antibody

Hsp90 alpha Antibody: HRP, Anti-HSP90 alpha Antibody: Clone 2G5.G3

MBS802750

0.2 mg

475 USD

monoclonal

mouse

HRP

[IgG]

human, mouse, rat

western blot, ELISA, immunohistochemistry, immunocytochemistry, immunoprecipitation

Antibody

Hsp90 alpha Antibody: HRP, Anti-HSP90 alpha Antibody: Clone 2G5.G3

[Hsp90 alpha]

[Hsp86; Hsp89A; Hsp90AA1; Hsp90Alpha; HspC1; HSPCA; HspCAL3]

[heat shock protein HSP 90-alpha isoform 1; Heat shock protein HSP 90-alpha; heat shock protein HSP 90-alpha; HSP 86; heat shock 86 kDa; LPS-associated protein 2; heat shock 90kD protein 1, alpha; heat shock 90kDa protein 1, alpha; renal carcinoma antigen NY-REN-38; heat shock 90kD protein, alpha-like 4; epididymis luminal secretory protein 52; heat shock 90kD protein 1, alpha-like 4; lipopolysaccharide-associated protein 2; heat shock protein 90kDa alpha (cytosolic), class A member 1; Heat shock 86 kDa; HSP 86; HSP86; Lipopolysaccharide-associated protein 2; LAP-2; LPS-associated protein 2; Renal carcinoma antigen NY-REN-38]

[HSP90AA1; HSP90AA1; EL52; HSPN; LAP2; HSP86; HSPC1; HSPCA; Hsp89; Hsp90; LAP-2; HSP89A; HSP90A; HSP90N; HSPCAL1; HSPCAL4; HSP90A; HSPC1; HSPCA; HSP 86; HSP86; LAP-2; LPS-associated protein 2]

HS90A_HUMAN

Monoclonal

IgG1 Kappa

[IgG]

Mouse

Human, Mouse, Rat

854

Detects ~90kDa. HSP90a-specific (>96%) a-specific by ELISA).

Protein G Purified

1mg/mL

Store at -20°C for 1 year . Avoid freeze thaw cycles.

WB, IHC, ICC/IF, IP, ELISA

WB (1:2000). ICC/IF (1:100). optimal dilutions for assays should be determined by the user.

Immunocytochemistry/Immunofluorescence (ICC/IF)

Western Blot (WB)

Buffer: PBS pH7.2, 50% glycerol, 0.09% sodium azide. Certificate of Analysis: 0.5 ug/mL of MBS802750 was sufficient for detection of HSP90 alpha in 20 ug of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG: HRP: as the secondary antibody. Research areas: Cancer Heat Shock. Cellular localization: Cytoplasm Melanosome

Chaperones, Heat Shock, Trafficking

Background Info: Hsp90alpha-specific (>96% alpha-specific by ELISA). Scientific Background: HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms alpha and beta, which share 85% sequence amino acid homology. The two isoforms of Hsp90 are expressed in the cytosolic compartment (1). Despite the similarities, HSP90alpha exists predominantly as a homodimer while HSP90beta 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 its 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).

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 SJH, 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 WB. (1998) Proc Soc Exptl Biol Med 217, 420-434. 9. Whitesell L, et al. (1994) Proc Natl Acad Sci USA 91, 8324-8328. 10. Nemoto, T. (1997) Biochem and Mol. Bio Intl. 42 (5), 881-889. 1. Orthwein, A. et al. (2010). Regulation of activation-induced deaminase stability and antibody gene diversification by Hsp90. JEM. 207 (12). 2751-2765. doi: 10.1084/jem.20101321 . 2. Di Noia, J.M. and Orthwein, A. (2011). Modulating and/or detecting activation induced deaminase and methods of use thereof. United States Patent Application. US 20110237560 A1. 3. O Neill, A.J. et al. (2011). Characterisation and manipulation of docetaxel resistant prostate cancer cell lines. Mol Cancer. 10 (126). doi:10.1186/1476-4598-10-126. 4. Quanz, M. et al. (2012). Heat Shock Protein 90 (Hsp90 ) Is Phosphorylated in Response to DNA Damage and Accumulates in Repair Foci. J Biol Chem. 287, 8803-8815. doi:10.1074/jbc.M111.320887

153792590

NP_001017963.2

NM_001017963.2

P07900

AhR Pathway (755436); Antigen Processing And Presentation Pathway (83074); Antigen Processing And Presentation Pathway (485); Attenuation Phase Pathway (980473); Axon Guidance Pathway (105688); Binding And Uptake Of Ligands By Scavenger Receptors Pathway (771599); Cell Cycle Pathway (530733); Cell Cycle, Mitotic Pathway (105765); Cellular Response To Heat Stress Pathway (980470); Cellular Responses To Stress Pathway (645258)

The protein encoded by this gene is an inducible molecular chaperone that functions as a homodimer. The encoded protein aids in the proper folding of specific target proteins by use of an ATPase activity that is modulated by co-chaperones. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jan 2012]

HSP90A: a molecular chaperone of the heat shock protein 90 family. Has ATPase activity. Known to interact with a wide variety of proteins including steroid hormone receptors, neuropeptide Y, FKBP51/54, and FKBP52. G protein-coupled receptor kinases are stabilized by interacting with HSP 90. Hsp70 and Hsp90 promote tau solubility and tau binding to microtubules, reducing insoluble tau phosphorylation of tau. Protein type: Heat shock protein; Chaperone. Chromosomal Location of Human Ortholog: 14q32.33. Cellular Component: nucleoplasm; mitochondrion; membrane; cytoplasm; melanosome; extracellular region; plasma membrane; cytosol; nucleus. Molecular Function: identical protein binding; protein binding; protein homodimerization activity; TPR domain binding; ATPase activity; nitric-oxide synthase regulator activity; unfolded protein binding; nucleotide binding; ATP binding. Biological Process: receptor-mediated endocytosis; axon guidance; positive regulation of nitric oxide biosynthetic process; organelle organization and biogenesis; signal transduction; nitric oxide metabolic process; protein import into mitochondrial outer membrane; response to unfolded protein; mitochondrial transport; innate immune response; protein refolding; mitotic cell cycle; regulation of nitric-oxide synthase activity; G2/M transition of mitotic cell cycle; vascular endothelial growth factor receptor signaling pathway; chaperone-mediated protein complex assembly

0.2 mg

475 USD