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AB48740

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

2 Images
Western blot - Recombinant Human Hsp27 protein (Tag Free) (AB48740)
  • 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 - Recombinant Human Hsp27 protein (Tag Free) (AB48740)
  • 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.

Key facts

Purity

>95% SDS-PAGE

Expression system

Escherichia coli

Tags

Tag free

Applications

SDS-PAGE, WB

applications

Biologically active

No

Accession

P04792

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.4 Constituents: 0.75% Potassium chloride, 0.476% HEPES, 0.0154% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p>ab48740 can be used as a WB positive control in conjunction with <a href='/en-us/products/unavailable/hsp27-antibody-ab78806'>ab78806</a>.</p>" }, "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p>Predicted molecular weight of 22.7kDa.</p>" } } }

Sequence info

[{"sequence":"MTERRVPFSLLRGPSWDPFRDWYPHSRLFDQAFGLPRLPEEWSQWLGGSSWPGYVRPLPPAAIESPAVAAPAYSRALSRQLSSGVSEIRHTADRWRVSLDVNHFAPDELTVKTKDGVVEITGKHEERQDEHGYISRCFTRKYTLPPGVDPTQVSSSLSPEGTLTVEAPMPKLATQSNEITIPVTFESRAQLGGPEAAKSDETAAK","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P04792","tags":[]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

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.

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

Product protocols

Target data

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).
See full target information HSPB1

Publications (5)

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

Physiological reports 11:e15788 PubMed37985159

2023

Geranylgeranylacetone reduces cardiomyocyte stiffness and attenuates diastolic dysfunction in a rat model of cardiometabolic syndrome.

Applications

Unspecified application

Species

Unspecified reactive species

Mark T Waddingham,Vasco Sequeira,Diederik W D Kuster,Elisa Dal Canto,M Louis Handoko,Frances S de Man,Denielli da Silva Gonçalves Bós,Coen A Ottenheijm,Shengyi Shen,Robbert J van der Pijl,Jolanda van der Velden,Walter J Paulus,Etto C Eringa

Molecular oncology 16:2537-2557 PubMed35064619

2022

TLK1-mediated MK5-S354 phosphorylation drives prostate cancer cell motility and may signify distinct pathologies.

Applications

Unspecified application

Species

Unspecified reactive species

Md Imtiaz Khalil,Vibha Singh,Judy King,Arrigo De Benedetti

Cancers 12: PubMed33297404

2020

NEK1 Phosphorylation of YAP Promotes Its Stabilization and Transcriptional Output.

Applications

Unspecified application

Species

Unspecified reactive species

Md Imtiaz Khalil,Ishita Ghosh,Vibha Singh,Jing Chen,Haining Zhu,Arrigo De Benedetti

Science advances 6: PubMed33188023

2020

The structure-function relationship of oncogenic LMTK3.

Applications

Unspecified application

Species

Unspecified reactive species

Angeliki Ditsiou,Chiara Cilibrasi,Nikiana Simigdala,Athanasios Papakyriakou,Leanne Milton-Harris,Viviana Vella,Joanne E Nettleship,Jae Ho Lo,Shivani Soni,Goar Smbatyan,Panagiota Ntavelou,Teresa Gagliano,Maria Chiara Iachini,Sahir Khurshid,Thomas Simon,Lihong Zhou,Storm Hassell-Hart,Philip Carter,Laurence H Pearl,Robin L Owen,Raymond J Owens,S Mark Roe,Naomi E Chayen,Heinz-Josef Lenz,John Spencer,Chrisostomos Prodromou,Apostolos Klinakis,Justin Stebbing,Georgios Giamas

The Journal of cell biology 204:187-202 PubMed24421331

2014

Human myocytes are protected from titin aggregation-induced stiffening by small heat shock proteins.

Applications

Unspecified application

Species

Unspecified reactive species

Sebastian Kötter,Andreas Unger,Nazha Hamdani,Patrick Lang,Matthias Vorgerd,Luitgard Nagel-Steger,Wolfgang A Linke
View all publications

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