HSP70 Antibodies

Target Information

a critical chaperone protein of the heat shock protein 70 family. 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. It binds extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. 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 co-chaperones are of three types: J-domain co-chaperones such as HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation. Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle. Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation. 2 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB. Triptolide, a potential therapeutic agent for progression/metastasis of pancreatic cancer, causes pancreatic cancer cell death by induction of apoptosis, an effect mediated by the inhibition of HSP70. Note: This description may include information from UniProtKB.

Alternate Names

dnaK-type molecular chaperone HSP70-1; epididymis secretory protein Li 103; epididymis secretory sperm binding protein; Heat shock 70 kDa protein 1; Heat shock 70 kDa protein 1/2; Heat shock 70 kDa protein 1A; Heat shock 70 kDa protein 1A/1B; Heat shock 70 kDa protein 1B; Heat shock 70 kDa protein 2; heat shock 70kD protein 1A; heat shock 70kD protein 1A/1B; heat shock 70kDa protein 1A; heat shock 70kDa protein 1A/1B; Heat Shock Protein 70; heat shock protein family A (Hsp70) member 1A; heat shock-induced protein; HEL-S-103; HS71A; HSP70; HSP70-1; HSP70-1/HSP70-2; HSP70-1A; HSP70-2; HSP70.1; HSP70.1/HSP70.2; HSP70.2; HSP70I; HSP71; HSP72; HSPA1; HSPA1A; HSPA1B; HSX70