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Key Documents

SRP0182

Sigma-Aldrich

Hsp90a Active human

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

Synonyme(s) :

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

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About This Item

Code UNSPSC :
12352200
Nomenclature NACRES :
NA.32

Source biologique

human

Produit recombinant

expressed in E. coli

Pureté

≥80% (SDS-PAGE)

Forme

aqueous solution

Puissance

≥8 nM

Poids mol.

85.5 kDa

Conditionnement

pkg of 200 μg

Conditions de stockage

avoid repeated freeze/thaw cycles

Concentration

>0.02 mg/mL

Numéro d'accès NCBI

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−70°C

Informations sur le gène

human ... HSP90AA2(3324)

Description générale

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.

Application

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

Actions biochimiques/physiologiques

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).

Forme physique

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

Notes préparatoires

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.

Pictogrammes

Health hazardExclamation mark

Mention d'avertissement

Danger

Mentions de danger

Classification des risques

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

Code de la classe de stockage

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

Classe de danger pour l'eau (WGK)

WGK 1


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Secretion of extracellular hsp90alpha via exosomes increases cancer cell motility: a role for plasminogen activation.
McCready J, et al.
BMC Cancer, 10:294 (2010)
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)
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)
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)

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