Product Name	Hsp90 (complex) Antibody
Catalog #	SMC-109A
Package size	50ug

Alternate Product Sizes	SMC-109B
Type	Monoclonal
Conjugate	N/A
Datasheet	SMC 109 Heat Shock Protein 90 complex
Description	Anti-Hsp90 complex
Research Area	Chaperones, Heat Shock, Trafficking
Clone Number	8D3
Host Species	Mouse
Isotype	IgM
Immunogen	Ah receptor (Aryl hydrocarbon receptor)
Applications	IP
Species Reactivity	Human, Mouse, Rat, Rabbit. Other species not yet tested.
Accession Number	NP_031381.2
Gene ID	3326
SwissProt	P08238
Background Info	Immunoprecipitates 90kDa proteins corresponding to the molecular mass of Hsp90. Co-immunoprecipitates Hsp90 complexes, including Hsp70, Hop, Ah receptors, glucocorticoid receptors, heme-regulated eukaryotic initiation factor 2a (eIF-2a) kinase (HRI).
Recommended Dilutions	Best results for IP associated with use of goat anti-mouse IgM beads.
Form	PEG Purified
Storage Buffer	PBS, 50% glycerol, 0.09% sodium azide
Concentration	1mg/mL
Certificate of Analysis	Goat anti-mouse IgM was used to bind 25 μl of protein G-Sepharose. SMC-109 IgM from 0.5 ml of high speed supernatant medium was loaded onto the IgG resin and incubated with 100 μl of rabbit reticulocyte lysate for 30 min. at 30C. After washing (4X1 ml), bound proteins were resolved on SDS PAGE, including hsp90, hsp70 and Hop.
Storage Temp	-20 °C
Shipping Temp	Blue Ice or 4 °C

Research Background	Hsp90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. From a functional perspective, hsp90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex (1-4). 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 (5-6). 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 (7).
References	1. Arlander SJH, et al. (2003) J Biol Chem 278: 52572-52577. 2. Pearl H, et al. (2001) Adv Protein Chem 59:157-186. 3. Neckers L, et al. (2002) Trends Mol Med 8:S55-S61. 4. Pratt W, Toft D. (2003) Exp Biol Med 228:111-133. 5. Pratt W, Toft D. (1997) Endocr Rev 18: 306–360. 6. Pratt WB. (1998) Proc Soc Exptl Biol Med 217: 420–434. 7. Whitesell L, et al. (1994) Proc Natl Acad Sci USA 91: 8324– 8328. 8. Perdew, G. H. (1988) JBC 263 (27): 13802-13805 9. Dalman, F. C. et al. (1989) JBC 264(33): 19815-19821 10. Uma, S. et al. (1997) JBC 272(17): 11648-11656.
Cited References	1. Ardi, V.C., Alexander, L.D., Johnson, V. and McAlpine S.R. (2011). Macrocycles that inhibit the binding between heat shock protein 90 and TPR-containing proteins. ACS Chem Biol. 6 (12), 1357-1366. doi: 10.1021/cb200203m