AB69549

Anti-Hsp104 antibody

Name: Anti-Hsp104 antibody (ab69549) | Abcam
Brand: Abcam Limited
SKU: AB69549
Price: 535 USD
Availability: InStock

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(14 Publications)

Rabbit Polyclonal Hsp104 antibody. Suitable for IP, WB and reacts with Saccharomyces cerevisiae samples. Cited in 14 publications.

View Alternative Names

Heat shock protein 104, Hsp 104, L0948

1 Images

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Western blot - Anti-Hsp104 antibody (AB69549)

All lanes:

Western blot - Anti-Hsp104 antibody (ab69549) at 1/1000 dilution

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Molecular weight marker

Lane 2:

Lysates prepared from saccharomyces cerevisiae

Predicted band size: 102 kDa

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Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

Reacts with

Saccharomyces cerevisiae

Applications

IP, WB

applications

Specificity

ab69549 detects an ~104 kDa protein, corresponding to the apparent molecular mass of Hsp104 on SDS-PAGE immunoblots, in samples from yeast (S. cerevisiae) origins. This antibody also detects an ~50 kDa band in yeast samples on immunoblot analysis. No reactivity is detected in immunoblot analysis with human, mouse, rat, monkey, and hamster proteins.

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "IP" : {"fullname" : "Immunoprecipitation", "shortname":"IP"}, "WB" : {"fullname" : "Western blot", "shortname":"WB"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Saccharomyces cerevisiae": { "IP-species-checked": "guaranteed", "IP-species-dilution-info": "", "IP-species-notes": "<p></p>", "WB-species-checked": "testedAndGuaranteed", "WB-species-dilution-info": "", "WB-species-notes": "<p></p>" } } }

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Properties and storage information

Form

Liquid

Purification technique

Affinity purification Protein A

Storage buffer

Preservative: 0.09% Sodium azide Constituents: PBS, 50% Glycerol (glycerin, glycerine)

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.

'Hsp104' also known as heat shock protein 104 is a chaperone protein found mainly in yeast but also in some bacteria. It has a molecular weight of about 104 kDa. This protein helps with the disaggregation of protein aggregates by unwinding misfolded proteins using ATP hydrolysis. You can find 'Hsp104' in the cytoplasm and nucleus of the cells where it acts to prevent protein toxicity by refolding denatured proteins. This protein plays a defensive role especially under stress conditions like heat shock by aiding cellular recovery.

Biological function summary

'Hsp104' assists in the maintenance and repair of cellular proteins under stress conditions. It is not usually part of larger complexes; instead it functions as a hexameric ring forming a powerful disaggregase. By refolding aggregated proteins 'Hsp104' enables the cell to maintain proteostasis and environmental adaptability. This activity is critical in organisms facing stressful environments allowing for survival under extreme conditions that could otherwise be fatal due to protein aggregation.

Pathways

'Hsp104' is involved in the protein quality control and stress response pathways. Its role in these pathways is important for cellular homeostasis and survival during heat shock or oxidative stress. 'Hsp104' interacts with other molecular chaperones like Hsp70 and Hsp40 which help in the initial binding and targeting of protein aggregates to 'Hsp104'. These interactions facilitate a coordinated response that ultimately leads to the restoration of cellular protein functionality.

Researchers are investigating 'Hsp104' for its potential role in neurodegenerative diseases like Huntington's disease and Parkinson's disease. These diseases are characterized by the accumulation of misfolded proteins and 'Hsp104's ability to refold and disaggregate proteins makes it a candidate of interest for therapies. Although 'Hsp104' is not naturally found in mammalian cells scientists are exploring ways to harness its properties in human cells as a treatment strategy. The protein's interactions with similar proteins such as Hsp70 highlight the complexity of protein aggregation disorders and the potential multi-faceted approach needed to address them.

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Product protocols

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

Visit the General protocols
Visit the Troubleshooting

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Target data

See full target information Hsp104

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Publications (14)

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

Current genetics 71:8 PubMed40156734

2025

Total propagation of yeast prion conformers in ssz1∆ upf1∆ Hsp104 triple mutants.

Applications

Unspecified application

Species

Unspecified reactive species

Chih-Yen King

Nature cell biology 23:1085-1094 PubMed34616026

2021

Reversible amyloids of pyruvate kinase couple cell metabolism and stress granule disassembly.

