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SAB4200812

Sigma-Aldrich

Anti-HSP90 antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Synonyme(s) :

(LAP-2), HSP86, Heat shock 86 kDa, Heat shock protein HSP 90-alpha, LPS-associated protein 2, Lipopolysaccharide-associated protein 2, Renal carcinoma antigen NY-REN-38

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

~90 kDa

Espèces réactives

human, mouse, rat

Conditionnement

antibody small pack of 25 μL

Concentration

~1 mg/mL

Technique(s)

immunoblotting: 1:125-1:250 using different cells extract

Numéro d'accès UniProt

P07900

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... HSP90AA1(3320)
mouse ... HSP90AA1(15519)
rat ... HSP90AA1(299331)

Catégories apparentées

Description générale

Heat shock proteins 90 (HSP90) subunits α and β, also known as HSP90AA1 and HSP90AB1 respectively, belong to the heat shock proteins (HSPC) family of highly conserved chaperones proteins, which are classified according to their cellular localization and their expression pattern. These stress inducible proteins, which includes Hsp20, Hsp60, Hsp70, and Hsp90 are molecular chaperones that bind other proteins assisting their correct folding. Hsp90 is dispensable in bacteria but is essential, conserved and highly abundant in eukaryotes, even under nonstress conditions.

Spécificité

Anti-HSP90 antibody specifically recognizes human, mouse and rat HSP90.

Immunogène

Synthetic peptide corresponding to the C-terminal region of human HSP90, conjugated to KLH

Application

Anti-HSP90 antibody produced in rabbit has been used in various immunochemical techniques including immunoblotting (~90 kDa). Detection of the HSP90 band by Immunoblotting is specifically inhibited by the immunogen.

Actions biochimiques/physiologiques

The heat shock proteins 90 (Hsp90) proteins facilitates various essential physiological processes such as cell survival, cell cycle control, hormone signaling, and apoptosis. Upregulated expression of Hsp90 is associated with the development of various pathological conditions, including several types of cancer, viral infection, inflammation, and neurodegenerative diseases.

Forme physique

Solution in 0.01 M phosphate buffered saline pH 7.4, containing 15 mM sodium azide as a preservative.

Stockage et stabilité

For continuous use, store at 2-8°C for up to one month. For extended storage, freeze in working aliquots. Repeated freezing and thawing is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilution samples should be discarded if not used within 12 hours.

Clause de non-responsabilité

Unless otherwise stated in our catalog  our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Code de la classe de stockage

10 - 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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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

The HSP90 Family: Structure, Regulation, Function, and Implications in Health and Disease
Hoter A, et al.
International Journal of Molecular Sciences, 19, 9-9 (2018)
Heat Shock Proteins: A Review of the Molecular Chaperones for Plant Immunity
Park CJ, et al.
The plant pathology journal, 31, 323-323 (2015)
Vanessa Strings-Ufombah et al.
Molecular therapy. Nucleic acids, 24, 67-78 (2021-03-20)
Oculopharyngeal muscular dystrophy (OPMD) is a rare autosomal dominant disease that results from an alanine expansion in the N-terminal domain of Poly-A Binding Protein Nuclear-1 (PABPN1). We have recently demonstrated that a two-vector gene therapy strategy significantly ameliorated the pathology
Alba Orea-Soufi et al.
Cancers, 13(21) (2021-11-14)
Tribbles pseudokinase 3 (TRIB3) has been proposed to both promote and restrict cancer generation and progression. However, the precise mechanisms that determine this dual role of TRIB3 in cancer remain to be understood. In this study we aimed to investigate

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