Product Name: Hsp90 beta

Product Number: AB-NN165-1

Size:	25 µl		Price:	89.00
			$US

Target Full Name: Heat shock protein HSP 90-beta

Target Alias: Hsp84; Hsp90; Hsp86; Hsp89; Hsp90B; Hsp90BETA; Hsp90N; HSPC2; HSPCA; HSPCAL1; HSPCB; HSPN; LAP2; NY REN 38 antigen

Product Type Specific: Heat shock/stress protein pan-specific antibody

Antibody Code: NN165-1

Antibody Target Type: Pan-specific

Protein UniProt: P08238

Protein SigNET: P08238

Antibody Type: Polyclonal

Antibody Host Species: Rabbit

Antibody Immunogen Source: Purified recombinant human Hsp90 beta

Production Method: Rabbit antiserum

Antibody Modification: Unconjugated. Contact KInexus if you are interest in having the antibody biotinylated or coupled with fluorescent dyes.

Storage Buffer: Rabbit antiserum

Storage Conditions: For long term storage, keep frozen at -40°C or lower. Stock solution can be kept at +4°C for more than 3 months. Avoid repeated freeze-thaw cycles.

Product Use: Western blotting, ELISA, Immunoprecipitation, Immunohistochemistry, Immunofluorescence

Antibody Dilution Recommended: 1:20000-40000 (ECL) (WB)

Antibody Potency: Detects a ~90 kDa proteins corresponding to the molecular mass of Hsp90-beta. Does not cross-react with Hsp90 alpha.

Antibody Species Reactivity: Human, Rat, Mouse

Antibody Positive Control: A 1:4000 dilution of SPC-177 was sufficient for detection of hsp90 in 20μg of HeLa cell lysate by ECL immunoblot analysis.

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Related Product 4: HSP90 alpha/beta pan-specific antibody (Cat. No.: AB-NN061-2)

Related Product 5: HSP90 pan-specific antibody (Cat. No.: AB-NN061-3)

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Related Product 7: HSP90 (total) pan-specific antibody (Cat. No.: AB-NN061-9)

Scientific 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 S.J.H. 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 W.B. (1998) Proc Soc Exptl Biol Med 217: 420–434.

[7] Whitesell L. et al. (1994) Proc Natl Acad Sci USA 91: 8324– 8328.