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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

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

~90 kDa

species reactivity

human, mouse, rat

packaging

antibody small pack of 25 μL

concentration

~1 mg/mL

technique(s)

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

UniProt accession no.

P07900

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

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

Categorías relacionadas

General description

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.

Specificity

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

Immunogen

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.

Biochem/physiol Actions

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.

Physical form

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

Storage and Stability

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.

Disclaimer

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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Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «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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