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SRP0182

Sigma-Aldrich

Hsp90a Active human

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

Sinônimo(s):

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

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200 μG
R$ 2.681,00

R$ 2.681,00


Previsão de entrega em18 de abril de 2025


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200 μG
R$ 2.681,00

About This Item

Código UNSPSC:
12352200
NACRES:
NA.32

R$ 2.681,00


Previsão de entrega em18 de abril de 2025


Solicite uma grande encomenda

fonte biológica

human

recombinante

expressed in E. coli

Ensaio

≥80% (SDS-PAGE)

Formulário

aqueous solution

potência

≥8 nM

peso molecular

85.5 kDa

embalagem

pkg of 200 μg

condição de armazenamento

avoid repeated freeze/thaw cycles

concentração

>0.02 mg/mL

nº de adesão NCBI

nº de adesão UniProt

Condições de expedição

dry ice

temperatura de armazenamento

−70°C

Informações sobre genes

human ... HSP90AA2(3324)

Descrição geral

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.[1][2][3]
HSP90α gene is mapped to human chromosome 11p14.1.[4]

Aplicação

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

Ações bioquímicas/fisiológicas

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.[1] Extracellular HSP90α induces pro-invasive protein matrix metalloproteinase-2 (MMP-2), thereby promoting tumor invasiveness.[1][5] 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.[2] 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).[6]

forma física

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

Nota de preparo

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.

Pictogramas

Health hazardExclamation mark

Palavra indicadora

Danger

Frases de perigo

Classificações de perigo

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

Código de classe de armazenamento

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

Classe de risco de água (WGK)

WGK 1


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

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