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 affinity 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. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release (PubMed:26865365).

Heat shock 70 kDa protein 6 (Heat shock 70 kDa protein B'') (Heat shock protein family A member 6)
HSPA6 HSP70B'' heat shock 70kDa protein 6 (HSP70B''); heat shock 70kD protein 6 (HSP70B'')

P17066

Human

WB,IF,ICC,FC

WB 1:500-2000
IF 1:100
ICC 1:100-1:400
FC 1:100

70.8 kDa

Mouse

Full length human recombinant protein of human HSPA6 (NP_002146) produced in HEK293T cell.

Monoclonal

Purified from mouse ascites fluids or tissue culture supernatant by affinity chromatography (protein A/G)

PBS (pH 7.3) containing 1% BSA, 50% glycerol and 0.02% sodium azide.

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