Recombinant Human HSP70 (E110D)

Background: HSP70 is a central molecular chaperone that maintains cellular proteostasis by regulating protein folding, stabilization, trafficking, and degradation. Within the ubiquitin–proteasome system (UPS), HSP70 cooperates with co-chaperones such as HSP40 and interacts directly with E3 ubiquitin ligases including CHIP (C-terminus of HSC70-Interacting Protein) to facilitate the ubiquitylation and proteasomal degradation of misfolded or damaged proteins. These chaperone–E3 ligase complexes play a critical role in substrate triage, determining whether client proteins are refolded or targeted for degradation. HSP70 has also emerged as an important modulator of targeted protein degradation (TPD), influencing degrader-induced substrate engagement, ubiquitin transfer, and proteasome processing efficiency. This product contains the naturally occurring E110D variant within the N-terminal nucleotide-binding domain of HSP70. Due to its central role in protein quality control and stress-response pathways, HSP70 is widely studied in cancer, neurodegeneration, and other diseases associated with disrupted proteostasis.