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Hsp27 is one of the most common members of the highly conserved and ubiquitously expressed family of small heat shock proteins (sHsp), which also includes alphaB-crystallin. It is characterized by a conserved C-terminal alpha-crystallin domain consisting of two anti-parallel beta-sheets that promote oligomer formation required for its primary chaperone function as inhibitor of irreversible protein aggregation. Hsp27 oligomerization is modulated by post-translational phosphorylation of Hsp27 at three serine residues, Ser15, Ser78, and Ser82, by a variety of protein kinases including MAPKAPK-3, PKAc-alpha, p70 S6K, PKD I, and PKC-delta. Hsp27 has been shown to inhibit actin polymerization by binding of unphosphorylated Hsp27 monomers to actin intermediate filaments. Anti-apoptotic functions of Hsp27 have also been identified through interactions with DAXX7, activation of Akt, and inhibition of apoptosome formation. Evidence suggests altered expression of Hsp27 is implicated in the pathogenesis of breast, ovarian, and prostate cancer.
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Western blot analysis of HSP27 pAb: Lane 1: MW marker, Lane 2: HSP27 Recombinant Human Protein, Lane 3: HSP25 Recombinant Murine Protein (Negative Control), Lane 4: HeLa, Lane 5: HeLa, Heat Shocked, Lane 6: Vero, Heat Shocked, Lane 7: 3T3, Heat Shocked, Lane 8: PC-12, Heat Shocked.
Immunohistochemistry analysis of human heart tissue stained with HSP27, pAb at 10µg/ml.
Molecular effects of HSP90 inhibition by 17‐AAG on HSP90 client proteins in parental and resistant cell lines. MDA‐435 parental and resistant MDA‐435R cells treated with 0.1 μm of 17‐AAG (~ 5 × 17‐AAG IC50 concentrations of the parental cell line) (A) and with 30 μm of 17‐AAG (~ 5 × 17‐AAG IC50 concentrations of the resistant cell line) (B). MDA‐231 parental and resistant MDA‐231R cells treated with 5.0 μm of 17‐AAG (~ 5 × 17‐AAG IC50 concentrations of the parental cell line) (C) and with 50 μm of 17‐AAG (~ 5 × 17‐AAG IC50 concentrations of the resistant cell line) (D). Total cell lysates were collected at the indicated time‐points and analysed by western blotting.
Image collected and cropped by CiteAb under a CC-BY license from the following publication: Histone deacetylase activity mediates acquired resistance towards structurally diverse HSP90 inhibitors. Mol Oncol (2017)
Molecular effects of HSP90 inhibition by 17‐AAG on HSP90 client proteins in parental and resistant cell lines. MDA‐435 parental and resistant MDA‐435R cells treated with 0.1 μm of 17‐AAG (~ 5 × 17‐AAG IC50 concentrations of the parental cell line) (A) and with 30 μm of 17‐AAG (~ 5 × 17‐AAG IC50 concentrations of the resistant cell line) (B). MDA‐231 parental and resistant MDA‐231R cells treated with 5.0 μm of 17‐AAG (~ 5 × 17‐AAG IC50 concentrations of the parental cell line) (C) and with 50 μm of 17‐AAG (~ 5 × 17‐AAG IC50 concentrations of the resistant cell line) (D). Total cell lysates were collected at the indicated time‐points and analysed by western blotting.
Image collected and cropped by CiteAb under a CC-BY license from the following publication: Histone deacetylase activity mediates acquired resistance towards structurally diverse HSP90 inhibitors. Mol Oncol (2017)
Molecular effects of HSP90 inhibition by 17‐AAG on HSP90 client proteins in parental and resistant cell lines. MDA‐435 parental and resistant MDA‐435R cells treated with 0.1 μm of 17‐AAG (~ 5 × 17‐AAG IC50 concentrations of the parental cell line) (A) and with 30 μm of 17‐AAG (~ 5 × 17‐AAG IC50 concentrations of the resistant cell line) (B). MDA‐231 parental and resistant MDA‐231R cells treated with 5.0 μm of 17‐AAG (~ 5 × 17‐AAG IC50 concentrations of the parental cell line) (C) and with 50 μm of 17‐AAG (~ 5 × 17‐AAG IC50 concentrations of the resistant cell line) (D). Total cell lysates were collected at the indicated time‐points and analysed by western blotting.
Image collected and cropped by CiteAb under a CC-BY license from the following publication: Histone deacetylase activity mediates acquired resistance towards structurally diverse HSP90 inhibitors. Mol Oncol (2017)
Molecular effects of HSP90 inhibition by 17‐AAG on HSP90 client proteins in parental and resistant cell lines. MDA‐435 parental and resistant MDA‐435R cells treated with 0.1 μm of 17‐AAG (~ 5 × 17‐AAG IC50 concentrations of the parental cell line) (A) and with 30 μm of 17‐AAG (~ 5 × 17‐AAG IC50 concentrations of the resistant cell line) (B). MDA‐231 parental and resistant MDA‐231R cells treated with 5.0 μm of 17‐AAG (~ 5 × 17‐AAG IC50 concentrations of the parental cell line) (C) and with 50 μm of 17‐AAG (~ 5 × 17‐AAG IC50 concentrations of the resistant cell line) (D). Total cell lysates were collected at the indicated time‐points and analysed by western blotting.
Image collected and cropped by CiteAb under a CC-BY license from the following publication: Histone deacetylase activity mediates acquired resistance towards structurally diverse HSP90 inhibitors. Mol Oncol (2017)
| Regulatory Status |
RUO – Research Use Only |
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Related Products
| Application | ELISA, WB |
|---|---|
| Host | Goat |
| Species Reactivity | Rabbit |