Product Specification
Alternative Name: | Heat shock protein 90α/β, HSP84, Heat shock protein 84 |
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Clone: | H90-10 |
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Host: | Mouse |
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Isotype: | IgG2a |
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Immunogen: | Purified human HSP90β (heat shock protein 90β). |
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UniProt ID: | P07900 (HSP90α), P08238 (HSP90β) |
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Source: | Purified from hybridoma tissue culture supernatant. |
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Species reactivity: | Human, Mouse Rabbit
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Applications: | ICC, IP, WB
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Recommended Dilutions/Conditions: | Western Blot (1:1,000) Suggested dilutions/conditions may not be available for all applications. Optimal conditions must be determined individually for each application. |
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Application Notes: | Works on endogenous. |
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Purity Detail: | Purified from concentrated hybridoma tissue culture supernatant. |
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Formulation: | Liquid. In PBS containing 0.02% sodium azide. |
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Use/Stability: | Stable for at least one year after receipt when stored as recommended. |
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Handling: | Avoid freeze/thaw cycles. |
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Shipping: | Shipped on Blue Ice |
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Long Term Storage: | -20°C |
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Regulatory Status: | RUO - Research Use Only |
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Product Literature References
Posttranscriptional Regulation of HIV-1 Gene Expression during Replication and Reactivation from Latency by Nuclear Matrix Protein MATR3: A. Sarracino, et al.; Mbio
9, e02158-18 (2018),
Abstract;
Full Text
Murine breast carcinoma 4T1 cells are more sensitive to atranorin than normal epithelial NMuMG cells in vitro: Anticancer and hepatoprotective effects of atranorin in vivo: P. Solar, et al.; Chem. Biol. Interact.
250, 27 (2016),
Application(s): Western blot,
Abstract;
A novel Hsp90 inhibitor to disrupt Hsp90/Cdc37 complex against pancreatic cancer cells: T. Zhang, et al.; Mol. Cancer Ther.
7, 162 (2008),
Abstract;
GCUNC-45 Is a Novel Regulator for the Progesterone Receptor/hsp90 Chaperoning Pathway: A. Chadli, et al.; Mol. Cell. Biol.
26, 1722 (2006),
Abstract;
Hsp90 inhibition depletes Chk1 and sensitizes tumor cells to replication stress: S.J. Arlander, et al.; J. Biol. Chem.
278, 52572 (2003),
Abstract;
Full Text
The Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKR: O. Donze, et al.; EMBO J.
20, 3771 (2001),
Abstract;
The hsp90-related protein TRAP1 is a mitochondrial protein with distinct functional properties: S.J. Felts, et al.; J. Biol. Chem.
275, 3305 (2000),
Abstract;
Full Text
Analysis of FKBP51/FKBP52 chimeras and mutants for Hsp90 binding and association with progesterone receptor complexes: R.L. Barent, et al.; Mol. Endocrinol.
12, 342 (1998),
Abstract;
Full Text
Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome: M.A. Loo, et al.; EMBO J.
17, 6879 (1998),
Abstract;
General Literature References
Cancer: the rules of attraction: L. Neckers and Y.S. Lee; Nature
425, 357 (2003), Review,
Abstract;
Heat shock protein 90 as a molecular target for cancer therapeutics: J.S. Isaacs, et al.; Cancer Cell
3, 213 (2003), Review,
Abstract;
More than folding: localized functions of cytosolic chaperones: J.C. Young, et al.; TIBS
28, 541 (2003), Review,
Abstract;