Recombinant Human Heat shock 70 kDa protein 6 (HSPA6), Truncated

Uniprot Id

P17066

Target Species

Human

Target Name

HSPA6

Target Full Name

Heat shock 70 kDa protein 6

Target Function

Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release.

Target Protein Families

Heat shock protein 70 family

Target Research Area

Cancer

Target Synonyms

Heat shock 70 kDa protein 6; Heat shock 70 kDa protein B'; Heat shock 70 kDa protein B''; heat shock 70kD protein 6 (HSP70B'); Heat shock 70kDa protein 6; HSP70B'; HSP70B-Prime; HSP76_HUMAN; HSPA6; OTTHUMP00000032372

Target Background

Enables enzyme binding activity; heat shock protein binding activity; and unfolded protein binding activity. Involved in cellular response to heat and protein refolding. Located in centriole and cytosol. Colocalizes with COP9 signalosome.