Hsp25/Hsp27 Monoclonal Antibody (Clone 8A7)_上海惠诚生物生物试剂,标准品,仪器设备,耗材,一站式服务

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Cat. Number

070346166585439

Chemical Name

Hsp25/Hsp27 Monoclonal Antibody (Clone 8A7)

References

Synonyms

Heat Shock Protein 25/27

Formulation

Protein G affinity-purified IgG at a concentration of 1 mg/ml in PBS containing 0.09% sodium azide and 50% glycerol

Stability

1 year

Storage

-20°C

Shipping

Wet ice in continental US; may vary elsewhere

Specificity

Murine Hsp25/Hsp27	+
Rat Hsp25/Hsp27	+
Bovine Hsp25/Hsp27	+
Canine Hsp25/Hsp27	+
Guinea pig Hsp25/Hsp27	+
Hamster Hsp25/Hsp27	+
Human Hsp25/Hsp27	+

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Background Reading

Welsh, M.J., Wu, W., Parvinen, M., et al. Variation in expression of Hsp27 messenger ribonucleic acid during the cycle of the seminiferous epithelium and co-localization of Hsp27 and microfilaments in sertoli cells of the rat. Biol Reprod 55 141-151 (1996).

Welch, W.J. Phorbol ester, calcium ionophore, or serum added to quiescent rat embryo fibroblast cells all result in the elevated phosphorylation of two 28,000-dalton mammalian stress proteins. J Biol Chem 260(5) 3058-3062 (1985).

Jia, Y., Ransom, R.F., Shibanuma, M., et al. Identification and characterization of hic-5/ARA55 as an Hsp27 binding protein. J Biol Chem 276(43) 39911-39918 (2001).

Ciocca, D.R., Oesterreich, S., Chamness, G.C., et al. Biological and clinical implications of heat shock protein 27000 (Hsp27): A review. J Natl Cancer Inst 85 1558-1570 (1993).

Sarto, C., Binz, P., and Mocarelli, P. Heat shock proteins in human cancer. Electrophoresis 21 1218-1226 (2000).

Arrigo, A. In search of the molecular mechanism by which small stress proteins counteract apoptosis during cellular differentiation. J Cell Biochem 94 241-246 (2005).

Kim, K.K., Kim, R., and Kim, S. Crystal structure of a small heat-shock protein. Nature 394 595-599 (1998).

Van Montfront, R., Slingsby, C., and Vierlingt, E. Structure and function of the small heat shock protein/crystallin family of molecular chaperones. Adv Protein Chem 59 105-156 (2001).

Ehrnsperger, M., Gräber, S., Gaestel, M., et al. Binding of non-native protein to Hsp25 during heat shock creates a reservior of folding intermediates for reactivation. EMBO J 16(2) 221-229 (1997).

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Size	Global Purchasing
25 µg
100 µg

Description

Antigen: Hsp27 peptide · Clone designation: 8A7 · Host: Mouse · Application(s): WB, immunofluorescence, ICC, IP · Heat shock protein 25 (Hsp25) is the murine homologue of the human Hsp27 protein, a member of the small Hsp family comprised of a diverse group of proteins from ~15 to >30 kDa.¹ The basic structure of most Hsps 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 weight 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, 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, Hsp27 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 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

1 Welch, W.J. Phorbol ester, calcium ionophore, or serum added to quiescent rat embryo fibroblast cells all result in the elevated phosphorylation of two 28,000-dalton mammalian stress proteins. J Biol Chem 260(5) 3058-3062 (1985).

2 Kim, K.K., Kim, R., and Kim, S. Crystal structure of a small heat-shock protein. Nature 394 595-599 (1998).

3 Van Montfront, R., Slingsby, C., and Vierlingt, E. Structure and function of the small heat shock protein/crystallin family of molecular chaperones. Adv Protein Chem 59 105-156 (2001).

4 Ehrnsperger, M., Gräber, S., Gaestel, M., et al. Binding of non-native protein to Hsp25 during heat shock creates a reservior of folding intermediates for reactivation. EMBO J 16(2) 221-229 (1997).

5 Ciocca, D.R., Oesterreich, S., Chamness, G.C., et al. Biological and clinical implications of heat shock protein 27000 (Hsp27): A review. J Natl Cancer Inst 85 1558-1570 (1993).

6 Welsh, M.J., Wu, W., Parvinen, M., et al. Variation in expression of Hsp27 messenger ribonucleic acid during the cycle of the seminiferous epithelium and co-localization of Hsp27 and microfilaments in sertoli cells of the rat. Biol Reprod 55 141-151 (1996).

7 Sarto, C., Binz, P., and Mocarelli, P. Heat shock proteins in human cancer. Electrophoresis 21 1218-1226 (2000).

8 Arrigo, A. In search of the molecular mechanism by which small stress proteins counteract apoptosis during cellular differentiation. J Cell Biochem 94 241-246 (2005).

下一个：Hsf2 Monoclonal Antibody (Clone 3E2)上一个：Hsp40 Polyclonal Antibody

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