Applications

Unspecified application

Species

Unspecified reactive species

Gea Cereghetti,Caroline Wilson-Zbinden,Vera M Kissling,Maren Diether,Alexandra Arm,Haneul Yoo,Ilaria Piazza,Shady Saad,Paola Picotti,D Allan Drummond,Uwe Sauer,Reinhard Dechant,Matthias Peter

Scientific reports 11:12819 PubMed34140587

2021

Comparison of endogenously expressed fluorescent protein fusions behaviour for protein quality control and cellular ageing research.

Applications

Unspecified application

Species

Unspecified reactive species

Kara L Schneider,Adam J M Wollman,Thomas Nyström,Sviatlana Shashkova

Journal of cell science 134: PubMed34085697

2021

Genome-wide imaging screen uncovers molecular determinants of arsenite-induced protein aggregation and toxicity.

Applications

Unspecified application

Species

Unspecified reactive species

Stefanie Andersson,Antonia Romero,Joana Isabel Rodrigues,Sansan Hua,Xinxin Hao,Therese Jacobson,Vivien Karl,Nathalie Becker,Arghavan Ashouri,Sebastien Rauch,Thomas Nyström,Beidong Liu,Markus J Tamás

Cell chemical biology 28:1283-1297.e8 PubMed33667410

2021

Regulation of the endocytosis and prion-chaperoning machineries by yeast E3 ubiquitin ligase Rsp5 as revealed by orthogonal ubiquitin transfer.

Applications

Unspecified application

Species

Unspecified reactive species

Yiyang Wang,Shuai Fang,Geng Chen,Rakhee Ganti,Tatiana A Chernova,Li Zhou,Duc Duong,Hiroaki Kiyokawa,Ming Li,Bo Zhao,Natalia Shcherbik,Yury O Chernoff,Jun Yin

Molecular microbiology 115:774-788 PubMed33190361

2020

Mutable yeast prion variants are stabilized by a defective Hsp104 chaperone.

Applications

Unspecified application

Species

Unspecified reactive species

Yu-Wen Huang,Vitaly V Kushnirov,Chih-Yen King

Nature structural & molecular biology 27:540-549 PubMed32367069

2020

Nucleation seed size determines amyloid clearance and establishes a barrier to prion appearance in yeast.

Applications

Unspecified application

Species

Unspecified reactive species

Janice Villali,Jason Dark,Teal M Brechtel,Fen Pei,Suzanne S Sindi,Tricia R Serio

Cell reports 28:2096-2110.e8 PubMed31433985

2019

Syntaxin 5 Is Required for the Formation and Clearance of Protein Inclusions during Proteostatic Stress.

Applications

Unspecified application

Species

Unspecified reactive species

Roja Babazadeh,Doryaneh Ahmadpour,Song Jia,Xinxin Hao,Per Widlund,Kara Schneider,Frederik Eisele,Laura Dolz Edo,Gertien J Smits,Beidong Liu,Thomas Nystrom

Cell stress & chaperones 23:581-594 PubMed29214607

2017

Generation and propagation of yeast prion [URE3] are elevated under electromagnetic field.

Applications

Unspecified application

Species

Unspecified reactive species

Hui-Yong Lian,Kang-Wei Lin,Chuanjun Yang,Peng Cai

Prion 10:444-465 PubMed27690738

2016

The small heat shock protein Hsp31 cooperates with Hsp104 to modulate Sup35 prion aggregation.

Applications

Unspecified application

Species

Unspecified reactive species

Kiran Aslam,Chai-Jui Tsai,Tony R Hazbun

View all publications

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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'.

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Anti-Hsp104 antibody

Western blot - Anti-Hsp104 antibody (AB69549)

Key facts

Host species

Clonality

Isotype

Carrier free

Reacts with

Applications

Specificity

Reactivity data

Properties and storage information

Form

Purification technique

Storage buffer

Shipped at conditions

Appropriate short-term storage duration

Appropriate short-term storage conditions

Appropriate long-term storage conditions

Aliquoting information

Storage information

Supplementary information

Biological function summary

Pathways

Product protocols

Target data

Publications (14)

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