Hsp70

Hsp70 (70 kDa heat shock protein) is a molecular chaperone that is involved in protein folding and the protection of proteins from damage during stress. The expression of Hsp70 is increased under conditions of thermal stress or in the presence of toxic chemicals.

Products
Background
Literature
Gene Data

Inhibitors

Cat No Product Name / Activity
2653 Pifithrin-μ
Inhibitor of p53-mitochondrial binding; also inhibits Hsp70 activity
3803 VER 155008
Hsp70 inhibitor

Other

Cat No Product Name / Activity
5375 BIX
BiP (Hsp70-5) ER chaperone inducer
5480 KRIBB11
HSF1 inhibitor
4621 MKT 077
Binds mot-2; selectively cytotoxic in cancer cells
4734 TRC 051384
Inducer of heat shock protein Hsp70

Related Targets

Hsp70 (70 kDa heat shock protein) is a molecular chaperone that is involved in protein folding and the protection of proteins from damage during stress. The expression of Hsp70 is increased under conditions of thermal stress or in the presence of toxic chemicals such as heavy metals.

Hsp70 binds in an ATP-dependent manner to sequences of hydrophobic residues. These can be on nascent polypeptide chains emerging from the ribosome, or exposed on other proteins by stress conditions. Binding by Hsp70 promotes folding of newly synthesized or mis-folded proteins to their native state. Hsp70 also prevents non-native protein aggregation by binding along with co-chaperones of the J-domain protein (JDP) family to hydrophobic residues of substrate molecules shielding them from other intermolecular attractions.

Hsp70 interacts with numerous eukaryotic regulatory proteins including nuclear receptors, kinases (e.g. Raf-1) and transcription factors. Hsp70 also acts in concert with other chaperones (e.g. Hsp90) and is regulated by a number of co-chaperones/accessory proteins (e.g. p23, Cdc37).

Hsp70 also interacts with key regulatory proteins ('clients') of signal transduction pathways for the control of cell homeostasis, proliferation, differentiation and cell death. For example, Hsp70 is involved in the caspase pathway and acts as a general antiapoptotic agent (such as Bcl-2) that inhibits heat shock-induced apoptosis. Hsp70 prevents the activation of caspase-3, PARP cleavage, DNA laddering and therefore apoptotic cell death- but has no effect on cytochrome c release.

Hsp70 family members include the constitutively expressed chaperone Hsc70, which facilitates protein folding and GRP-78 (78kDa glucose-regulated protein) involved in the transportation of proteins to the endoplasmic reticulum.

Literature for Hsp70

Cancer

Cancer Research Product Guide

A collection of over 750 products for cancer research, the guide includes research tools for the study of:

  • Cancer Metabolism
  • Epigenetics in Cancer
  • Receptor Signaling
  • Cell Cycle and DNA Damage Repair
  • Angiogenesis
  • Invasion and Metastasis
Neurodegeneration

Neurodegeneration Product Guide

A collection of over 275 products for neurodegeneration research, the guide includes research tools for the study of:

  • Alzheimer's disease
  • Parkinson's disease
  • Huntington's disease

Hsp70 Gene Data

Gene Species Gene Symbol Gene Accession No. Protein Accession No.
Heat shock 70kDa protein 1A Human HSPA1A NM_005345 P08107
Mouse Hspa1a NM_010749 Q69616
Rat Hspa1a NM_212504 Q6LA95
Heat shock 70kDa protein 1B Human HSPA1B NM_005346 P08107
Mouse Hspa1b NM_010478 P17879
Rat Hspa1b NM_31971 Q07439
Heat shock 70kDa protein 1-like Human HSPA1L NM_005527 P34931
Mouse Hspa1l NM_013558 P16627
Rat Hspa1l NM_212546 P55063
Heat shock 70kDa protein 5 Human HSPA5 NM_005347 P11021
Mouse Hspa5 NM_022310 P20029
Rat Hspa5 NM_013083 P06761
Heat shock 70kDa protein 8 Human HSPA8 NM_006597 P11142
Mouse Hspa8 NM_031165 P63017
Rat Hspa8 NM_024351 P63018