Product Name: HSP27
Product Number: AB-NN152-2
| Size: | 50 µg | Price: | 89.00 | |
| $US |
Target Full Name: Heat shock protein beta-1
Target Alias: 28k Da heat shock protein; CMT2F; HSP25; HSP27; HSP28; HSPB1; SRP27
Product Type Specific: Heat shock/stress protein pan-specific antibody
Antibody Code: NN152-2
Antibody Target Type: Pan-specific
Protein UniProt: P04792
Protein SigNET: P04792
Antibody Type: Polyclonal
Antibody Host Species: Rabbit
Antibody Ig Isotype Clone: N/A
Antibody Immunogen Source: Human HSP27, His tagged
Target Alias: 28k Da heat shock protein; CMT2F; HSP25; HSP27; HSP28; HSPB1; SRP27
Product Type Specific: Heat shock/stress protein pan-specific antibody
Antibody Code: NN152-2
Antibody Target Type: Pan-specific
Protein UniProt: P04792
Protein SigNET: P04792
Antibody Type: Polyclonal
Antibody Host Species: Rabbit
Antibody Ig Isotype Clone: N/A
Antibody Immunogen Source: Human HSP27, His tagged
Production Method: Protein A purified
Antibody Modification: Unconjugated. Contact KInexus if you are interest in having the antibody biotinylated or coupled with fluorescent dyes.
Antibody Concentration: 1.4 mg/ml
Storage Buffer: Phosphate buffered saline pH7.4, 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 | ICC/Immunofluorescence
Antibody Dilution Recommended: WB (1:2000); optimal dilutions for assays should be determined by the user.
Antibody Modification: Unconjugated. Contact KInexus if you are interest in having the antibody biotinylated or coupled with fluorescent dyes.
Antibody Concentration: 1.4 mg/ml
Storage Buffer: Phosphate buffered saline pH7.4, 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 | ICC/Immunofluorescence
Antibody Dilution Recommended: WB (1:2000); optimal dilutions for assays should be determined by the user.
Antibody Potency: Detects a ~27 kDa protein in cell and tissue lysates by Western blotting.
Antibody Species Reactivity: Human | Mustelus antarcticus (Shark) | Galeorhinus galeus (Shark)
Antibody Positive Control: A 1:2000 dilution of SPC-106 was sufficient for detection of HSP27 in 20 µg of HeLa cell lysate by ECL immunoblot analysis.
Related Product 1: HSP27 pan-specific antibody (Cat. No.: AB-NN152-3)
Antibody Species Reactivity: Human | Mustelus antarcticus (Shark) | Galeorhinus galeus (Shark)
Antibody Positive Control: A 1:2000 dilution of SPC-106 was sufficient for detection of HSP27 in 20 µg of HeLa cell lysate by ECL immunoblot analysis.
Related Product 1: HSP27 pan-specific antibody (Cat. No.: AB-NN152-3)
Scientific Background: HSP27s belong to an abundant and ubiquitous family of small heat shock proteins (sHSP). It is an important HSP found in both normal human cells and cancer cells. 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 (1, 2). HSP27-oligomers consist of stable dimers formed by as many as 8-40 HSP27 protein monomers (3). The oligomerization status is connected with the chaperone activity: aggregates of large oligomers have high chaperone activity, whereas dimers have no chaperone activity (4). 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. 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 (5). 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 (6). Looking for more information on HSP27? Visit our new HSP27 Scientific Resource Guide at http://www.HSP27.com.
References
[1] Kim K.K., Kim R., and Kim, S. (1998) Nature 394(6693): 595-599.
[2] Van Montfort R., Slingsby C., and Vierling E. (2001) Addv Protein Chem. 59: 105-56.
[3] Ehrnsperger M., Graber S., Gaestel M. and Buchner J. (1997) EMBO J. 16: 221-229.
[4] Ciocca D.R., Oesterreich S., Chamness G.C., McGuire W.L., and Fugua S.A. (1993) J Natl Cancer Inst. 85 (19): 1558-70.
[5] Sarto C., Binnz P.A., and Mocarelli P. (2000) Electrophoresis. 21(6): 1218-26.
[6] Arrigo A.P. (2005) J Cell Biochem. 94(2): 241-6.
[1] Kim K.K., Kim R., and Kim, S. (1998) Nature 394(6693): 595-599.
[2] Van Montfort R., Slingsby C., and Vierling E. (2001) Addv Protein Chem. 59: 105-56.
[3] Ehrnsperger M., Graber S., Gaestel M. and Buchner J. (1997) EMBO J. 16: 221-229.
[4] Ciocca D.R., Oesterreich S., Chamness G.C., McGuire W.L., and Fugua S.A. (1993) J Natl Cancer Inst. 85 (19): 1558-70.
[5] Sarto C., Binnz P.A., and Mocarelli P. (2000) Electrophoresis. 21(6): 1218-26.
[6] Arrigo A.P. (2005) J Cell Biochem. 94(2): 241-6.
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