Catalog Number | Size | Price | Availability |
IW-PA1121 | 9 ml | $258 | Yes |
Description
|
The heat-shock proteins (HSPs) belong to a larger group of
polypeptides, the stress proteins, that are induced in
various combinations in response to environmental challenges
and developmental transitions. Synthesis of the small
(27-kD) HSP has been shown to be correlated with the
acquisition of thermotolerance. The deduced 199-amino acid
HSP27 protein shows sequence similarity to mammalian alpha-crystallins.
Approximately 20% of its residues are susceptible to
phosphorylation. The HSP27 gene, which is mapped to 7q11.23
and has 3 exons1, produced a 2.2-kb transcript in
an in vitro transcription assay. Decreasing ROS in cells
expressing mutant huntingtin, HSP27 protects cells against
oxidative stress2. In other words, HSP27 is a
suppressor of polyglutamine (polyQ)-mediated cell death3.
Furthermore, MAPKAPK5 is a major stress-activated kinase
that can phosphorylate HSP27 in vitro.
|
Catalog Number
|
IW-PA1121 |
Quantity
|
9 ml |
Host
|
Rabbit
|
Clone
|
Polyclonal
|
Isotype
|
IgG
|
Immunogen
|
A synthetic peptide corresponding to a sequence at the
C-terminal of human
HSP27,
different from the related mouse sequence by two amino
acids.
|
Purity
|
Immunogen affinity purified
|
Conjugate
|
Unconjugated
|
Species Reactivity
|
Human, mouse, rat.
Not tested in other species. |
Positive Control
|
Human breast cancer
|
Cellular Localization
|
Cytoplasmic
|
Form
|
Ready to use solution. No further dilution needed. Serum
blocking step should be omitted.
|
Storage
|
Store at 2-8
°C.
Do not freeze.
|
Applications
|
IHC-P: Heat induced epitope retrieval is required on
formalin fixed paraffin sections.
IHC-Fr: Not tested.
ICC: Not tested.
|
Limitations
|
This product is intended for Research Use Only.
Interpretation of the test results is solely the
responsibility of the user.
|
Precautions
|
Users should follow general laboratory precautions when
handling this product. Wear personal protective equipment to
avoid contact with skin and eyes.
|
References
|
1.Hickey, E.; Brandon, S. E.; Sadis, S.; Smale, G.; Weber,
L. A. : Molecular cloning of sequences encoding the human
heat-shock proteins and their expression during
hyperthermia. Gene 43: 147-154, 1986.
2.Wyttenbach, A.; Sauvageot, O.; Carmichael, J.; Diaz-Latoud,
C.; Arrigo, A.-P.; Rubinsztein, D. C. : Heat shock protein
27 prevents cellular polyglutamine toxicity and suppresses
the increase of reactive oxygen species caused by huntingtin.
Hum. Molec. Genet. 11: 1137-1151, 2002.
3.Wyttenbach, A.; Sauvageot, O.; Carmichael, J.; Diaz-Latoud,
C.; Arrigo, A.-P.; Rubinsztein, D. C. : Heat shock protein
27 prevents cellular polyglutamine toxicity and suppresses
the increase of reactive oxygen species caused by huntingtin.
Hum. Molec. Genet. 11: 1137-1151, 2002.
4.New, L.; Jiang, Y.; Zhao, M.; Liu, K.; Zhu, W.; Flood, L.
J.; Kato, Y.; Parry, G. C. N.; Han, J. :
PRAK, a novel protein kinase regulated by the p38 MAP kinase.
EMBO J. 17: 3372-3384, 1998.
|
Images
|
Immunohistochemical analysis of formalin fixed
paraffin-embedded human
breast cancer
using HSP27 antibody showing cytoplasmic staining.
|
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