Pular para o conteúdo
Merck
Todas as fotos(1)

Documentos Principais

Visualizar Toda a Documentação

SRP5191

Sigma-Aldrich

HSP90 α, His tagged human

recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution

Sinônimo(s):

FLJ31884, HSP86, HSP90AA1, HSP90N, HSPC1, HSPCA, HSPCAL1, HSPCAL4, HSPN, Hsp89, Hsp90, LAP2

Faça loginpara ver os preços organizacionais e de contrato
Todas as fotos(1)

About This Item

Número CAS:
481150-77-0
Código UNSPSC:
12352200
NACRES:
NA.32

fonte biológica

human

recombinante

expressed in baculovirus infected Sf9 cells

Ensaio

≥70% (SDS-PAGE)

Formulário

buffered aqueous glycerol solution

peso molecular

~94 kDa

técnica(s)

cell culture | mammalian: suitable

solubilidade

water: soluble

adequação

suitable for molecular biology

nº de adesão NCBI

NM_005348

Condições de expedição

dry ice

temperatura de armazenamento

−70°C

Informações sobre genes

human ... HSP90AA1(3320)

Descrição geral

Research area: Cell cycle. The gene encoding this protein is localized on human chromosome 14q32.31.

Aplicação

HSP90 α, His tagged human has been used to measure antibodypolyspecificity by flow cytometry. It has also been used as a molecularmarker to study the effect of Temozolomide on glioblastoma cells releasedextracellular vesicles.

Ações bioquímicas/fisiológicas

Heat shock protein 90α (HSP90α) is a molecular chaperone involved in the folding, assembly-disassembly, and activation of multiple types of target proteins such as kinases, steroid hormone receptors and transcription factors. HSP90 inhibitors bind to HSP90, and induce the proteasomal degradation of HSP90 client proteins. HSP90α is an important mediator of cancer cell invasion and is expressed extracellularly on fibrosarcoma and breast cancer cells where it interacts with MMP2 (matrix metalloproteinase-2).HSP90α are important molecular chaperones involved in signal transduction, cell cycle control, stress management, folding, degradation, and transport of proteins.

forma física

Supplied in 50mM MOPS, pH 7.0, 300mM NaCl, 150mM imidazole, 0.1mM PMSF, 0.25mM DTT, 25% glycerol.

Nota de preparo

after opening, aliquot into smaller quantities and store at -70 °C. Avoid repeating handling and multiple freeze/thaw cycles

Pictogramas

Health hazardExclamation mark
GHS08,GHS07

Palavra indicadora

Danger

Frases de perigo

H315,H319,H360D

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

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Escolha uma das versões mais recentes:

Certificados de análise (COA)

Lot/Batch Number
E192-1
R279-1

Não está vendo a versão correta?

Se precisar de uma versão específica, você pode procurar um certificado específico pelo número do lote ou da remessa.

Pesquise por COA

Já possui este produto?

Encontre a documentação dos produtos que você adquiriu recentemente na biblioteca de documentos.

Visite a Biblioteca de Documentos

Secretion of extracellular hsp90alpha via exosomes increases cancer cell motility: a role for plasminogen activation.
McCready J
BMC Cancer (2010)
Role of plant heat- hock proteins and molecular chaperones in the abiotic stress response
Wang-Xia Wang
Trends in Plant Science (2004)
De novo unbalanced translocation resulting in monosomy for distal 5p (5p14.1 ? pter) and 14q (14q32.31 ? qter) associated with fetal nuchal edema, microcephaly, intrauterine growth restriction, and single umbilical artery: Prenatal diagnosis and molecular cytogenetic characterization
Chih-Ping
Taiwanese Journal of Obstetrics & Gynecology (2013)
Functional proteomic screens reveal an essential extracellular role for hsp90 alpha in cancer cell invasiveness.
Eustace BK
Nature Cell Biology (2004)
P Csermely et al.
Pharmacology & therapeutics, 79(2), 129-168 (1998-09-28)
The 90-kDa molecular chaperone family (which comprises, among other proteins, the 90-kDa heat-shock protein, hsp90 and the 94-kDa glucose-regulated protein, grp94, major molecular chaperones of the cytosol and of the endoplasmic reticulum, respectively) has become an increasingly active subject of
Exibir todos os documentos relacionados

Nossa equipe de cientistas tem experiência em todas as áreas de pesquisa, incluindo Life Sciences, ciência de materiais, síntese química, cromatografia, química analítica e muitas outras.

Entre em contato com a assistência técnica