HSP90 Antibody | StressMarq Biosciences SMC-107B product information

product summary

company name :

StressMarq Biosciences

product type :

antibody

product name :

HSP90 Antibody

catalog :

SMC-107B

quantity :

200 µg

price :

314.00 USD

clonality :

monoclonal

host :

mouse

conjugate :

nonconjugated

clone name :

H9010

reactivity :

human, mouse, rat, dogs

application :

western blot, ELISA, immunohistochemistry, immunocytochemistry, immunoprecipitation

more info or order :

StressMarq Biosciences product webpage

citations: 20

Published Application/Species/Sample/Dilution	Reference
western blot; human; loading ...; fig 5b, 6c	Inda M, Joshi S, Wang T, Bolaender A, Gandu S, Koren Iii J, et al. The epichaperome is a mediator of toxic hippocampal stress and leads to protein connectivity-based dysfunction. Nat Commun. 2020;11:319 pubmed publisher
immunohistochemistry; human; 1:500; loading ...; fig 3b	Rodina A, Wang T, Yan P, Gomes E, Dunphy M, Pillarsetty N, et al. The epichaperome is an integrated chaperome network that facilitates tumour survival. Nature. 2016;538:397-401 pubmed publisher
western blot; human; fig 1	Dong H, Zou M, Bhatia A, Jayaprakash P, Hofman F, YING Q, et al. Breast Cancer MDA-MB-231 Cells Use Secreted Heat Shock Protein-90alpha (Hsp90Î±) to Survive a Hostile Hypoxic Environment. Sci Rep. 2016;6:20605 pubmed publisher
western blot; human	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
western blot; human; 1:2500	Patel P, Yan P, Seidler P, Patel H, Sun W, Yang C, et al. Paralog-selective Hsp90 inhibitors define tumor-specific regulation of HER2. Nat Chem Biol. 2013;9:677-84 pubmed publisher
western blot; human; 1:2000	Taldone T, Zatorska D, Patel P, Zong H, Rodina A, Ahn J, et al. Design, synthesis, and evaluation of small molecule Hsp90 probes. Bioorg Med Chem. 2011;19:2603-14 pubmed publisher
western blot; human; 1:4000	Gershburg S, Murphy L, Marschall M, Gershburg E. Key motifs in EBV (Epstein-Barr virus)-encoded protein kinase for phosphorylation activity and nuclear localization. Biochem J. 2010;431:227-35 pubmed publisher
	Peksel B, Gombos I, Peter M, Tiszlavicz Á, Brameshuber M, Balogh G, et al. Mild heat induces a distinct "eustress" response in Chinese Hamster Ovary cells but does not induce heat shock protein synthesis. Sci Rep. 2017;7:15643 pubmed publisher
	Guo J, Jayaprakash P, Dan J, Wise P, Jang G, Liang C, et al. PRAS40 Connects Microenvironmental Stress Signaling to Exosome-Mediated Secretion. Mol Cell Biol. 2017;37: pubmed publisher
	Dong H, Le Y, Wang Y, Zhao H, Huang C, Hu Y, et al. Extracellular heat shock protein 90? mediates HDM-induced bronchial epithelial barrier dysfunction by activating RhoA/MLC signaling. Respir Res. 2017;18:111 pubmed publisher
	de la Mare J, Jurgens T, Edkins A. Extracellular Hsp90 and TGFÎ² regulate adhesion, migration and anchorage independent growth in a paired colon cancer cell line model. BMC Cancer. 2017;17:202 pubmed publisher
	Zou M, Bhatia A, Dong H, Jayaprakash P, Guo J, Sahu D, et al. Evolutionarily conserved dual lysine motif determines the non-chaperone function of secreted Hsp90alpha in tumour progression. Oncogene. 2017;36:2160-2171 pubmed publisher
	Matsuzaka Y, Tanihata J, Komaki H, Ishiyama A, Oya Y, Ruegg U, et al. Characterization and Functional Analysis of Extracellular Vesicles and Muscle-Abundant miRNAs (miR-1, miR-133a, and miR-206) in C2C12 Myocytes and mdx Mice. PLoS ONE. 2016;11:e0167811 pubmed publisher
	Tunnah L, MacKellar S, Barnett D, MacCormack T, Stehfest K, Morash A, et al. Physiological responses to hypersalinity correspond to nursery ground usage in two inshore shark species (Mustelus antarcticus and Galeorhinus galeus). J Exp Biol. 2016;219:2028-38 pubmed publisher
	Goldstein R, Yang S, Taldone T, Chang B, Gerecitano J, Elenitoba Johnson K, et al. Pharmacoproteomics identifies combinatorial therapy targets for diffuse large B cell lymphoma. J Clin Invest. 2015;125:4559-71 pubmed publisher
	Teigen L, Orczewska J, McLaughlin J, O Brien K. Cold acclimation increases levels of some heat shock protein and sirtuin isoforms in threespine stickleback. Comp Biochem Physiol A Mol Integr Physiol. 2015;188:139-47 pubmed publisher
	Jayaprakash P, Dong H, Zou M, Bhatia A, O Brien K, Chen M, et al. Hsp90Î± and Hsp90Î² together operate a hypoxia and nutrient paucity stress-response mechanism during wound healing. J Cell Sci. 2015;128:1475-80 pubmed publisher
	Bessemer R, Butler K, Tunnah L, Callaghan N, Rundle A, Currie S, et al. Cardiorespiratory toxicity of environmentally relevant zinc oxide nanoparticles in the freshwater fish Catostomus commersonii. Nanotoxicology. 2015;9:861-70 pubmed publisher
	Espallergues J, Teegarden S, Veerakumar A, Boulden J, Challis C, Jochems J, et al. HDAC6 regulates glucocorticoid receptor signaling in serotonin pathways with critical impact on stress resilience. J Neurosci. 2012;32:4400-16 pubmed publisher
	Chen Q, Prior M, Dargusch R, Roberts A, Riek R, Eichmann C, et al. A novel neurotrophic drug for cognitive enhancement and Alzheimer's disease. PLoS ONE. 2011;6:e27865 pubmed publisher

