HSP90α (human), (recombinant) | Enzo Life Sciences ADI-SPP-776-F product information

This webpage contains legacy information. The product is either no longer available from the supplier or has been delisted at Labome.

product summary

company name :

Enzo Life Sciences

other brands :

Stressgen, BioMol, Alexis Corporation, Assay Designs, Alexis

product type :

protein

product name :

HSP90α (human), (recombinant)

catalog :

ADI-SPP-776-F

quantity :

200 µg

citations: 4

Reference
Neubert T, Numa M, Ernst J, Clemens J, Krenitsky P, Liu M, et al. Discovery of novel oxazepine and diazepine carboxamides as two new classes of heat shock protein 90 inhibitors. Bioorg Med Chem Lett. 2015;25:1338-42 pubmed publisher
Gillan V, O Neill K, Maitland K, Sverdrup F, Devaney E. A repurposing strategy for Hsp90 inhibitors demonstrates their potency against filarial nematodes. PLoS Negl Trop Dis. 2014;8:e2699 pubmed publisher
Sharp S, Boxall K, Rowlands M, Prodromou C, Roe S, Maloney A, et al. In vitro biological characterization of a novel, synthetic diaryl pyrazole resorcinol class of heat shock protein 90 inhibitors. Cancer Res. 2007;67:2206-16 pubmed
Li W, Li Y, Guan S, Fan J, Cheng C, Bright A, et al. Extracellular heat shock protein-90alpha: linking hypoxia to skin cell motility and wound healing. EMBO J. 2007;26:1221-33 pubmed

product information

Product ID :

ADI-SPP-776

Catalog Number :

ADI-SPP-776-F

Product Name :

HSP90α (human), (recombinant)

Product Type :

Protein

Size :

200 µg

list of Pubmed id :

25677667, 24551261, 17332351, 17304217

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.

ALTnames :

HSP86, Heat shock protein 90α

Purity :

≥90% (SDS-PAGE; Western blot)

Buffer :

Liquid. In Dulbecco's PBS containing 2.7mM potassium chloride, 1.5mM potassium phosphate, 137mM sodium chloride, 8.1mM sodium phosphate, and 10% glycerol.

Uses :

Western blot control.

Application Summary :

Storage :

-80°C