Heat Shock Protein 70

E0522Ra

Sandwich

48T,96T

0.01ng/ml

0.05-15ng/ml

Serum, plasma, cell culture supernates

Rat

2-8ºC

1h 30m

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. 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. Plays a role in spermatogenesis. In association with SHCBP1L may participate in the maintenance of spindle integrity during meiosis in male germ cells.

69,642

60460

Heat shock protein 70.2;Heat shock-related 70 kDa protein 2;HSPA 2;HSPA2;HST;Testis-specific heat shock protein-related

HSPA2

Signal Transduction

HSPA2