Product Name

Hsp90

Catalog #

SMC-107A

Alternative Names

Hsp84, Hsp90, Hsp90 beta, Hsp90B, HspC2, HSPCB

Clone Number

H9010

Immunogen

Recombinant human Hsp90beta

Accession Number

NP_031381.2

Gene ID

3326

SwissProt

P08238

Applications

WB, IP, ELISA, IHC

Host Species

Mouse

Isotype

IgG2a

Species Reactivity

Human (beta-specific), Rabbit (Beta Specific), Chicken (Alpha/Beta), Rat, Canine

Recommended Dilutions

1µg/ml was sufficient for detection of hsp90beta by Western Blot in 20µg of HeLa lysate.

Form

Protein G Purified

Storage Buffer

PBS pH7.2, 50% glycerol

Concentration

1mg/mL

Background Info

Detects 90kDa proteins corresponding to the molecular mass of Hsp90β.

Conjugate

N/A

Package Size

50ug

Storage Temp

-20°C

Shipping Temp

Blue Ice or 4°C

Datasheet

SMC 107 Heat Shock Protein 90 (Hsp90)

Research Area

Chaperones, Heat Shock, Trafficking

Certificate of Analysis

1 μg/mL of SMC-107 was sufficient for detection of Hsp90beta in 20μg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.

Price

$139.00 USD Add to Cart Bulk Quote

Western blot analysis of Hsp90 using cell lysates from 12 human cancer cell lines at a 1:1000 dilution of SMC-107.


Western blot comparison of H9010s behavior with Hsp90 human beta (1) and Hsp90 human alpha (2). 
Picture courtesy of David Toft, Mayo Clinic.


Western blot analysis of Hsp90 in HeLa cell lysates using a 1:1000 dilution of SMC-107.

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. 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.

Cited References

1. Tony Taldonea, Danuta Zatorska, Pallav D. Patel, Hongliang Zong, Anna Rodina, James H. Ahn, Kamalika Moulick, Monica L. Guzman, Gabriela Chiosis. Design, synthesis, and evaluation of small molecule Hsp90 probes.    Bioorganic & Medicinal Chemistry. Volume 19, Issue 8, 15 April 2011, Pages 2603-2614. doi:10.1016/j.bmc.2011.03.013

2. Stasyk, T., Hotzmann, J., Stumberger, S., Ebner, H. L., Hess, M. W., Bonn. G. K., Mechtler, K. and Huber, L. A. Proteomic analysis of endosomes from genetically modified p14/MP1 mouse embryonic fibroblasts. Proteomics, Volume 10, Issue 22, pp 4117-4127 2010. DOI: 10.1002/pmic.201000258.

3. Anne Bailey and Lorne J. Hofseth. A method to enhance the sensitivity and reproducibility of immunohistochemistry http://www.prohisto.com/pdfs/Hofseth_Manuscript-81.pdf 2. Svetlana Gershburg, Leann Murphy, Manfred Marschall, Edward Gershburg. Key Motifs in Epstein-Barr Virus (EBV)-encoded protein kinase for phosphorylation activity and nuclear localization. Biochemical Journal Immediate Publication. Published on 12 Aug 2010 as manuscript BJ20100558

4. Espallergues J, Teegarden SL, Veerakumar A, Boulden J, Challis C, Jochems J, Chan M, Petersen T, Deneris E, Matthias P, Hahn CG, Lucki I, Beck SG, Berton O. HDAC6 Regulates Glucocorticoid Receptor Signaling in Serotonin Pathways with Critical Impact on Stress Resilience.  The Journal of Neuroscience, 28 March 2012, 32(13): 4400-4416; doi: 10.1523/​JNEUROSCI.5634-11.2012