Hsp60 Pure 24/HSP60 150ug

Heat shock proteins (Hsp) are a set of highly conserved proteins that include constitutively expressed (Hsp60, Hsp70, and Hsp90) and

stress-induced (Hsp27 and Hsp72) proteins. Hsp60 is localized to the mitochondria, where it promotes mitochondrial protein folding and

facilitates proteolytic degradation of misfolded or denatured proteins. It binds Hsp10, which regulates the substrate binding and ATPase

activity of Hsp60. In HeLa and Jurkat mitochondria, Hsp60 associates with caspase-3 to form a complex that dissociates and releases from the

mitochondria during apoptosis. In addition, Hsp60 accelerates the maturation of procaspase-3 through its ATP-dependent "foldase" activity. In

addition to its role in protein folding, Hsp60 has also been implicated in immune function. In macrophages, its binding to the toll-like

receptor-4 complex induces production of TNFα and nitric oxide and stimulation of a proinflammatory response. Thus, the protein folding

function of Hsp60 is involved in mitochondrial protein folding in both normal and apoptotic cells, while release of Hsp60 during necrosis is

thought to stimulate a proinflammatory response.

1.Since applications vary, each investigator should titrate the reagent to obtain optimal results.

2.Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.

3.This antibody has been developed and certified for the bioimaging application. However, a routine bioimaging test is not performed on every lot. Researchers are encouraged to titrate the reagent for optimal performance.