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HSP90α (human), ELISA kit

Most sensitive, rapid ELISA kit for highly specific, quantitative detection of human HSP90α.
ADI-EKS-895 96 wells 781.00 USD
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  • Reproducible with less than 10% variation between assays
  • Highly sensitive detecting as little as 50 pg/ml of human HSP90α
  • Higher throughput format, test up to 40 samples in duplicate in just 3 hours
  • Fully quantitative results that surpass semi-quantitative Western blot analysis
The HSP90α (human), EIA kit is a colorimetric immunometric enzyme immunoassay kit with results in < 3 hours. Absorbance is read at 450 nm. Save time, money, and precious sample with fully quantitative results and increased sensitivity compared to Western blot analysis.
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Product Specification

Alternative Name:Heat shock protein 90α, HSP86
Sensitivity:50 pg/ml (range 62.5 - 4,000 pg/ml)
Assay Time:<3 hours
Applications:ELISA, Colorimetric detection
Application Notes:For the quantitative determination of HSP90α in cell lysates, serum, and tissue of human origin.
Species reactivity:Human
Crossreactivity:HSP90α (100%). No reactivity with HSP90β, Grp94, HSP60, or HSP70 (HSP72).
Use/Stability:Store all components at +4°, except standard at -20°.
Shipping:Shipped on Dry Ice
Contents:Microtiter plate, 5X Extraction reagent 2, Standard, Sample diluent, Wash buffer concentrate, HRP Conjugate, Conjugate diluent, TMB Substrate, Stop solution 2
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.
UniProt ID:P07900

Product Literature References

Proinsulin and heat shock protein 90 as biomarkers of beta-cell stress in the early period after onset of type 1 diabetes: R.A. Watkins, et al.; Transl. Res. 168, 96 (2016), Application(s): HSP90 levels measured in serum samples, Abstract;
Could the Anti-Chaperone VER155008 Replace Temozolomide for Glioma Treatment: L. Shervington, et al.; J. Cancer 6, 786 (2015), Application(s): ELISA using human cell lysate, Abstract; Full Text
Effects of cytarabine on activation of human T cells - cytarabine has concentration-dependent effects that are modulated both by valproic acid and all-trans retinoic acid: E. Ersvaer, et al.; BMC Pharmacol. Toxicol. 16, 12 (2015), Application(s): ELISA using human supernatant, Abstract; Full Text
Secreted Hsp90 is a novel regulator of the epithelial to mesenchymal transition (EMT) in prostate cancer: M.W. Hance, et al.; J. Biol. Chem. 287, 37732 (2012), Abstract;

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