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Key Documents

AB3468

Sigma-Aldrich

Anti-Heat Shock Protein 90β Antibody

Chemicon®, from rabbit

Synonym(s):

HSP84

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

rabbit

Quality Level

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

polyclonal

species reactivity

human, rat, mouse

manufacturer/tradename

Chemicon®

technique(s)

immunocytochemistry: suitable
immunohistochemistry: suitable (paraffin)
immunoprecipitation (IP): suitable
western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

Specificity

Reacts with a protein of 84 kD identified as heat shock protein 90beta (HSP90beta). No reactivity with HSP90alpha/HSP86.

CELLULAR LOCALIZATION: Nuclear and Cytoplasmic.

Immunogen

Synthetic peptide corresponding to amino acids 2-13 from the N-terminus of mouse heat shock protein 90b.

Application

Immunoblotting: 5 μg/mL

Immunohistochemistry (frozen and formalin/paraffin): 5-10 μg/mL. Staining of formalin fixed tissue sections requires boiling the tissue sections in 10mM citrate buffer, pH 6.0 for 10-20 minutes followed by cooling at room temperature for 20 minutes.

Immunocytochemistry

Immunoprecpitation: 10 μg/mg of protein lysate.

Optimal working dilutions must be determined by end user.
Research Category
Protein Trafficking
Research Sub Category
Chaperones
This Anti-Heat Shock Protein 90β Antibody is validated for use in IP, WB, IC, IH(P) for the detection of Heat Shock Protein 90β.

Physical form

Format: Purified
Purified immunoglobulin. Liquid in 10 mM PBS, pH 7.4 with 0.2% BSA and 15 mM sodium azide.

Storage and Stability

Maintain at 2-8°C in undiluted aliquots for up to 6 months.

Analysis Note

Control
POSITIVE CONTROL: MAD109 cells or breast carcinoma.

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Legal Information

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), 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 Code

12 - Non Combustible Liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Thorsten Stühmer et al.
British journal of haematology, 147(3), 319-327 (2009-08-19)
The 90 kD heat shock protein (Hsp90) molecular chaperone sustains multiple components of oncogenic pathways and has recently emerged as a therapeutic target that is now being clinically tested in a number of malignancies. In order to address formulation issues
Signalling profile and antitumour activity of the novel Hsp90 inhibitor NVP-AUY922 in multiple myeloma.
Stuhmer, T; Zollinger, A; Siegmund, D; Chatterjee, M; Grella, E; Knop, S; Kortum et al.
Leukemia null
Ying-Li Wu et al.
Journal of cell science, 119(Pt 13), 2797-2806 (2006-06-15)
The involvement of telomerase in cellular immortalization and senescence has often been assessed by means of telomerase expression at the RNA level and quantification of telomerase activity by the telomeric repeat amplification protocol assay. However, these methods either neglected the
Vrushali Sagare-Patil et al.
Journal of assisted reproduction and genetics, 34(4), 495-503 (2017-02-27)
The aims of this paper were to study whether heat shock protein 90 (HSP90) is a regulator of sperm functions and to determine its association with oligoasthenozoospermia. The levels of HSP90 in sperm lysates were measured by ELISA. Localization of
Tanja Heimberger et al.
British journal of haematology, 160(4), 465-476 (2012-12-21)
The heat shock transcription factor 1 (HSF1) has recently been reported to promote malignant transformation and growth. Here we provide experimental evidence for a role of HSF1 in the pathogenesis of multiple myeloma (MM). Immunohistochemical analyses revealed that HSF1 was

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