HSP27 Antibody (6H11) [DyLight 594] Summary
Immunogen |
Recombinant full length human HSP27 expressed in and purified from E. coli. [UniProt# P04792] |
Localization |
Cytoplasm. Nucleus. Cytoplasm > cytoskeleton > spindle. |
Isotype |
IgG1 |
Clonality |
Monoclonal |
Host |
Mouse |
Gene |
HSPB1 |
Purity |
Immunogen affinity purified |
Innovator's Reward |
Test in a species/application not listed above to receive a full credit towards a future purchase. |
Applications/Dilutions
Dilutions |
- CyTOF-ready
- Flow Cytometry
- Immunocytochemistry/ Immunofluorescence
- Immunohistochemistry
- Knockout Validated
- Western Blot
|
Application Notes |
Optimal dilution of this antibody should be experimentally determined. |
Reactivity Notes
Packaging, Storage & Formulations
Storage |
Store at 4C in the dark. |
Buffer |
50mM Sodium Borate |
Preservative |
0.05% Sodium Azide |
Purity |
Immunogen affinity purified |
Notes
DyLight (R) is a trademark of Thermo Fisher Scientific Inc. and its subsidiaries.
Alternate Names for HSP27 Antibody (6H11) [DyLight 594]
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 approx. 15 to >30kDa(1). The basic structure of most sHsps is a homologous and highly conserved amino acid sequence, with an alpha-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), thermotolerance 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).
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are
guaranteed for 1 year from date of receipt.
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