HSP104 Saccharomyces
Description
Product Specs
Product Science Overview
Heat Shock Protein 104 (HSP104) is a molecular chaperone found in the budding yeast Saccharomyces cerevisiae. It plays a crucial role in stress tolerance and protein homeostasis by assisting in the refolding and disaggregation of denatured proteins. This protein is particularly significant in the context of recombinant protein production, where it is often expressed in Escherichia coli for research and industrial applications.
HSP104 is a large protein with a molecular weight of approximately 102 kDa, consisting of 908 amino acids . It belongs to the Clp/Hsp100 family of ATPases associated with various cellular activities. The protein operates as a hexamer, forming a ring-like structure that facilitates its chaperone activity.
The primary function of HSP104 is to disaggregate and refold misfolded proteins, thereby preventing the accumulation of toxic protein aggregates. This activity is vital for cell survival under stress conditions such as high temperatures and high ethanol concentrations . Unlike other heat shock proteins, HSP104 does not protect proteins from denaturation but rather helps in the recovery of proteins that have already been denatured .
Recombinant HSP104 is typically produced in E. coli expression systems. The gene encoding HSP104 is cloned into an expression vector, which is then introduced into E. coli cells. The protein is expressed and subsequently purified using conventional column chromatography techniques to achieve high purity levels (>90% by SDS-PAGE) .
HSP104 is essential for the maintenance of [psi(+)] prions in S. cerevisiae, a phenomenon that has been extensively studied to understand prion biology and protein aggregation . The protein’s ability to disaggregate and refold proteins makes it a valuable tool in biotechnology and medicine, particularly in the development of therapies for protein misfolding diseases.
- Research: HSP104 is used as a model to study protein folding and aggregation mechanisms. Its role in prion maintenance provides insights into similar processes in higher organisms.
- Biotechnology: The protein’s chaperone activity is harnessed in various industrial processes to improve the yield and stability of recombinant proteins.
- Medicine: Understanding HSP104’s function can aid in developing treatments for diseases caused by protein misfolding and aggregation, such as Alzheimer’s and Parkinson’s diseases.
