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AB190314

Anti-Hsp27 antibody [6H11]

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(1 Publication)

Mouse Monoclonal Hsp27 antibody. Suitable for WB, ICC/IF and reacts with Human samples. Cited in 1 publication. Immunogen corresponding to Recombinant Full Length Protein corresponding to Human HSPB1.

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

3 Images
Immunocytochemistry/ Immunofluorescence - Anti-Hsp27 antibody [6H11] (AB190314)
  • ICC/IF

Supplier Data

Immunocytochemistry/ Immunofluorescence - Anti-Hsp27 antibody [6H11] (AB190314)

Immunofluorescence analysis of HeLa (human epithelial cell line from cervix adenocarcinoma) cells stained for Hsp27 using ab190314 at 1/2000 dilution (green) and costained with chicken polyclonal antibody to Hsp60 at 1/2000 dilution (red). Counter-stained with DAPI.

Immunocytochemistry/ Immunofluorescence - Anti-Hsp27 antibody [6H11] (AB190314)
  • ICC/IF

Supplier Data

Immunocytochemistry/ Immunofluorescence - Anti-Hsp27 antibody [6H11] (AB190314)

Immunofluorescent analysis of HeLa cells labeling Hsp27 with ab190314 at 1/1000 dilution (red), and counterstained with chicken polyclonal antibody to Vimentin (green) and DNA (blue).

Western blot - Anti-Hsp27 antibody [6H11] (AB190314)
  • WB

Supplier Data

Western blot - Anti-Hsp27 antibody [6H11] (AB190314)

All lanes:

Western blot - Anti-Hsp27 antibody [6H11] (ab190314) at 1/10000 dilution

Lane 1:

Protein standard

Lane 2:

Rat brain lysate

Lane 3:

Mouse brain lysate

Lane 4:

NIH/3T3 (mouse embryo fibroblast cell line) cell lysate

Lane 5:

HEK-293 (human epithelial cell line from embryonic kidney) cell lysate

Lane 6:

HeLa (human epithelial cell line from cervix adenocarcinoma) cell lysate

Predicted band size: 23 kDa

false

Key facts

Host species

Mouse

Clonality

Monoclonal

Clone number

6H11

Isotype

IgG1

Carrier free

No

Reacts with

Human

Applications

WB, ICC/IF

applications

Immunogen

Recombinant Full Length Protein corresponding to Human HSPB1.

P04792

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "WB" : {"fullname" : "Western blot", "shortname":"WB"}, "ICCIF" : {"fullname" : "Immunocytochemistry/ Immunofluorescence", "shortname":"ICC/IF"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Human": { "WB-species-checked": "testedAndGuaranteed", "WB-species-dilution-info": "1/10000", "WB-species-notes": "<p></p>", "ICCIF-species-checked": "testedAndGuaranteed", "ICCIF-species-dilution-info": "1/1000", "ICCIF-species-notes": "<p></p>" } } }
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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein G
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
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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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Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:
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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 (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
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Publications (1)

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

Nature communications 9:2702 PubMed30006572

2018

ATP synthase F subunits recruited to centromeres by CENP-A are required for male meiosis.

Applications

Unspecified application

Species

Unspecified reactive species

Caitríona M Collins,Beatrice Malacrida,Colin Burke,Patrick A Kiely,Elaine M Dunleavy
View all publications
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Product promise

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