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SAB4200812

Sigma-Aldrich

Anti-HSP90 antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Sinônimo(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

Código UNSPSC:
12352203
NACRES:
NA.41

fonte biológica

rabbit

forma do anticorpo

affinity isolated antibody

tipo de produto de anticorpo

primary antibodies

clone

polyclonal

forma

buffered aqueous solution

peso molecular

~90 kDa

reatividade de espécies

human, mouse, rat

embalagem

antibody small pack of 25 μL

concentração

~1 mg/mL

técnica(s)

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

nº de adesão UniProt

P07900

Condições de expedição

dry ice

temperatura de armazenamento

−20°C

modificação pós-traducional do alvo

unmodified

Informações sobre genes

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

Categorias relacionadas

Descrição geral

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.

Especificidade

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

Imunogênio

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

Aplicação

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.

Ações bioquímicas/fisiológicas

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.

forma física

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

Armazenamento e estabilidade

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.

Exoneração de responsabilidade

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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Código de classe de armazenamento

10 - Combustible liquids

Classe de risco de água (WGK)

WGK 1

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Certificados de análise (COA)

Busque Certificados de análise (COA) digitando o Número do Lote do produto. Os números de lote e remessa podem ser encontrados no rótulo de um produto após a palavra “Lot” ou “Batch”.

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Faruk Tas et al.
Asian Pacific journal of cancer prevention : APJCP, 18(3), 599-601 (2017-04-26)
Background: Cellular heat shock proteins (HSPs) play significant roles in sustaining normal cellular conditions. The stimulated expressions of HSPs result in cellular stabilization at times of stress, such as cancer. The objective of this study was to determine the clinical
Heat Shock Proteins: A Review of the Molecular Chaperones for Plant Immunity
Park CJ, et al.
The plant pathology journal, 31, 323-323 (2015)
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)
Luke Whitesell et al.
Nature reviews. Cancer, 5(10), 761-772 (2005-09-22)
Standing watch over the proteome, molecular chaperones are an ancient and evolutionarily conserved class of proteins that guide the normal folding, intracellular disposition and proteolytic turnover of many of the key regulators of cell growth, differentiation and survival. This essential
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

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