Product Details
| Alternative Name: | HspB1, Heat shock protein 27 |
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| MW: | ~27kDa |
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| Source: | Produced in E. coli. |
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| UniProt ID: | P04792 |
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| GenBank ID: | L39370 |
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| Formulation: | Liquid. In 60mM Tris-HCl, pH 7.5, containing 5mM sodium chloride, 1mM EGTA, 0.5mM EDTA, 15mM DTT, 0.1mM ATP, and 15mM magnesium chloride. |
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| Purity: | ≥90% (SDS-PAGE; Western blot) |
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| Purity Detail: | Purified by multi-step chromatography. |
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| Applications: | WB
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| Application Notes: | Western blot control. |
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| Shipping: | Shipped on Dry Ice |
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| Long Term Storage: | -80°C |
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| Scientific Background: | 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 aB-crystallin. It is characterized by a conserved C-terminal a-crystallin domain consisting of two antiparallel β-sheets that promote oligomer formation required for its primary chaperone function as inhibitors of irreversible protein aggregation. Hsp27 oligomerization is modulated by post-translational phosphorylation of Hsp27 at three serine residues, Ser-15, Ser-78, and Ser-82, by a variety of protein kinases including MAPKAPK-3, PKAcα, p70S6K, PKD I, and PKCδ. Hsp27 has been shown to inhibit actin polymerization by binding of unphosphorylated Hsp27 monomers to actin intermediate filaments. Antiapoptotic 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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| Regulatory Status: | RUO - Research Use Only |
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Western Blot analysis: Lane 1: MWM, Lane 2: Hsp27 (phospho) protein, probed with Hsp27 (pSer82) pAb
SDS-PAGE analysis: Lane 1: MW marker, Lane 2: 0.5µg, Lane 3: 1µg, Lane 4: 2µg, Lane 5: 5µg Hsp27 (phospho) protein
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Product Literature References
Monocyte Proteomics Reveals Involvement of Phosphorylated HSP27 in the Pathogenesis of Osteoporosis: B. Daswani, et al.; Disease Markers
2015, 196589 (2015),
Application(s): Cell Culture, Assay,
Abstract;
Full Text
Release of Phosphorylated HSP27 (HSPB1) from Platelets Is Accompanied with the Acceleration of Aggregation in Diabetic Patients: H. Tokuda, et al.; PLoS One
10, e0128977 (2015),
Application(s): Cell Culture,
Abstract;
Full Text
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