HSP90α, mAb (9D2) (PE conjugate)



ADI-SPA-840PE-0050	50 µg	190.00 USD

ADI-SPA-840PE-0200	200 µg	410.00 USD

Product Specification

Alternative Name:	Hsp86, heat shock protein 90

Clone:	9D2

Host:	Rat

Isotype:	IgG2a

Immunogen:	Purified Hsp90 isolated from human therapeutic orchiectomy specimens.

UniProt ID:	P07900

Application:	Flow Cytometry (1:200) Optimal conditions must be determined individually for each application.

Specificity:	Recognizes human and chicken HSP90α. Detects a band of ~90kDa by Western blot.

Purity Detail:	Protein G-affinity purified.

Formulation:	Liquid. In PBS, pH 7.2, containing 0.09% sodium azide.

Long Term Storage:	+4°C

Miscellaneous/General:	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.

General Literature References

Association of hsp90 to the hTERT promoter is necessary for hTERT expression in human oral cancer cells: R.H. Kim, et al.; Carcinogenesis 29, 2425 (2008), Abstract;

Expression of hsp90 in the human kidney and in proximal tubule cells exposed to heat, sodium arsenite and cadmium chloride: S. Somji, et al. ; Toxicol. Lett. 133, 241 (2002), Application(s): IHC, WB using human samples, Abstract;

Nucleophosmin-anaplastic lymphoma kinase (NPM-ALK), a novel Hsp90-client tyrosine kinase: down-regulation of NPM-ALK expression and tyrosine phosphorylation in ALK(+) CD30(+) lymphoma cells by the Hsp90 antagonist 17-allylamino,17-demethoxygeldanamycin: P. Bonvini, et al. ; Cancer Res. 62, 1559 (2002), Abstract;

The charged region of Hsp90 modulates the function of the N-terminal domain: T. Scheibel, et al.; PNAS USA 96, 1297 (1999), Abstract;

Hsp90 as a capacitor for morphological evolution: S.L. Rutherford & S. Lindquist; Nature 396, 336 (1998), Abstract;

Oligomeric forms of the 90-kDa heat shock protein: T. Nemoto & N. Sato; Biochem J. 330, 989 (1998), Abstract;

The Hsp90 complex--a super-chaperone machine as a novel drug target: T. Scheibel & J. Buchner; Biochem. Pharmacol. 56, 675 (1998), Abstract;

Guidebook to Chaperones: T. Scheibel & J. Buchner; Ed. Gething, M.J. Oxford Univ. Press 147-150 (1997), Book,

Quantitation and intracellular localization of the 85K heat shock protein by using monoclonal and polyclonal antibodies: B.T. Lai, et al.; Mol. Cell Biol. 4, 2802 (1984), Abstract;