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AB92457

Recombinant Mouse Hsp27 protein

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(1 Publication)

Recombinant Mouse Hsp27 protein is a Mouse Full Length protein, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, WB.

View Alternative Names

Hsp25, Hsp27, Hspb1, Heat shock protein beta-1, HspB1, Growth-related 25 kDa protein, Heat shock 25 kDa protein, Heat shock 27 kDa protein, p25, HSP 25, HSP 27

1 Images
SDS-PAGE - Recombinant Mouse Hsp27 protein (AB92457)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Mouse Hsp27 protein (AB92457)

SDS-PAGE Analysis :
Lane 1 : Molecular weight marker
Lane 2 : 0.5 μg ab92457
Lane 3 : 1.0 μg ab92457
Lane 4 : 2.0 μg ab92457
Lane 5 : 5.0 μg ab92457

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

Tag free

Applications

SDS-PAGE, WB

applications

Biologically active

No

Accession

P14602

Animal free

No

Carrier free

No

Species

Mouse

Storage buffer

Constituents: PBS

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"P14602","tags":[]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Hsp27 also known as HSPB1 is a small heat shock protein with a molecular weight of approximately 27 kilodaltons. This protein is expressed in various tissues including muscle heart and brain. It functions as a molecular chaperone that stabilizes unfolded proteins preventing their aggregation. Hsp27 undergoes phosphorylation at specific residues which modulates its chaperone activity and interaction with other proteins.
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.

Hsp27 has connections to neurodegenerative diseases and cancer. In neurodegenerative conditions such as Alzheimer's disease its chaperone activity is thought to protect neurons from misfolded protein aggregates. In cancer Hsp27 supports tumor cell survival and resistance to chemotherapy by interacting with proteins like Akt and p53. These interactions highlight the complex role of Hsp27 in modulating cellular responses in various pathological states.
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Specifications

Form

Liquid

Additional notes

Purified by multi-step chromatography.> 90% pure as determined by SDS-PAGE and Western Blot analysis.

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General info

Function

Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state. Plays a role in stress resistance and actin organization (PubMed : 17661394). Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins (By similarity).

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 (By similarity). 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:1860870, PubMed:21575178, PubMed:8093612).

Subcellular localisation

Nucleus

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Product protocols

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Target data

Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state. Plays a role in stress resistance and actin organization (PubMed : 17661394). Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins (By similarity).
See full target information Hspb1
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Publications (1)

Recent publications for all applications. Explore the full list and refine your search

OncoTargets and therapy 11:395-408 PubMed29403285

2018

Progranulin modulates cholangiocarcinoma cell proliferation, apoptosis, and motility via the PI3K/pAkt pathway.

Applications

Unspecified application

Species

Unspecified reactive species

Minerva Daya,Watcharin Loilome,Anchalee Techasen,Malinee Thanee,Prakasit Sa-Ngiamwibool,Attapol Titapun,Puangrat Yongvanit,Nisana Namwat
View all publications
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