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Documentos Principais

SRP4858

Sigma-Aldrich

Heat Shock Protein 90 human

recombinant, expressed in baculovirus infected Sf9 cells, ≥99% (SDS-PAGE)

Sinônimo(s):

HSP86, HSPC1, HSPCA, HSPN, Hsp89, LAP2

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About This Item

Número MDL:
MFCD02253027
Código UNSPSC:
12352200
NACRES:
NA.32

fonte biológica

human

recombinante

expressed in baculovirus infected Sf9 cells

Ensaio

≥99% (SDS-PAGE)

Formulário

liquid

peso molecular

~90 kDa

embalagem

pkg of 25 μg

condição de armazenamento

avoid repeated freeze/thaw cycles

Impurezas

endotoxin, tested

nº de adesão NCBI

P08238

nº de adesão UniProt

P14625

Condições de expedição

dry ice

temperatura de armazenamento

−70°C

Informações sobre genes

human ... HSP90B1(7184)

Descrição geral

Heat shock protein 90 (HSP90) is a molecular chaperone and one of the most abundant proteins in unstressed cells.[1] In mammalian cells, there are two genes encoding cytosolic Hsp90 homologues, with the human Hsp90α showing 85% sequence identity to Hsp90β. The recombinant Hsp90 produced from Sf9 cells represents the full length (a.a. 1-723) of Hsp90β subunit.

Ações bioquímicas/fisiológicas

Heat shock protein 90kDa beta member 1 (HSP90B1) is activated during apoptosis. It is associated with the endoplasmic reticulum membrane and undergoes specific proteolytic cleavage leading to the activation of the caspase CPP32 and initiation of DNA fragmentation. The protein protects cells against flux in Ca2+ homeostasis, which would otherwise result in cell death. It maintains the chromosomal stability in mammalian cells by associating with FAC. HSP90B1 chaperones toll-like receptors (TLRs) and thus optimizes the B cell functioning. These proteins are also the main downstream chaperones which mediate the ER unfolded protein response (UPR), which is very essential for maintaining protein homeostasis in the ER.[1][2][3]

forma física

Protein is provided in a solution of 40 mM HEPES/KOH, pH 7.5, containing 400 mM potassium chloride and 5% glycerol.

Nota de preparo

Centrifuge the vial prior to opening. Avoid freeze-thaw cycles

Código de classe de armazenamento

12 - Non Combustible Liquids

Classe de risco de água (WGK)

WGK 1

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

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Certificados de análise (COA)

Lot/Batch Number
61158
60958
51058

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T Hoshino et al.
Blood, 91(11), 4379-4386 (1998-05-30)
The FAC protein encoded by the gene defective in Fanconi anemia (FA) complementation group C binds to at least three ubiquitous cytoplasmic proteins in vitro. We used here the complete coding sequence of FAC in a yeast two-hybrid screen to
Bei Liu et al.
Blood, 112(4), 1223-1230 (2008-05-30)
Endoplasmic reticulum (ER) unfolded protein response (UPR) plays pivotal roles in both early B-cell development and plasma cell differentiation. As a major ER chaperone to mediate the UPR and a master chaperone for Toll-like receptors (TLRs), HSP90b1 (grp94, gp96) has
R K Reddy et al.
The Journal of biological chemistry, 274(40), 28476-28483 (1999-09-25)
GRP94 is a 94-kDa chaperone glycoprotein with Ca(2+)-binding properties. We report here that during apoptosis induced by the topoisomerase II inhibitor etoposide, a fraction of GRP94 associated with the endoplasmic reticulum membrane undergoes specific proteolytic cleavage, coinciding with the activation

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