|Tested species reactivity||Yeast|
|Published species reactivity||Yeast|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Synthetic peptide corresponding to the C-terminal residues D(894) D D N E D S M E I D D D L D(908) of S. cerevisiae HSP104.|
|Purification||Antigen affinity chromatography|
|Storage buffer||PBS with 1mg/ml BSA|
|Contains||0.05% sodium azide|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|Western Blot (WB)||1 ug/ml|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
|Western Blot (WB)||See 1 publications below|
PA1-024 detects HSP104 from yeast samples.
PA1-024 has been successfully used in Western blot procedures. By Western blot, this antibody detects a single ~104 kDa protein from yeast.
The PA1-024 immunogen is a synthetic peptide corresponding to the C-terminal residues D(894) D D N E D S M E I D D D L D(908) of S. cerevisiae HSP104.
Heat shock proteins (HSP) are expressed in response to various biological stresses, including high temperatures. There are several major families of HSPs including HSP70, HSP90 and HSP100. The HSP100 proteins generally have amino acid sequences of about 900 residues and contain two nucleotide-binding sites. Within the HSP100 family of proteins, yeast express a ~104 kDa form which is necessary to protect cells from various stress conditions such as heat, heavy metals and ethanol, though mutation studies have shown that the protein is not required for normal growth. Yeast HSP104 has been shown to be a ClpB protein with significant sequence homology to E. coli ClpB, particularly in the two nucleotide-binding sites.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
[PHI+], a novel Sup35-prion variant propagated with non-Gln/Asn oligopeptide repeats in the absence of the chaperone protein Hsp104.
PA1-024 was used in western blot to study a novel prion variant propagation mechanism
|Crist CG,Nakayashiki T,Kurahashi H,Nakamura Y||Genes to cells : devoted to molecular and cellular mechanisms (8:603)||2003|