JavaScript is disabled in your browser. Please enable JavaScript to view this website.
AB245922

Recombinant Human Hsp27 protein

Be the first to review this product! Submit a review

|

(0 Publication)

Recombinant Human Hsp27 protein is a Human Full Length protein, in the 1 to 205 aa range, expressed in Escherichia coli, with >90%, suitable for 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

1 Images
SDS-PAGE - Recombinant Human Hsp27 protein (AB245922)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human Hsp27 protein (AB245922)

SDS-PAGE analysis of Recombinant Human Hsp27 protein (ab245922)

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

Tag free

Applications

SDS-PAGE

applications

Biologically active

No

Accession

P04792

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.5 Constituents: 10% Glycerol (glycerin, glycerine), 2.61% Sodium chloride, 0.32% Tris HCl, 0.08% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

style
left-column

Complementary Products

Secondary Antibodies

AB150077

Goat Anti-Rabbit IgG H&L (Alexa Fluor® 488)

Immunocytochemistry/ Immunofluorescence - Goat Anti-Rabbit IgG H&L (Alexa Fluor® 488) (AB150077)

  • 5
  • 20
Proteins & Peptides

AB48779

Recombinant Human Alpha B Crystallin protein

Western blot - Recombinant Human Alpha B Crystallin protein (AB48779)

  • 5
  • 1
Primary Antibodies

AB109376

Anti-Hsp27 antibody [EPR5477]

RabMAb|Recombinant|KO Validated

Flow Cytometry (Intracellular) - Anti-Hsp27 antibody [EPR5477] (AB109376)

  • 5
  • 2
Proteins & Peptides

AB78434

Recombinant human Hsp70 protein (Active)

Bioactive

SDS-PAGE - Recombinant human Hsp70 protein (Active) (AB78434)

  • 0
  • 0
style
left-column

Reactivity data

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

Sequence info

[{"sequence":"MTERRVPFSLLRGPSWDPFRDWYPHSRLFDQAFGLPRLPEEWSQWLGGSSWPGYVRPLPPAAIESPAVAAPAYSRALSRQLSSGVSEIRHTADRWRVSLDVNHFAPDELTVKTKDGVVEITGKHEERQDEHGYISRCFTRKYTLPPGVDPTQVSSSLSPEGTLTVEAPMPKLATQSNEITIPVTFESRAQLGGPEAAKSDETAAK","proteinLength":"Full Length","predictedMolecularWeight":"27 kDa","actualMolecularWeight":null,"aminoAcidEnd":205,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P04792","tags":[]}]
style
left-column

Properties and storage information

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

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.
style
left-column

Specifications

Form

Liquid

Additional notes

Affinity Purified

style
left-column

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

style
left-column

Product protocols

style
left-column

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
style
left-column
style
left-column
style
right-column

Product promise

We are committed to supporting your work with high-quality reagents, and we're here for you every step of the way. In the unlikely event that one of our products does not perform as expected, you're protected by our Product Promise.
For full details, please see our Terms & Conditions

Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.

For licensing inquiries, please contact partnerships@abcam.com