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Key Documents

SRP0182

Sigma-Aldrich

Hsp90a Active human

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

Sinonimo/i:

HSP86, HSPCAL3, Heat shock protein 90 kDa α, LAP2, NY-REN-38 (renal carcinoma antigen)

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About This Item

Codice UNSPSC:
12352200
NACRES:
NA.32

Origine biologica

human

Ricombinante

expressed in E. coli

Saggio

≥80% (SDS-PAGE)

Forma fisica

aqueous solution

Potenza

≥8 nM

PM

85.5 kDa

Confezionamento

pkg of 200 μg

Condizioni di stoccaggio

avoid repeated freeze/thaw cycles

Concentrazione

>0.02 mg/mL

N° accesso NCBI

N° accesso UniProt

Condizioni di spedizione

dry ice

Temperatura di conservazione

−70°C

Informazioni sul gene

human ... HSP90AA2(3324)

Descrizione generale

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.

Applicazioni

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

Azioni biochim/fisiol

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).

Stato fisico

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

Nota sulla preparazione

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.

Pittogrammi

Health hazardExclamation mark

Avvertenze

Danger

Indicazioni di pericolo

Classi di pericolo

Eye Irrit. 2 - Repr. 1B - Skin Irrit. 2

Codice della classe di stoccaggio

6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects

Classe di pericolosità dell'acqua (WGK)

WGK 1


Certificati d'analisi (COA)

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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)
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)
Hsp90alpha chaperones large C-terminally extended proteolytic intermediates in the MHC class I antigen processing pathway.
Kunisawa J and Shastri N.
Immunity, 24(5), 523-534 (2006)
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
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)

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