Recombinant Human Hsp27 protein (Tag Free)
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(5 Publications)
Recombinant Human Hsp27 protein (Tag Free) is a Human Full Length protein, expressed in Escherichia coli, with >95%, suitable for WB, SDS-PAGE.
View Alternative Names
HSP27, HSP28, HSPB1, Heat shock protein beta-1, HspB1, 28 kDa heat shock protein, Estrogen-regulated 24 kDa protein, Heat shock 27 kDa protein, Heat shock protein family B member 1, Stress-responsive protein 27, HSP 27, SRP27
- WB
Unknown
Western blot - Recombinant Human Hsp27 protein (Tag Free) (AB48740)
All lanes:
Anti-Hsp27 antibody (<a href='/en-us/products/unavailable/hsp27-antibody-ab78806'>ab78806</a>) at 1 µg/mL
Lane 1:
Western blot - Recombinant Human Hsp27 protein (Tag Free) (ab48740) at 0.01 µg
Lane 2:
Western blot - Recombinant Human Hsp27 protein (Tag Free) (ab48740) at 0.001 µg
Secondary
All lanes:
Western blot - Goat Anti-Rabbit IgG H&L (HRP) preadsorbed (<a href='/en-us/products/secondary-antibodies/goat-rabbit-igg-h-l-hrp-preadsorbed-ab97080'>ab97080</a>) at 1/5000 dilution
true
Exposure time: 4min
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human Hsp27 protein (Tag Free) (AB48740)
3ug by SDS-PAGE under reducing conditions and visualized by coomassie blue stain.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Hsp27 plays a critical role in cellular stress response by regulating actin cytoskeleton dynamics and inhibiting apoptosis. It forms part of a complex that includes other proteins such as alphaB-crystallin. This complex facilitates the reorganization of proteins under stress conditions enhancing cell survival during oxidative stress or thermal shock. Hsp27 also modulates inflammatory responses and has been shown to affect cell migration.
Pathways
Hsp27 integrates into the apoptosis and inflammation pathways. It interacts with apoptotic machinery such as caspase proteins to protect cells by hindering apoptosome formation. Additionally Hsp27 can engage with pathways involving the nuclear factor-kappa B (NF-kB) impacting inflammatory signaling. CPTC (carboxyl-pyrene-trioctylamine) can modulate these pathways by altering Hsp27 function and interactions.
Specifications
Form
Liquid
Additional notes
Recombinant human Hsp27 was overexpressed in E. coli and purified by conventional chromatography.
General info
Function
Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state (PubMed : 10383393, PubMed : 20178975). Plays a role in stress resistance and actin organization (PubMed : 19166925). Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins (PubMed : 23728742).
Sequence similarities
Belongs to the small heat shock protein (HSP20) family.
Post-translational modifications
Phosphorylated upon exposure to protein kinase C activators and heat shock (PubMed:8325890). Phosphorylation by MAPKAPK2 and MAPKAPK3 in response to stress dissociates HSPB1 from large small heat-shock protein (sHsps) oligomers and impairs its chaperone activity and ability to protect against oxidative stress effectively. Phosphorylation by MAPKAPK5 in response to PKA stimulation induces F-actin rearrangement (PubMed:1332886, PubMed:19166925, PubMed:8093612).
Subcellular localisation
Nucleus
Target data
Publications (5)
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Physiological reports 11:e15788 PubMed37985159
2023
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Unspecified reactive species
Molecular oncology 16:2537-2557 PubMed35064619
2022
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Cancers 12: PubMed33297404
2020
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Science advances 6: PubMed33188023
2020
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Unspecified reactive species
The Journal of cell biology 204:187-202 PubMed24421331
2014
Applications
Unspecified application
Species
Unspecified reactive species
Product promise
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