Hsp70 (encoded by three very closely related paralogs: HSPA1A, HSPA1B, and HSPA1L) is a stress-induced protein. High levels can be produced by cells in response to hyperthermia, oxidative stress, and changes in pH .

Introduction to Hsp70 Structure and Function. Heat shock protein 70 (Hsp70) is a molecular chaperone that is expressed in response to stress.

Hsp70 proteins are central components of the cellular network of molecular chaperones and folding catalysts. They assist a large variety of protein folding processes in the cell by transient association of their substrate binding domain with short hydrophobic peptide segments within their substrate proteins.

2019年6月28日 · The Hsp70 chaperones regulate protein metabolism, including folding, unfolding, subcellular localization, aggregation/disaggregation and incorporation into protein complexes.

Heat shock proteins (HSPs) are induced in response to many injuries including stroke, neurodegenerative disease, epilepsy, and trauma. The overexpression of one HSP in particular, Hsp70, serves a protective role in several different models of nervous system injury, but has also been linked to a deleterious role in some diseases.

2007年7月31日 · The human heat shock protein 70 (Hsp70) family contains at least eight homologous chaperone proteins. Endoplasmatic reticulum and mitochondria have their specific Hsp70 proteins, whereas the remaining six family members reside …

The HSP70 protein family is the best characterized and contains the largest number of members localized in many different compartments of the cell, including cytosol, mitochondria, and ER. The HSP70 is, by far, the most conserved protein in evolution.

HSP70 is a 70 kDa heat shock protein involved in folding of protein and protection of cells from stress [149, 150]. When newly synthesised protein appears from ribosome, the hydrophobic domain of protein interacts with binding site of HSP70.

Know comprehensive HSP70 protein information including protein sequence, molecular weight, theoretical pI, structure, function and protein interaction.

More recent findings suggest that chaperones also contribute to key steps in protein degradation. In particular, Hsp70 has an essential role in substrate degradation through the ubiquitin-proteasome system, as well as through different autophagy pathways.