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HSP104 (yeast) polyclonal antibody

ADI-SPA-1040-D 50 µg 213.00 USD
ADI-SPA-1040-F 200 µg 470.00 USD
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Product Details

Alternative Name:ClpA, Heat shock protein 104
Immunogen:Synthetic peptide corresponding to the sequence near the C-terminus of yeast Hsp104.
UniProt ID:P31539
GenBank ID:Z73131
Source:Purified from rabbit serum.
Species reactivity:Yeast
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.
Application Notes:Detects a band of ~104kDa by Western blot.
Purity Detail:Protein A affinity purified.
Formulation:Liquid. In PBS containing 50% glycerol and 0.09% sodium azide.
Handling:Avoid freeze/thaw cycles.
Shipping:Blue Ice
Long Term Storage:-20°C
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.
Regulatory Status:RUO - Research Use Only
HSP104 (yeast) polyclonal antibody Western blot
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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HSP104 (yeast) polyclonal antibody Western blot

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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