HSP90α (human), ELISA kit

Most sensitive, rapid ELISA kit for highly specific, quantitative detection of human HSP90α.



ADI-EKS-895	96 wells	709.00 USD

Reproducible - less than 10% variation between assays
Sensitive – detect as little as 50 pg/ml of human HSP90α
Higher throughput - test up to 40 samples in duplicate in just 3 hours
Quantitative - obtain precise, statistically significant results, facilitating comparison of data between multiple experiments

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

Sensitivity:	50 pg/ml (range 62.5 - 4,000 pg/ml)

Kit/Set Contains:	Microtiter plate, 5X Extraction reagent 2, Standard, Sample diluent, Wash buffer concentrate, HRP Conjugate, Conjugate diluent, TMB Substrate, Stop solution 2

Application:	For the quantitative determination of HSP90α in cell lysates, serum, and tissue of human origin.

Use/Stability:	Store all components at +4°, except standard at -20°.

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.