Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, chaperone-mediated autophagy, 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 of HSP70 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. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. Substrate recognition component in chaperone-mediated autophagy (CMA), a selective protein degradation process that mediates degradation of proteins with a -KFERQ motif: HSPA8/HSC70 specifically recognizes and binds cytosolic proteins bearing a -KFERQ motif and promotes their recruitment to the surface of the lysosome where they bind to lysosomal protein LAMP2. KFERQ motif-containing proteins are eventually transported into the lysosomal lumen where they are degraded (By similarity). May play a role in uncoating of clathrin-coated vesicles (By similarity).

Q90473

Heat shock cognate 71 kDa protein, Heat shock 70 kDa protein 8, hspa8, hsc70

Human,Mouse,Zebrafish

WB

WB 1:2000

71 kD

Rabbit

polyclonal

Rabbit IgG

This antibody is purified by peptide affinity purification.

PBS (pH7.4) with 0.09% (W/V) sodium azide.

Store at -20°C. Stable for 12 months from date of receipt.Do not aliquot the antibody.Avoid freeze / thaw cycle.