product information

Catalog No :

SMC-107B

Product Name :

HSP90 Antibody

Description :

Mouse Anti-Human HSP90 Monoclonal IgG2a

Target :

HSP90

Conjugate :

Unconjugated

2021 List Price :

314.00 USD

Currency :

USD

Research Area(s) :

Cancer Heat Shock Cell Signaling Protein Trafficking Chaperone Proteins Cancer Tumor Biomarkers

Alternative Name(s) :

HSP84 Antibody, HSP90 Antibody, HSP90 beta Antibody, HSP90B Antibody, HSPC2 Antibody, HSPCB Antibody

Size :

200 µg

Category :

Antibodies

Product Type :

Monoclonal

Clone Number :

H9010

Immunogen :

Recombinant human HSP90beta

Immunogen Species :

Human

Accession Number :

NP_031381.2

Swiss-Prot :

P08238

Applications :

WB IHC ICC/IF IP ELISA AM

Host Species :

Mouse

Isotype :

IgG2a

Species Reactivity Abbreviation :

Hu Ms Rt Rb Ck Dg Fs Shk Hm

Species Reactivity Full Name :

Human Mouse Rat Rabbit Chicken Dog Fish White Sucker Fish (Catostomus commersonii) Shark Gummy Shark (Mustelus antarcticus) School Shark (Galeorhinus galeus) Hamster

Antibody Dilution :

WB (1:2500), IHC (1:100); optimal dilutions for assays should be determined by the user.

Purification :

Protein G Purified

Storage Buffer :

PBS pH7.2, 50% glycerol, 0.09% sodium azide

Concentration :

1 mg/ml

Specificity :

Detects 90kDa. Detects HSP90 beta in all reactive species except in Chicken, where it detects both alpha and beta isoforms.

