ST13 Human
Description
ST13 human recombinant is purified by conventional chromatography techniques.
Product Specs
RRQSGAQYGS FPGGFPGGMP GNFPGGMPGM GGGMPGMAGM PGLNEILSDP EVLAAMQDPE VMVAFQDVAQ NPANMSKYQS NPKVMNLISK LSAKFGGQA.
Product Science Overview
HSP70 Interacting Protein (HIP) is a co-chaperone that plays a crucial role in the cellular stress response by interacting with the 70 kDa heat shock proteins (HSP70). HSP70 proteins are molecular chaperones that assist in the folding of nascent proteins, the refolding of misfolded or aggregated proteins, and the transport of proteins across cellular membranes. HIP enhances the function of HSP70 by stabilizing its interaction with client proteins.
HIP belongs to the family of tetratricopeptide repeat (TPR) domain-containing proteins. The TPR domain is a structural motif that mediates protein-protein interactions and is found in various proteins involved in diverse cellular processes.
HIP is characterized by its ability to bind to the C-terminal EEVD motif of HSP70 through its TPR domain. This interaction is essential for the formation of a stable HSP70-HIP complex, which is critical for the proper functioning of the HSP70 chaperone system. HIP is ubiquitously expressed in various tissues and is highly conserved across different species, indicating its fundamental role in cellular homeostasis.
The primary function of HIP is to regulate the activity of HSP70 by stabilizing its interaction with client proteins. This stabilization is crucial for the efficient folding and refolding of proteins, especially under stress conditions such as heat shock. HIP also plays a role in the degradation of misfolded proteins by targeting them to the proteasome for degradation.
HIP interacts with HSP70 through its TPR domain, which binds to the C-terminal EEVD motif of HSP70. This interaction prevents the premature release of client proteins from HSP70, thereby enhancing the chaperone’s ability to fold proteins correctly. Additionally, HIP can recruit other co-chaperones and components of the protein degradation machinery to form multi-protein complexes that facilitate the proper folding and degradation of proteins.
The expression and activity of HIP are regulated at multiple levels, including transcriptional, post-transcriptional, and post-translational modifications. Stress conditions such as heat shock can induce the upregulation of HIP, ensuring an adequate supply of co-chaperones to assist HSP70 in managing the increased load of misfolded proteins. Post-translational modifications, such as phosphorylation, can also modulate the activity of HIP, affecting its interaction with HSP70 and other co-chaperones.
