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SAB4200812

Sigma-Aldrich

Anti-HSP90 antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Sinónimos:

(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

origen biológico

rabbit

forma del anticuerpo

affinity isolated antibody

tipo de anticuerpo

primary antibodies

clon

polyclonal

Formulario

buffered aqueous solution

mol peso

~90 kDa

reactividad de especies

human, mouse, rat

envase

antibody small pack of 25 μL

concentración

~1 mg/mL

técnicas

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

Nº de acceso UniProt

P07900

Condiciones de envío

dry ice

temp. de almacenamiento

−20°C

modificación del objetivo postraduccional

unmodified

Información sobre el gen

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

Categorías relacionadas

Descripción general

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.

Especificidad

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

Inmunógeno

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

Aplicación

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.

Acciones bioquímicas o 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.

Almacenamiento y estabilidad

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.

Cláusula de descargo de responsabilidad

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 clase de almacenamiento

10 - Combustible liquids

Clase de riesgo para el agua (WGK)

WGK 1

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

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Certificados de análisis (COA)

Lot/Batch Number
039M4884V
51180306

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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
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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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