Exbio — Research products — Antibodies — Nucleus — Anti-HSP90 alpha/beta Purified

Anti-HSP90 alpha/beta Purified

Regulatory status

RUO

Antigen

HSP90 alpha/beta

Clone

MBH90AB

Format

Purified

Reactivity

Cow, Mouse, Human

Application

WB, IHC-P

Variant

0.1 mg

11-533-C100

In stock

242.00 USD

0.025 mg

11-533-C025

In stock

121.00 USD

Variant

0.1 mg

11-533-C100

In stock

242.00 USD

0.025 mg

11-533-C025

In stock

121.00 USD

Contact distributor

Product details

Description

Images

References

SDS download

Isotype

Mouse IgG1

Specificity

The antibody MBH90AB recognizes the epitope EEEVE within N-terminal part of ubiquitously expressed Hsp90 alpha and Hsp90 beta intracellular proteins with calculated Mw of 84.7 kDa and 83.3 kDa, respectively, however, migrating as 90 kDa bands under reducing SDS-PAGE conditions.

Application

WB, IHC-P

Application details

Western blotting: Recommended dilution: 1 μg/ml.

Reactivity

Cow, Mouse, Human

Immunogen

Peptide corresponding to the sequence EEVHHGEEEVEC within N-terminal part of human Hsp90.

Concentration

1 mg/ml

Preparation

Purified by protein-A affinity chromatography.

Formulation

Stabilizing phosphate buffered saline (PBS), pH 7.4, 15 mM sodium azide

Storage and handling

Store at 2-8°C. Do not freeze.

The product is intended For Research Use Only. Diagnostic or therapeutic applications are strictly forbidden. Products shall not be used for resale or transfer to third parties either as a stand-alone product or as a manufacture component of another product without written consent of EXBIO Praha, a.s. EXBIO Praha, a.s. will not be held responsible for patent infringement or any other violations of intellectual property rights that may occur with the use of the products. Orders for all products are accepted subject to the Term and Conditions available at www.exbio.cz. EXBIO, EXBIO Logo, and all other trademarks are property of EXBIO Praha, a.s.

Other names

HSP90A, HSP90B, LAP-2, LAP2, EL52

Antigen description

Hsp90 (heat shock protein 90) is one of the most abundant chaperones in the cytosol of eukaryotic cells. It interacts with various proteins, including protein kinases and transcription factors, and either facilitates their stabilization and activation or directs them for proteasomal degradation. Hsp90 thus affects multiple signaling pathways and biological processes and modulation of this single target offers the prospect of simultaneous intervence to various key points of oncogenic transformation. Hsp90 operates as a dimer in a conformational cycle driven by ATP binding and hydrolysis. There are two isoforms, alpha and beta, of vertebrate Hsp90. Whereas Hsp90 beta is expressed constitutively to a high level, Hsp90 alpha is stress-inducible and is overexpressed in many cancerous cells.

Western blotting analysis of Hsp90 alpha and beta protein by antibody MBH90AB to both Hsp90 alpha and beta isoform.

Immunohistochemistry staining of human testis (paraffin sections) using anti-HSP90 alpha/beta (MBH90AB).

General references:

Millson SH, Truman AW, Rácz A, Hu B, Panaretou B, Nuttall J, Mollapour M, Söti C, Piper PW: Expressed as the sole Hsp90 of yeast, the alpha and beta isoforms of human Hsp90 differ with regard to their capacities for activation of certain client proteins, whereas only Hsp90beta generates sensitivity to the Hsp90 inhibitor radicicol. FEBS J. 2007 Sep;274(17):4453-63.
PubMed

Pearl LH, Prodromou C, Workman P: The Hsp90 molecular chaperone: an open and shut case for treatment. Biochem J. 2008 Mar 15;410(3):439-53.
PubMed

Hooven TA, Yamamoto Y, Jeffery WR: Blind cavefish and heat shock protein chaperones: a novel role for hsp90alpha in lens apoptosis. Int J Dev Biol. 2004;48(8-9):731-8.
PubMed

Scheibel T, Buchner J: The Hsp90 complex--a super-chaperone machine as a novel drug target. Biochem Pharmacol. 1998 Sep 15;56(6):675-82.
PubMed

Pratt WB: The hsp90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors. Proc Soc Exp Biol Med. 1998 Apr;217(4):420-34.
PubMed

Product specific references:

Reiter K, Aguilar PP, Wetter V, Steppert P, Tover A, Jungbauer A: Separation of virus-like particles and extracellular vesicles by flow-through and heparin affinity chromatography. J Chromatogr A. 2019 Mar 15;1588:77-84
PubMed