Labelling Review row-Online

Heat Shock Protein 27
Clone 2B4
1 mL lyophilized NCL-HSP27 FPW
Prokaryotes and eukaryotes express a variety of heat shock proteins (Hsps)
in response to stress, including sublethal heat shock, exposure to heavy
metals, hormones and viral infection. Hsp27 (27 kD) is the most common
small Hsp found in man. In breast tissue, it is reported that expression of
Hsp27 is taken as evidence of a functional estrogen receptor pathway.
Human breast carcinoma: immunohistochemical staining for Hsp27 using NCL-HSP27.
Note intense cytoplasmic staining of tumor cells. Paraffin section.
Heat Shock Protein 70
Clone 8B11
1 mL lyophilized NCL-HSP70 P (HIER)
The response of cells or organisms to stress, such as exposure to heat or
chemicals, is associated with the induction of heat shock proteins. Heat
shock protein 70 (Hsp70) is reported to have a protective role in ischemic
disease, inflammation, infection and a potential role in antigen processing
as well as a possible regulatory role in cytokine biosynthesis. Hsp70 exists in
the cell in equilibrium between its free state, in the cytoplasm, and its bound
state, protecting proteins in the nucleolus, perhaps either by helping refold
some of the unfolded ribosomal proteins or by solubilizing the denatured
ribosomal proteins to facilitate their turnover. During recovery from heat
shock and as the nucleoli begin to return to their normal activities, most of
the Hsp70 returns to the cytoplasm.
Product Specific Information
NCL-HSP70 is reactive with Hsp70 and heat shock cognate 70 (Hsc70) in man,
mouse and rat.
Heat Shock Protein 90
Clone JPB24
1 mL lyophilized NCL-HSP90 P (HIER) W
Heat shock proteins are highly conserved proteins in nearly all organisms
and are induced by various kinds of stress, including non-physiological
temperatures. Heat shock protein 90 (Hsp90) is associated with the folding
of signal-transducing proteins such as steroid hormone receptors and
protein kinases. Hsp90 forms several discrete subcomplexes, each
containing distinct groups of co-chaperones that function in these folding
pathways. Hsp90 has been reported to be expressed in epithelial cells,
mononuclear cells, giant cells, nerve cells and endothelial cells of small
vessels. Hsp90 expression has been reported to be correlated with sex
steroid receptor status in endometrial carcinomas. In breast cancer, MHC
class I expression is reported to correlate with nuclear localization of Hsp90.
Heat Shock Protein 105
Clone 58F12
1 mL lyophilized NCL-HSP105 P (HIER) W
Heat shock protein 105 (Hsp105) exists as two isoforms; alpha and beta
which belong to the Hsp105/Hsp110 protein family. Hsp105 acts as both a
chaperone to prevent thermal aggregation of proteins and as a regulator of
mammalian cells. The Hsp105 isoforms are reported to be found in the
cytoplasm but not in the nucleoli under non-stressed and stressed conditions.
In rodents, Hsp105 isoforms are reported to be moderately expressed
in the adrenal glands, spleen, liver and heart and both are markedly
increased after heat shock. In the testis, Hsp105 is specifically localized in
the cytoplasm of germ cells but may translocate to the nucleus after heat
shock. The most abundant expression of Hsp105 occurs in the brain with
nuclear and cytoplasmic expression in nearly all neurons, oligodendrocytes,
microglia and astrocytes. Increased expression reported during
embryogenesis suggests that Hsp105 may have an important role during
mouse development.
Human brain, cerebellum: immunohistochemical staining for heat shock protein 105 using
NCL-HSP105. Note intense cytoplasmic and nuclear staining of Purkinje cells and neuronal
processes. Paraffin section.
F Frozen I Immunofluorescence E Electron microscopy
P Paraffin C Flow cytometry O Other applications
W Western blotting
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Primary Antibodies