Application
| WB, IHC, ICC, IP, FC |
|---|---|
| Primary Accession | P04792 |
| Other Accession | NP_001532.1 |
| Host | Mouse |
| Isotype | IgG1 Kappa |
| Reactivity | Human, Mouse, Rat, Hamster, Bovine, Sheep, Guinea Pig, Dog |
| Clonality | Monoclonal |
| Description | Mouse Anti-Human HSP25/HSP27 Monoclonal IgG1 Kappa |
| Target/Specificity | Detects ~25kDa or ~27kDa. Recognizes HSP25 and HSP27, cross reacts with alpha B crystallin. |
| Other Names | HSPB2 Antibody, Heat shock protein beta-2 Antibody, HSPB2 Antibody, DMPK-binding protein Antibody, MKBP Antibody |
| Clone Names | 8A7 |
| Immunogen | HSP27 peptide |
| Purification | Protein G Purified |
| Storage | -20ºC |
| Storage Buffer | PBS, 50% glycerol, 0.09% sodium azide |
| Shipping Temperature | Blue Ice or 4ºC |
| Certificate of Analysis | A 1:5000 dilution of SMC-114 was sufficient for detection of HSP27 in 20 µg of HeLa cell lysate by ECL immunoblot analysis. |
| Cellular Localization | Cytoplasm | Nucleus | Cytoskeleton | Spindle |
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Provided below are standard protocols that you may find useful for product applications.
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). For more information visit our 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.