Storage Temperature :

-20ºC

Shipping Temperature :

Blue Ice or 4ºC

Cite this Product :

StressMarq Biosciences Cat# SMC-107B, RRID: AB_854214

Certificate of Analysis :

1 µg/ml of SMC-107 was sufficient for detection of HSP90beta in 20 µg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.

Cellular Localization :

Cytoplasm Melanosome

Scientific Background :

HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms α and β, which share 85% sequence amino acid homology. The two isoforms of HSP90, are expressed in the cytosolic compartment (1). Despite the similarities, HSP90α exists predominantly as a homodimer while HSP90β exists mainly as a monomer (2). From a functional perspective, HSP90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex (3-6). Furthermore, HSP90 is highly conserved between species; having 60% and 78% amino acid similarity between mammalian and the corresponding yeast and Drosophila proteins, respectively. HSP90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. Despite it's label of being a heat-shock protein, HSP90 is one of the most highly expressed proteins in unstressed cells (1–2% of cytosolic protein). It carries out a number of housekeeping functions – including controlling the activity, turnover, and trafficking of a variety of proteins. Most of the HSP90-regulated proteins that have been discovered to date are involved in cell signaling (7-8). The number of proteins now know to interact with HSP90 is about 100. Target proteins include the kinases v-Src, Wee1, and c-Raf, transcriptional regulators such as p53 and steroid receptors, and the polymerases of the hepatitis B virus and telomerase (5). When bound to ATP, HSP90 interacts with co-chaperones Cdc37, p23, and an assortment of immunophilin-like proteins, forming a complex that stabilizes and protects target proteins from proteasomal degradation. In most cases, HSP90-interacting proteins have been shown to co-precipitate with HSP90 when carrying out immunoadsorption studies, and to exist in cytosolic heterocomplexes with it. In a number of cases, variations in HSP90 expression or HSP90 mutation has been shown to degrade signaling function via the protein or to impair a specific function of the protein (such as steroid binding, kinase activity) in vivo. Ansamycin antibiotics, such as geldanamycin and radicicol, inhibit HSP90 function (9). For more information visit our HSP90 Scientific Resource Guide at http://www.HSP90.ca.

References :

1. Nemoto T., et al. (1997) J.Biol Chem. 272: 26179-26187. 2. Minami Y., et al. (1991), J.Biol Chem. 266: 10099-10103. 3. Arlander S.J.H., et al. (2003) J Biol Chem 278: 52572-52577. 4. Pearl H., et al. (2001) Adv Protein Chem 59:157-186. 5. Neckers L., et al. (2002) Trends Mol Med 8:S55-S61. 6. Pratt W., Toft D. (2003) Exp Biol Med 228:111-133. 7. Pratt W., Toft D. (1997) Endocr Rev 18:306–360. 8. Pratt W.B. (1998) Proc Soc Exptl Biol Med 217: 420–434. 9. Whitesell L., et al. (1994) Proc Natl Acad Sci USA 91: 8324–8328. 10. Barent R. L. (1998) Mol. Endocrinol. 12: 342-354 11. Lo. M.A. (1998) EMBO J. 17: 6879-6887.

Field of Use :

Not for use in humans. Not for use in diagnostics or therapeutics. For in vitro research use only.

Image Filenames :

SMC-107_Hsp90_Antibody_H9010_IHC_Human_colon-carcinoma_40x_1.png SMC-107_Hsp90_Antibody_H9010_WB_Human_cell-lysates-from-various-cell-lines_1.png SMC-107_Hsp90_Antibody_H9010_IHC_Human_colon-carcinoma_40x_2.png SMC-107_Hsp90_Antibody_H9010_IHC_Mouse_inflamed-colon_40x_2.png SMC-107_Hsp90_Antibody_H9010_IHC_Mouse_backskin_1.png SMC-107_Hsp90_Antibody_H9010_WB_Human_HeLa-cell-lysates_1.png SMC-107_Hsp90_Antibody_H9010_WB_Human_Lysates_1.png
SMC-107_Hsp90_Antibody_H9010_IHC_Mouse_
inflamed-colon_40x_1.png

more info or order :

StressMarq Biosciences product webpage