Hsp90a Active human

HSP90α (heat shock protein 90α) is an ATP-binding, ubiquitous molecular chaperone protein. This protein contains an N-terminal domain, a charged region, a middle domain, and a C-terminal domain. It is an intracellular protein present in the cytoplasm, but is also released extracellularly through exosomes. The secretion of HSP90α is controlled by the EEVD motif in the C-terminal through its interaction with tetratricopeptide repeat domain-containing proteins. The secreted form is truncated at the C-terminal.

HSP90α gene is mapped to human chromosome 11p14.1.

Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.

HSP90α (heat shock protein 90α) is involved intracellularly in the folding, assembly-disassembly and activation of multiple types of target proteins such as kinases, steroid hormone receptors and transcription factors. Extracellularly this protein is also required for neuronal and dermal fibroblast motility, and melanoma migration, invasion and metastasis. Extracellular HSP90α induces pro-invasive protein matrix metalloproteinase-2 (MMP-2), thereby promoting tumor invasiveness. This protein facilitates the migration of dermal and epidermal cells to the site of wound in a surface receptor LRP-1 (LDL receptor-related protein 1)-dependent manner, and is thus, involved in wound healing. In an early stage of the antigen processing pathway, HSP90α might function as a chaperone for precursors of pMHC I (peptide-loaded major histocompatibility I complexes).

Formulated in 25 mM Tris-HCl, pH 7.5, 400 mM NaCl, 0.05% Tween 20, 10% glycerol and 3 mM DTT.

Thaw on ice. Upon first thaw, briefly spin tube containing enzyme to recover full content of the tube. Aliquot enzyme into single use aliquots. Store remaining undiluted enzyme in aliquots at -70°C. Note: Enzyme is very sensitive to freeze/thaw cycles.