Anti-Hsp70/Hsc70 Antibody

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. {UniProtKB:P0DMV8}.

Immunoblotting: use at 1ug/mL. <br><br>Immunohistochemistry: use at 1-5ug/mL. <br><br>These are recommended concentrations. <br><br>Endusers should determine optimal concentrations for their applications.

This antibody detects 72 and 73kDa proteins corresponding to the predicted molecular masses of Hsp70 and Hsc70, respectively, on immunoblots of human, mouse, rat, rabbit, monkey, hamster, guinea pig, dog, bovine, sheep, pig, chicken yeast, fish, and Xenopus samples. This antibody recognizes the inducible and constitutive forms of Hsp70 and does not cross-react with Hsp90.

Members of the Hsp70 family are molecular chaperones that function in protein folding, transport, maturation and degradation by binding to nascent polypeptide chains as well as partially folded protein intermediates and preventing their aggregation and misfolding. The 70kDa heat shock cognate protein, Hsc70, is closely related biochemically and biologically to Hsp70.