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HSP90α (human), (recombinant)

 
ADI-SPP-776-D 50 µg 222.00 USD
 
ADI-SPP-776-F 200 µg 510.00 USD
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Product Specification

Alternative Name:HSP86, Heat shock protein 90α
 
Recommended Dilutions/Conditions:Western Blot (50ng, 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 E. coli.
 
UniProt ID:P07900
 
Formulation:Liquid. In Dulbecco's PBS containing 2.7mM potassium chloride, 1.5mM potassium phosphate, 137mM sodium chloride, 8.1mM sodium phosphate, and 10% glycerol.
 
Purity:≥90% (SDS-PAGE; Western blot)
 
Purity Detail:Purified by multi-step chromatography.
 
Applications:WB
 
Application Notes:Western blot control.
 
Shipping:Shipped on 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.
 

Product Literature References

Secreted heat shock protein 90 promotes prostate cancer stem cell heterogeneity: K.D. Nolan, et al.; Oncotarget 8, 19323 (2017), Abstract; Full Text
Anti-heat shock protein autoantibody profiling in breast cancer using customized protein microarray: L. Shi, et al.; Anal. Bioanal. Chem. 408, 1497 (2016), Abstract;
Discovery of novel oxazepine and diazepine carboxamides as two new classes of heat shock protein 90 inhibitors: T. Neubert, et al.; Bioorg. Med. Chem. Lett. 25, 1338 (2015), Application(s): Fluorescence Assay, Abstract;
Structure-activity relationship in a purine-scaffold compound series with selectivity for the endoplasmic reticulum Hsp90 paralog Grp94: H.J. Patel, et al.; J. Med. Chem. 58, 3922 (2015), Abstract; Full Text
Tumor-secreted Hsp90 subverts polycomb function to drive prostate tumor growth and invasion: K.D. Nolan, et al.; J. Biol. Chem. 290, 8271 (2015), Abstract; Full Text
A Repurposing Strategy for Hsp90 Inhibitors Demonstrates Their Potency against Filarial Nematodes: V. Gillan, et al.; PLoS Negl. Trop. Dis. 8, e2699 (2014), Application(s): Fluorescence polarization, Abstract; Full Text
Extracellular Hsp90 mediates an NF-κB dependent inflammatory stromal program: implications for the prostate tumor microenvironment: J.E. Bohonowych, et al.; Prostate 74, 395 (2014), Abstract; Full Text
Paralog-selective Hsp90 inhibitors define tumor-specific regulation of HER2: P.D. Patel, et al.; Nat. Chem. Biol. 9, 677 (2013), Abstract; Full Text
Human heat shock protein (Hsp) 90 interferes with Neisseria meningitidis adhesin A (NadA)-mediated adhesion and invasion: P. Montanari, et al.; Cell. Microbiol. 14, 368 (2012), Abstract;
A Novel Extracellular Hsp90 Mediated Co-Receptor Function for LRP1 Regulates EphA2 Dependent Glioblastoma Cell Invasion: U. Gopal, et al.; PLoS One 6, e17649 (2011), Abstract; Full Text
Extracellular heat shock protein-90α: linking hypoxia to skincell motility and wound healing: W. Li, et al. ; EMBO J. 26, 1221 (2007), Abstract;
In vitro biological characterization of a novel, synthetic diarylpyrazole resorcinol class of heat shock protein90 inhibitors: P. Workman, et al. ; Cancer Res. 67, 2206 (2007), Abstract;

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