product Specification Sheet
Datasheet Download PDF
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.
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