HSPA1B (HRP)

Recombinant protein corresponding to aa418-641 from human heat shock 70kD protein 1B protein.

Suitable for use in ELISA. Other applications not tested.

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. 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. The co-chaperones are of three types.

IgG

Polyclonal

Purified by Protein G affinity chromatography.

Suitable for use in ELISA. Other applications not tested.

Optimal dilutions to be determined by the researcher.

Rabbit

Hu

Recognizes human HSPA1B.

Heat shock 70kD protein 1B (Heat shock 70kD protein 2) (HSP70-2) (HSP70.2), HSPA1B, HSP72

P0DMV9