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 co-chaperones have been shown to not only regulate different steps of the ATPase cycle, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation.

Heat shock 70 kDa protein 1A (Heat shock 70 kDa protein 1) (HSP70-1) (HSP70.1) (Heat shock protein family A member 1A)HSPA1A HSP72 HSPA1 HSX70

Human, Mouse, Rat;

WB,IP

WB 1:2000-1:5000； IHC/IF 1:50-1:500

70 kDa

HSPA1A HSP72 HSPA1 HSX70

P0DMV8

https://www.uniprot.org/uniprotkb/p0dmv8

Mouse

Monoclonal

Mouse IgG

HSP70 Antibody detects endogenous levels of total HSP70.

PBS, pH 7.4, 40% glycerol, and 0.01% sodium azide.

Store at -20 °C. Stable for 12 months from date of receipt.Store at -20°C long term.