Abcam, ab69549, Anti-Hsp104 antibody

Size: 200µL
Rabbit Polyclonal Hsp104 antibody. Suitable for IP, WB and reacts with Saccharomyces cerevisiae samples. Cited in 14 publications.
Key facts
Host species:Rabbit,
Clonality:Polyclonal,
Isotype:IgG,
Carrier free:No,
Reacts with:Saccharomyces cerevisiae,
Applications:WB, IPSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
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.

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Protein A, Storage buffer-Preservative: 0.09% Sodium azideConstituents: 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

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.