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AB2924

Anti-Hsp104 antibody

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(8 Publications)

Rabbit Polyclonal Hsp104 antibody. Suitable for WB and reacts with Saccharomyces cerevisiae samples. Cited in 8 publications.

View Alternative Names

YLL026W, L0948, HSP104, Heat shock protein 104, Protein aggregation-remodeling factor HSP104

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Saccharomyces cerevisiae

Applications

WB

applications

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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"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Drosophila melanogaster": { "WB-species-checked": "notRecommended", "WB-species-dilution-info": "", "WB-species-notes": "<p></p>" }, "Escherichia coli": { "WB-species-checked": "notRecommended", "WB-species-dilution-info": "", "WB-species-notes": "<p></p>" }, "Plants": { "WB-species-checked": "notRecommended", "WB-species-dilution-info": "", "WB-species-notes": "<p></p>" }, "Saccharomyces cerevisiae": { "WB-species-checked": "guaranteed", "WB-species-dilution-info": "", "WB-species-notes": "<p></p>" } } }
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Properties and storage information

Form
Liquid
Purity
Whole antiserum
Storage buffer
Preservative: 0.05% Sodium azide
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:
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Target data

Required, in concert with Hsp40 (YDJ1) and Hsp70 (SSA1) and small Hsps (HSP26), for the dissociation, resolubilization and refolding of aggregates of damaged proteins after heat or other environmental stresses. Extracts proteins from aggregates by unfolding and threading them in an ATP-dependent process through the axial channel of the protein hexamer, after which they can be refolded by components of the Hsp70/Hsp40 chaperone system. Substrate binding is ATP-dependent, and release of bound polypeptide is triggered by ATP hydrolysis. Also responsible for the maintenance of prions by dissociating prion fibrils into smaller oligomers, thereby producing transmissible seeds that can infect daughter cells during mitosis and meiosis. Loss of HSP104 can cure yeast cells of the prions [PSI+], [URE3] and [PIN+]. Excess HSP104 can also specifically cure cells of [PSI+].
See full target information HSP104
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Publications (8)

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

Molecular microbiology 111:798-810 PubMed30582872

2019

Forms and abundance of chaperone proteins influence yeast prion variant competition.

Applications

Unspecified application

Species

Unspecified reactive species

Chang-I Yu,Chih-Yen King

Scientific reports 8:3894 PubMed29497115

2018

Loss of mRNA surveillance pathways results in widespread protein aggregation.

Applications

Unspecified application

Species

Unspecified reactive species

Nur Hidayah Jamar,Paraskevi Kritsiligkou,Chris M Grant

The Journal of cell biology 216:2295-2304 PubMed28630146

2017

ER stress causes widespread protein aggregation and prion formation.

Applications

WB

Species

Saccharomyces cerevisiae S288C

Norfadilah Hamdan,Paraskevi Kritsiligkou,Chris M Grant

Eukaryotic cell 13:635-47 PubMed24632242

2014

Hsp104 overexpression cures Saccharomyces cerevisiae [PSI+] by causing dissolution of the prion seeds.

Applications

WB

Species

Unspecified reactive species

Yang-Nim Park,Xiaohong Zhao,Yang-In Yim,Horia Todor,Robyn Ellerbrock,Michael Reidy,Evan Eisenberg,Daniel C Masison,Lois E Greene

PloS one 7:e37692 PubMed22719845

2012

Differences in the curing of [PSI+] prion by various methods of Hsp104 inactivation.

Applications

WB

Species

Saccharomyces cerevisiae S288C

Yang-Nim Park,David Morales,Emily H Rubinson,Daniel Masison,Evan Eisenberg,Lois E Greene

Cell 148:690-701 PubMed22341442

2012

Spt4 is selectively required for transcription of extended trinucleotide repeats.

Applications

Unspecified application

Species

Unspecified reactive species

Chia-Rung Liu,Chuang-Rung Chang,Yijuang Chern,Tzu-Han Wang,Wen-Chieh Hsieh,Wen-Chuan Shen,Chi-Yuan Chang,I-Chieh Chu,Ning Deng,Stanley N Cohen,Tzu-Hao Cheng

The Journal of biological chemistry 284:4238-45 PubMed19074437

2008

Functional rescue of mutant human cystathionine beta-synthase by manipulation of Hsp26 and Hsp70 levels in Saccharomyces cerevisiae.

Applications

WB

Species

Saccharomyces cerevisiae S288C

Laishram R Singh,Warren D Kruger

Nature 353:270-3 PubMed1896074

1991

Hsp104 is a highly conserved protein with two essential nucleotide-binding sites.

Applications

Unspecified application

Species

Unspecified reactive species

D A Parsell,Y Sanchez,J D Stitzel,S Lindquist
View all publications
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Product promise

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