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SRP4858

Sigma-Aldrich

Heat Shock Protein 90 human

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

Synonyme(s) :

HSP86, HSPC1, HSPCA, HSPN, Hsp89, LAP2

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About This Item

Numéro MDL:
MFCD02253027
Code UNSPSC :
12352200
Nomenclature NACRES :
NA.32

Source biologique

human

Produit recombinant

expressed in baculovirus infected Sf9 cells

Pureté

≥99% (SDS-PAGE)

Forme

liquid

Poids mol.

~90 kDa

Conditionnement

pkg of 25 μg

Conditions de stockage

avoid repeated freeze/thaw cycles

Impuretés

endotoxin, tested

Numéro d'accès NCBI

P08238

Numéro d'accès UniProt

P14625

Conditions d'expédition

dry ice

Température de stockage

−70°C

Informations sur le gène

human ... HSP90B1(7184)

Description générale

Heat shock protein 90 (HSP90) is a molecular chaperone and one of the most abundant proteins in unstressed cells. 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.

Actions biochimiques/physiologiques

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.

Forme physique

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

Notes préparatoires

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

Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

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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