Product Name: HSP90 alpha/beta

Product Number: AB-NN061-2

Size:	25 µg		Price:	89.00
			$US

Target Full Name: Heat shock protein HSP 90-alpha/beta

Target Alias: HSP86; HSP89A; HSP90AA1; HSP90Alpha; HSPC1; HSPCA; HSPCAL3; HSP84; HSP90B; HSPC2; HSPCB; D6S182; FLJ26985

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

Antibody Code: NN061-2

Antibody Target Type: Pan-specific

Protein UniProt: P07900

Protein SigNET: P07900

Antibody Type: Monoclonal

Antibody Host Species: Mouse

Antibody Ig Isotype Clone: IgG2a

Antibody Immunogen Source: Recombinant human HSP90alpha; Specificity mapped to amino acids 291-304

Production Method: Protein G purified

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

Antibody Concentration: 1 mg/ml

Storage Buffer: Phosphate buffered saline pH7.2, 50% glycerol, 0.09% sodium azide

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 | Immunohistochemistry | ICC/Immunofluorescence | ELISA

Antibody Dilution Recommended: WB (1:1000), ICC/IF (1:100); optimal dilutions for assays should be determined by the user.

Antibody Potency: Very high potency. Detects a ~90 kDa protein, and will detect both alpha and beta form of HSP90.

Antibody Species Reactivity: Human | Mouse | Rat | S. cerevisiae | S. pombe

Antibody Positive Control: 1 µg/ml was sufficient for detection of HSP90αβ in 20 µg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat Anti-Mouse IgG:HRP as the secondary.

Antibody Specificity: Very high

Related Product 1: HSP90 complex pan-specific antibody (Cat. No.: AB-NN061-18)

Related Product 2: HSP90 alpha pan-specific antibody (Cat. No.: AB-NN061-19)

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

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

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 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). Looking for more information on HSP90? Visit our new HSP90 Scientific Resource Guide at http://www.HSP90.ca.

Figure 1. Immunoblotting of various cell lines with AB-NN061-2 antibody at a 1 µg/mL final concentration. The target protein HSP90a is indicated. Each lane was loaded with 15 µg of cell lysate protein. The max signal count was 55647.

Figure 2. Immunoblotting of various tissue lines with AB-NN061-2 antibody at a 1 µg/mL final concentration. The target protein HSP90a is indicated. Each lane was loaded with 15 µg of tissue lysate protein. The max signal count was 51975.

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 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] Kishimoto J et al. (2005). Cell Stress and Chaperones. 10 (4): 296-311.