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

Anti-HSP90 beta Purified

Regulatory status

RUO

Antigen

HSP90 beta

Clone

MBH90B

Format

Purified

Reactivity

Cow, Human, Mouse

Application

IP, WB, ICC

Variant

0.1 mg

11-534-C100

In stock

242.00 USD

0.025 mg

11-534-C025

Delivery 1 week

121.00 USD

Variant

0.1 mg

11-534-C100

In stock

242.00 USD

0.025 mg

11-534-C025

Delivery 1 week

121.00 USD

Contact distributor

Product details

Description

Images

References

SDS download

Isotype

Mouse IgG1

Specificity

The antibody MBH90B recognizes the EEVHHG epitope within the N-terminal part of Hsp90 beta an ubiquitously expressed intracellular protein with calculated Mw of 83.3 kDa, however, migrating as a 90 kDa band under reducing SDS-PAGE conditions.

Application

IP, WB, ICC

Application details

Western blotting: Recommended dilution: 1 μg/ml.
Immunocytochemistry: Recommended dilution: 1 μg/ml.
Immunoprecipitation: Recommended dilution: 1 μg/ml.

Reactivity

Cow, Human, Mouse

Immunogen

Peptide corresponding to the EEVHHGEEEVEC sequence 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

HSP90B, HSPCB

Antigen description

Hsp90 beta (heat shock protein 90 beta) is a constitutively expressed isoform of Hsp90, one of the most abundant chaperones in the cytosol of eukaryotic cells. Hsp90 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.

UniProt ID P08238

Western blotting analysis of MBH90B reactivity with various cell lines and recombinant Hsp90 alpha and Hsp90 beta protein.

General references:

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

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

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

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:

Kakeda M, Arock M, Schlapbach C, Yawalkar N: Increased expression of heat shock protein 90 in keratinocytes and mast cells in patients with psoriasis. J Am Acad Dermatol. 2014 Apr;70(4):683-690.
PubMed