Product Details
Alternative Name: | ClpA, Heat shock protein 104 |
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Host: | Rabbit |
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Immunogen: | Synthetic peptide corresponding to the sequence near the C-terminus of yeast Hsp104. |
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UniProt ID: | P31539 |
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GenBank ID: | Z73131 |
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Source: | Purified from rabbit serum. |
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Species reactivity: | Yeast
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Applications: | WB
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Recommended Dilutions/Conditions: | Western Blot (1:1,000, ECL) Suggested dilutions/conditions may not be available for all applications. Optimal conditions must be determined individually for each application. |
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Application Notes: | Detects a band of ~104kDa by Western blot. |
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Purity Detail: | Protein A affinity purified. |
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Formulation: | Liquid. In PBS containing 50% glycerol and 0.09% sodium azide. |
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Handling: | Avoid freeze/thaw cycles. |
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Shipping: | Blue Ice |
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Long Term Storage: | -20°C |
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Scientific Background: | The 104 kDa yeast heat shock protein (Hsp104) is a cytosolic member of the Hsp100 family of proteins. Hsp104 cooperates with Hsp40 and Hsp70 co-chaperones in yeast in the reactivation of heat-damaged proteins. Hsp104 is also critical for the establishment and maintenance of the [PSI] prion phenotype in Saccharomyces cerevesiae. |
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Regulatory Status: | RUO - Research Use Only |
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Western Blot Analysis of HSP104 (yeast), pAb (Prod. No. ADI-SPA-1040): Lane 1: MW Marker, Lane 2: Yeast Cell Lysate
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Product Literature References
Molecular determinants and modifiers of Matrin-3 toxicity, condensate dynamics, and droplet morphology: M.L. Sprunger, et al.; iScience
25, 103900 (2022),
Abstract;
Rbs1 protein, involved in RNA polymerase III complex assembly in the yeast Saccharomyces cerevisiae, induces a Gcn4 response and forms aggregates when overproduced: I. Rudzińska, et al.; Gene
809, 146034 (2022),
Abstract;
Functional analysis of proposed substrate-binding residues of Hsp104: M.K. Howard, et al.; PLoS One
15, e0230198 (2020),
Abstract;
Full Text
Engineered protein disaggregases mitigate toxicity of aberrant prion-like fusion proteins underlying sarcoma: J.J. Ryan, et al.; J. Biol. Chem.
294, 11296 (2019),
Abstract;
FUS inclusions disrupt RNA localization by sequestering kinesin-1 and inhibiting microtubule detyrosination: K. Yasuda, et al.; J. Cell Biol.
216, 1015 (2017),
Abstract;
Full Text
Mechanistic Insights into Hsp104 Potentiation: M.P. Torrente, et al.; J. Biol. Chem.
291, 5101 (2016),
Abstract;
Full Text
In budding yeast, contraction of the actomyosin ring and formation of the primary septum at cytokinesis depend on each other: E. Cabib, et al. ; J. Cell. Sci.
115, 293 (2002),
Application(s): WB using yeast samples,
Abstract;
A role for cytosolic hsp70 in yeast [PSI(+)] prion propagation and [PSI(+)] as a cellular stress: D.C. Masison, et al. ; Genetics
156, 559 (2000),
Application(s): WB using yeast samples,
Abstract;
Prion-dependent switching between respiratory competence and deficiency in the yeast nam9-1 mutant: S. Rospert, et al. ; Mol. Cell. Biol.
20, 7220 (2000),
Application(s): WB using yeast samples,
Abstract;
Hsp104 is a highly conserved protein with two essential nucleotide-binding sites: S. Lindquist, et al. ; Nature
353, 270 (1991),
Application(s): WB using yeast samples,
Abstract;
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