HSP90α monoclonal antibody (9D2) | Enzo Life Sciences ADI-SPA-840-J product information

product summary

company name :

Enzo Life Sciences

other brands :

Stressgen, BioMol, Alexis Corporation, Assay Designs, Alexis

product type :

antibody

product name :

HSP90α monoclonal antibody (9D2)

catalog :

ADI-SPA-840-J

quantity :

1 mg

clonality :

monoclonal

host :

rat

conjugate :

nonconjugated

clone name :

9D2

reactivity :

human, chicken, E. coli

application :

western blot, immunohistochemistry, immunocytochemistry, immunoprecipitation, flow cytometry

more info or order :

Enzo Life Sciences product webpage

citations: 19

Published Application/Species/Sample/Dilution	Reference
flow cytometry; human; loading ...; fig 2	Bzowska M, Nogieć A, Bania K, Zygmunt M, Zarebski M, Dobrucki J, et al. Involvement of cell surface 90 kDa heat shock protein (HSP90) in pattern recognition by human monocyte-derived macrophages. J Leukoc Biol. 2017;102:763-774 pubmed publisher
immunoprecipitation; human; loading ...; fig 6b	Huang Z, Zhou X, He Y, Ke X, Wen Y, Zou F, et al. Hyperthermia enhances 17-DMAG efficacy in hepatocellular carcinoma cells with aggravated DNA damage and impaired G2/M transition. Sci Rep. 2016;6:38072 pubmed publisher
immunoprecipitation; human; fig 8 western blot; human; fig 7	Seidel C, Schnekenburger M, Mazumder A, Teiten M, Kirsch G, Dicato M, et al. 4-Hydroxybenzoic acid derivatives as HDAC6-specific inhibitors modulating microtubular structure and HSP90Î± chaperone activity against prostate cancer. Biochem Pharmacol. 2016;99:31-52 pubmed publisher
western blot; human; 1:2000	Riebold M, Kozany C, Freiburger L, Sattler M, Buchfelder M, Hausch F, et al. A C-terminal HSP90 inhibitor restores glucocorticoid sensitivity and relieves a mouse allograft model of Cushing disease. Nat Med. 2015;21:276-80 pubmed publisher
western blot; E. coli; fig 2	Liu W, Landgraf R. Phosphorylated and unphosphorylated serine 13 of CDC37 stabilize distinct interactions between its client and HSP90 binding domains. Biochemistry. 2015;54:1493-504 pubmed publisher
	Veit G, Oliver K, Apaja P, Perdomo D, Bidaud Meynard A, Lin S, et al. Ribosomal Stalk Protein Silencing Partially Corrects the ΔF508-CFTR Functional Expression Defect. PLoS Biol. 2016;14:e1002462 pubmed publisher
	Zhang X, Qian Z, Zhu H, Tang S, Wu D, Zhang M, et al. HSP90 gene expression induced by aspirin is associated with damage remission in a chicken myocardial cell culture exposed to heat stress. Br Poult Sci. 2016;57:462-73 pubmed publisher
	Zhang X, Zhu H, Qian Z, Tang S, Wu D, Kemper N, et al. The association of Hsp90 expression induced by aspirin with anti-stress damage in chicken myocardial cells. J Vet Sci. 2016;17:35-44 pubmed publisher
	Joshi A, Barabutis N, Birmpas C, Dimitropoulou C, Thangjam G, Cherian Shaw M, et al. Histone deacetylase inhibitors prevent pulmonary endothelial hyperpermeability and acute lung injury by regulating heat shock protein 90 function. Am J Physiol Lung Cell Mol Physiol. 2015;309:L1410-9 pubmed publisher
	Zeng X, Wang H, Bai F, Zhou X, Li S, Ren L, et al. Identification of matrine as a promising novel drug for hepatic steatosis and glucose intolerance with HSP72 as an upstream target. Br J Pharmacol. 2015;172:4303-18 pubmed publisher
	Liu W, Vielhauer G, Holzbeierlein J, Zhao H, Ghosh S, Brown D, et al. KU675, a Concomitant Heat-Shock Protein Inhibitor of Hsp90 and Hsc70 that Manifests Isoform Selectivity for Hsp90Î± in Prostate Cancer Cells. Mol Pharmacol. 2015;88:121-30 pubmed publisher
	Huang T, Chen S, Han H, Li H, Huang Z, Zhang J, et al. Expression of Hsp90? and cyclin B1 were related to prognosis of esophageal squamous cell carcinoma and keratin pearl formation. Int J Clin Exp Pathol. 2014;7:1544-52 pubmed
	Hunter M, O Hagan K, Kenyon A, Dhanani K, Prinsloo E, Edkins A. Hsp90 binds directly to fibronectin (FN) and inhibition reduces the extracellular fibronectin matrix in breast cancer cells. PLoS ONE. 2014;9:e86842 pubmed publisher
	Knee K, Sergeeva O, King J. Human TRiC complex purified from HeLa cells contains all eight CCT subunits and is active in vitro. Cell Stress Chaperones. 2013;18:137-44 pubmed publisher
	Solier S, Kohn K, Scroggins B, Xu W, Trepel J, Neckers L, et al. Heat shock protein 90? (HSP90?), a substrate and chaperone of DNA-PK necessary for the apoptotic response. Proc Natl Acad Sci U S A. 2012;109:12866-72 pubmed publisher
	Pellegrin S, Heesom K, Satchwell T, Hawley B, Daniels G, van den Akker E, et al. Differential proteomic analysis of human erythroblasts undergoing apoptosis induced by epo-withdrawal. PLoS ONE. 2012;7:e38356 pubmed publisher
	Teng Y, Ngoka L, Mei Y, Lesoon L, Cowell J. HSP90 and HSP70 proteins are essential for stabilization and activation of WASF3 metastasis-promoting protein. J Biol Chem. 2012;287:10051-9 pubmed publisher
	Sahu D, Zhao Z, Tsen F, Cheng C, Park R, Situ A, et al. A potentially common peptide target in secreted heat shock protein-90? for hypoxia-inducible factor-1?-positive tumors. Mol Biol Cell. 2012;23:602-13 pubmed publisher
	Kim R, Kim R, Chen W, Hu S, Shin K, Park N, et al. Association of hsp90 to the hTERT promoter is necessary for hTERT expression in human oral cancer cells. Carcinogenesis. 2008;29:2425-31 pubmed publisher

product information

Product ID :

ADI-SPA-840

Catalog Number :

ADI-SPA-840-J

Product Name :

HSP90α monoclonal antibody (9D2)

Host species :

Rat

Clonality :

Monoclonal

Product Type :

Antibody

Size :

1 mg

list of Pubmed id :

26549368, 25939977, 25619116, 24817950, 24466266, 23011926, 22753480, 22723854, 22315230, 22190738

Clone :

9D2

Isotype :

IgG2a

SPECIES REACTIVITY :

Human, Chicken

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

Immunogen :

Purified Hsp90 isolated from human therapeutic orchiectomy specimens.

Buffer :

Liquid. In PBS, pH 7.2, containing 50% glycerol and 0.09% sodium azide.

Uses :

Detects a band of ~90kDa by Western blot.

Application Summary :

FC, ICC, IHC, IP, WB

Storage :

-20°C

more info or order :

Enzo Life Sciences product webpage