Hsp90a Active human

recombinant, expressed in E. coli, ≥80% (SDS-PAGE)

HSP86, NY-REN-38 (renal carcinoma antigen), HSPCAL3, LAP2, Heat shock protein 90 kDa α
En este momento no podemos mostrarle ni los precios ni la disponibilidad

biological source



expressed in E. coli


≥80% (SDS-PAGE)


aqueous solution


≥8 nM

mol wt

85.5 kDa


pkg of 200 μg

storage condition

avoid repeated freeze/thaw cycles


>0.02 mg/mL

NCBI accession no.

UniProt accession no.

shipped in

dry ice

storage temp.


Gene Information

human ... HSP90AA2(3324)

General description

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


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

Biochem/physiol Actions

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).

Physical form

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

Preparation Note

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.
Certificado de Análisis
Bo Qiao et al.
BMC proceedings, 3 Suppl 7, S132-S132 (2009-12-19)
The genes PTPN22 and HLA-DRB1 have been found by a number of studies to confer an increased risk for rheumatoid arthritis (RA), which indicates that both genes play an important role in RA etiology. It is believed that they not...
Functional proteomic screens reveal an essential extracellular role for hsp90 alpha in cancer cell invasiveness.
Eustace BK, et al.
Nature Cell Biology, 6(6), 507-514 (2004)
Secretion of extracellular hsp90alpha via exosomes increases cancer cell motility: a role for plasminogen activation.
McCready J, et al.
BMC Cancer, 10:294 (2010)
The regulatory mechanism of Hsp90alpha secretion and its function in tumor malignancy.
Wang X, et al.
Proceedings of the National Academy of Sciences of the USA, 106(50), 21288-21293 (2009)
Transforming growth factor alpha (TGFalpha)-stimulated secretion of HSP90alpha: using the receptor LRP-1/CD91 to promote human skin cell migration against a TGFbeta-rich environment during wound healing.
Cheng CF, et al.
Molecular and Cellular Biology, 28(10), 3344-3358 (2008)

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