H8158
Heat Shock Protein 27 human
recombinant, expressed in E. coli, buffered aqueous solution
Synonym(s):
HSP 27
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About This Item
UNSPSC Code:
12352200
biological source
human
Quality Level
recombinant
expressed in E. coli
assay
~90% (SDS-GE)
form
buffered aqueous solution
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... HSPB1(3315)
Biochem/physiol Actions
Heat shock proteins (HSPs) are molecular chaperones. They prevent aggregation of unfolded proteins. HSP27 is involved in anti-apoptosis and actin, and microtubule stabilization. It exists in unphosphorylated inactive form and phosphorylated active form.[1] In monocytes, phosphorylated HSP27 is associated with bone mineral density and can contribute to the pathogenesis of osteoporosis.[2] It also participates in iron metabolism and negatively regulates ferroptosis-associated cancer cell death.[3]
Physical form
Solution in 20 mM Tris HCl, pH 7.5, 10 mM NaCl, 1 mM EDTA, 1 mM DTT
Storage Class
12 - Non Combustible Liquids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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Haruhiko Tokuda et al.
PloS one, 10(6), e0128977-e0128977 (2015-06-06)
We investigated the relationship between HSP27 phosphorylation and collagen-stimulated activation of platelets in patients with diabetes mellitus (DM). Platelet-rich plasma was prepared from blood of type 2 DM patients. The platelet aggregation was analyzed in size of aggregates by an
Monocyte Proteomics Reveals Involvement of Phosphorylated HSP27 in the Pathogenesis of Osteoporosis.
Bhavna Daswani et al.
Disease markers, 2015, 196589-196589 (2015-06-13)
Peripheral monocytes, precursors of osteoclasts, have emerged as important candidates for identifying proteins relevant to osteoporosis, a condition characterized by low Bone Mineral Density (BMD) and increased susceptibility for fractures. We employed 4-plex iTRAQ (isobaric tags for relative and absolute
K Engel et al.
Biomedica biochimica acta, 50(9), 1065-1071 (1991-01-01)
A hybrid protein containing the N-terminal part of the murine stress protein hsp25 (amino acids 1 to 110) and the C-terminal part of the human stress protein hsp27 (amino acids 111 to 208) was expressed in E. coli using a
X Sun et al.
Oncogene, 34(45), 5617-5625 (2015-03-03)
Ferroptosis is an iron-dependent form of non-apoptotic cell death, but its molecular mechanism remains largely unknown. Here, we demonstrate that heat shock protein beta-1 (HSPB1) is a negative regulator of ferroptotic cancer cell death. Erastin, a specific ferroptosis-inducing compound, stimulates
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