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HSP90 (human), (native)



ADI-SPP-770-D	50 µg	439.00 USD

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Product Details

Alternative Name:	HSP86, Heat shock protein 90

Recommended Dilutions/Conditions:	Western Blot (100ng, colorimetric) Suggested dilutions/conditions may not be available for all applications. Optimal conditions must be determined individually for each application.

MW:	~90kDa

Source:	Produced in HeLa cells.

UniProt ID:	P07900 (HSP90α), P08238 (HSP90β)

Formulation:	Liquid. In 50mM TRIS-HCl, pH 7.5, containing 1.0mM DTT and 100mM sodium chloride.

Purity:	≥90% (SDS-PAGE; Western blot)

Purity Detail:	Purified by multi-step chromatography.

Applications:	ELISA, WB Antigen microarray

Application Notes:	Western blot control.

Shipping:	Dry Ice

Long Term Storage:	-80°C

Scientific Background:	The Hsp90 family of heat shock proteins represents one of the most abundantly expressed and highly conserved families of cellular chaperones whose expression can be upregulated under conditions of cellular stress, and includes cytoplasmic (Hsp90-alpha/beta), ER (grp94), and mitochondrial (TRAP1) localized members. Structurally, Hsp90 is characterized by an N-terminal ATP-binding domain, a medial substrate-binding domain, and a C-terminal dimerization motif. Hsp90 dimers function in cooperation with cochaperones (e.g. Hsp40, Hsp70, Hop, p23) to stabilize a multitude of client protein substrates, including steroid hormone receptors, protein kinases, and transcription factors. The essential binding and hydrolysis of ATP by Hsp90 is inhibited by ansamycin drugs (e.g. geldanamycin, 17-AAG) which occupy the N-terminal Hsp90 nucleotide-binding pocket. Many Hsp90 client proteins such as erbB2/Her-2, c-raf, bcr-abl, p53, and hTERT, are members of well characterized oncogenic pathways, making Hsp90 inhibitors useful anticancer agents.

Regulatory Status:	RUO - Research Use Only

SDS-PAGE analysis: Lane 1: MW marker, Lane 2: 1.0µg of Natural Source Human HSP90 Protein.

Western Blot analysis: Lane 1: MWM, Lane 2: Natural Source Human HSP90 Protein.

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Product Literature References

Intergenerational plasticity to cycling high temperature and hypoxia affects offspring stress responsiveness and tolerance in zebrafish: M.Y.T. Lim & N.J. Bernier; J. Exp. Biol. (2023), Abstract;

Zebrafish parental progeny investment in response to cycling thermal stress and hypoxia: deposition of heat shock proteins but not cortisol: M.Y.T. Lim & N.J. Bernier; J. Exp. Biol. 225, jeb244715 (2022), Abstract;

Nck-associated protein 1 associates with HSP90 to drive metastasis in human non-small-cell lung cancer: Y. Xiong, et al.; J. Exp. Clin. Cancer Res. 38, 122 (2019), Abstract; Full Text

Pass the salt: physiological consequences of ecologically relevant hyposmotic exposure in juvenile gummy sharks (Mustelus antarcticus) and school sharks (Galeorhinus galeus): A.J. Morash, et al.; Conserv. Physiol. 4, cow036 (2016), Abstract; Full Text

CpG-A stimulates Hsp72 secretion from plasmacytoid dendritic cells, facilitating cross-presentation: T. Tanaka, et al.; Immunol. Lett. 167, 34 (2015), Application(s): ELISA using human or murine DCs , Abstract;

The Effects of Acute Waterborne Exposure to Sublethal Concentrations of Molybdenum on the Stress Response in Rainbow Trout, Oncorhynchus mykiss: C.D. Ricketts, et al.; PLoS One 10, e0115334 (2015), Application(s): Western Blotting, Abstract; Full Text

Antigen microarrays identify unique serum autoantibody signatures inclinical and pathologic subtypes of multiple sclerosis: H. Weiner, et al. ; PNAS 105, 18889 (2008), Application(s): Antigen Microarray , Abstract;

CAIR-1/BAG-3 abrogates heat shock protein-70 chaperone complex-mediated protein degradation: accumulation of poly-ubiquitinated Hsp90 client proteins: E.C. Kohn, et al. ; J. Biol. Chem. 278, 28490 (2003), Application(s): WB , Abstract;

Development of a purine-scaffold novel class of Hsp90 binders that inhibit the proliferation of cancer cells and induce the degradation of Her2 tyrosine kinase: N. Rosen, et al. ; Bioorg. Med. Chem. 10, 3555 (2002), Abstract;

Hsp90 makes the human HBV Pol competent for in vitro priming rather than maintaining the human HBV Pol/pregenomic RNA complex: G. Jung, et al. ; Arch. Biochem. Biophys. 401, 99 (2002), Application(s): WB , Abstract;

Identification of heat shock protein90 and other proteins as tumour antigens by serological screening of an ovarian carcinoma expression library: E.P. Diamandis, et al. ; Br. J. Cancer 87, 339 (2002), Application(s): EIA , Abstract;

Hsp25 and -90 immunoreactivity in the normal rat eye: M. Tytell, et al. ; Invest. Ophthalmol. Vis. Sci. 42, 3031 (2001), Application(s): WB , Abstract;

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