Product Name: HSP25/HSP27
Product Number: AB-NN056-2
Size: 25 µg      Price:89.00
      $US
Target Full Name: Heat shock protein beta-1

Target Alias: HSPB2; Heat shock protein beta-2; HSPB2; DMPK-binding protein; MKBP

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

Antibody Code: NN056-2

Antibody Target Type: Pan-specific

Protein UniProt: P04792 

Protein SigNET: P04792 

Antibody Type: Monoclonal

Antibody Host Species: Mouse

Antibody Ig Isotype Clone: IgG1Kappa

Antibody Immunogen Source: HSP27 peptide

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, 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 | Immunoprecipitation

Antibody Dilution Recommended: WB (1:5000), ICC/IF (1:200), IHC (1:100); optimal dilutions for assays should be determined by the user.

Antibody Potency: Detects a ~25 kDa protein (HSP25) and ~27 kDa (HSP27) proteins in cell and tissue lysates by Western blotting.

Antibody Species Reactivity: Human | Mouse | Rat | Bovine | Dog | Guinea pig | Hamster

Antibody Positive Control: A 1:5000 dilution of SMC-114 was sufficient for detection of HSP27 in 20 µg of HeLa cell lysate by ECL immunoblot analysis.

Antibody Cross Reactivity: Antibody cross-reacts with alpha B crystallin.

Scientific Background: HSP25 is the mouse homologue of the human HSP27 protein, a member of the small heat shock protein family comprised of a diverse group of proteins from ~15 to >30kDa(1). The basic structure of most sHSPs is a homologous and highly conserved amino acid sequence, with an α-crystallin-domain at the C-terminus and the WD/EPF domain at the less conserved N-terminus. This N-terminus is essential for the development of high molecular oligomers (2, 3). HSP27-oligomers consist of stable dimers formed by as many as 8-40 HSP27 protein monomers (4). The oligomerization status is connected with the chaperone activity: aggregates of large oligomers have high chaperone activity, whereas dimers have no chaperone activity (5). HSP27 is localized to the cytoplasm of unstressed cells but can redistribute to the nucleus in response to stress, where it may function to stabilize DNA and/or the nuclear membrane. It can be rapidly phosphorylated in response to physiological stimuli relevant to the cell type examined. Thus, HSP27 has been suggested to be an important intermediate in second messenger-mediated signaling pathways (6). Other functions include chaperone activity (as mentioned above), thermo-tolerance in vivo, inhibition of apoptosis, and signal transduction. Specifically, in vitro, it acts as an ATP-independent chaperone by inhibiting protein aggregation and by stabilizing partially denatured proteins, which ensures refolding of the HSP70 complex. HSP27 is also involved in the apoptotic signaling pathway because it interferes with the activation of cytochrome c/Apaf-1/dATP complex, thereby inhibiting the activation of procaspase-9. It is also hypothesized that HSP27 may serve some role in cross-bridge formation between actin and myosin (7). And finally, HSP27 is also thought to be involved in the process of cell differentiation. The up-regulation of HSP27 correlates with the rate of phosphorylation and with an increase of large oligomers. It is possible that HSP27 may play a crucial role in termination of growth (8). Looking for more information on HSP27? Visit our new HSP27 Scientific Resource Guide at http://www.HSP27.com.
References

[1] Welch W.J. (1985) J Biol. Chem. 260: 3058-3062.

[2] Kim K.K., Kim R., and Kim S. (1998) Nature 394(6693): 595-599.

[3] Van Montfort R., Slingsby C., and Vierling E. (2001) Addv Protein Chem. 59: 105-56.

[4] Ehrnsperger M., Graber S., Gaestel M. and Buchner J. (1997) EMBO J. 16: 221-229.

[5] Ciocca D.R., Oesterreich S., Chamness G.C., McGuire W.L., and Fugua S.A. (1993) J Natl Cancer Inst. 85 (19): 1558-70.

[6] Welsh M.J., Wu W., Parvinem M., and Gilmont R.R. (1996) Biol. Of Reprod. 55: 141-151.

[7] Sarto C. Binnz P.A. and Mocarelli P. (2000) Electrophoresis. 21(6): 1218-26.

[8] Arrigo A.P. (2005) J Cell Biochem. 94(2): 241-6.

[9] Jia, Y. et al. (2001) J. Biol. Chem. 276(43):39911-39918.