HSP70 (Heat shock protein) is an HSP that's expressed in response to biological stressors, such as high temperatures. HSP70 is one of the major HSP families. HSP90, HSP100 and HSP90 are also included. HSP70 is a family of highly conserved proteins which are inducible by various biological stresses including heat stress in all organisms that have been studied.
HSP70 is a protein that is highly inducible in all species, but is also constitutively present in primate cells. HSP72 is a 72kDa protein that can be induced only under stress conditions. HSC70 is a 72kDa constitutively expressed protein that is involved in uncoating clathrin coated vessels. You can know more about a Hsp70/HSPA1A/HSPA1B antibody online.
GRP78 or BiP is a glucose-regulated 78kDa protein located in the endoplasmic retina. HSP75 is a protein that can be found in the mitochondria. HSP70, encoded by an intronless genome, is responsible for stabilizing existing proteins against aggregation, and mediating the folding of newly-translated proteins in the cell and organelles.
Through interaction with the AU rich element RNA binding protein 1, HSP70 is involved in the ubiquitin–proteasome pathway. The HSP70 gene can be found in the major histocompatibility complexity class III region. It is in a cluster that includes two genes closely related, which encode similar proteins.
The Hsp70 proteins form a central component of the cellular network molecular chaperones/folding catalysts. Transient association of the substrate binding domain of Hsp70 proteins with short hydrophobic segments of peptide within their substrate proteins allows them to assist in a wide range of protein folding processes.