Anti-Hsp104 antibody (ab2924)
Key features and details
- Rabbit polyclonal to Hsp104
- Suitable for: WB
- Reacts with: Saccharomyces cerevisiae
- Isotype: IgG
Overview
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Product name
Anti-Hsp104 antibody
See all Hsp104 primary antibodies -
Description
Rabbit polyclonal to Hsp104 -
Host species
Rabbit -
Tested applications
Suitable for: WBmore details -
Species reactivity
Reacts with: Saccharomyces cerevisiae
Does not react with: Drosophila melanogaster, Plants, Escherichia coli -
Immunogen
Synthetic peptide corresponding to Saccharomyces cerevisiae Hsp104 aa 894-908 (C terminal).
Sequence:DDDNEDSMEIDDDLD
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General notes
The Life Science industry has been in the grips of a reproducibility crisis for a number of years. Abcam is leading the way in addressing this with our range of recombinant monoclonal antibodies and knockout edited cell lines for gold-standard validation. Please check that this product meets your needs before purchasing.
If you have any questions, special requirements or concerns, please send us an inquiry and/or contact our Support team ahead of purchase. Recommended alternatives for this product can be found below, along with publications, customer reviews and Q&As
Properties
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Form
Liquid -
Storage instructions
Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C. Avoid freeze / thaw cycle. -
Storage buffer
Preservative: 0.05% Sodium azide -
Concentration information loading...
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Purity
Whole antiserum -
Primary antibody notes
Heat Shock Proteins (HSP) are expressed in response to various biological stresses, including high temperatures. There are several major families of HSPs including HSP 70, HSP 90 and HSP 100. The HSP 100 proteins generally have amino acid sequences of about 900 residues and contain two nucleotide-binding sites. Within the HSP 100 family of proteins, yeast express an ~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 HSP 104 has been shown to be a ClpB protein with significant sequence homology to E. coli ClpB, particularly in the two nucleotide-binding sites. -
Clonality
Polyclonal -
Isotype
IgG -
Research areas
Associated products
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Compatible Secondaries
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Isotype control
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Recombinant Protein
Applications
The Abpromise guarantee
Our Abpromise guarantee covers the use of ab2924 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Application | Abreviews | Notes |
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WB |
1/5000. Detects a band of approximately 100-105 kDa.
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Notes |
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WB
1/5000. Detects a band of approximately 100-105 kDa. |
Target
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Relevance
Hsp104 is a molecular chaperone required for stress tolerance and for maintenance of [psi(+)] prions in the budding yeast Saccharomyces cerevisiae. Hsp104 is vital to protect yeast cells against high temperature and high concentration of ethanol. It is not required for normal growth. -
Cellular localization
Cytoplasmic and Nuclear -
Database links
- Entrez Gene: 850633 Saccharomyces cerevisiae
- SwissProt: P31539 Saccharomyces cerevisiae
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Alternative names
- L0948 antibody
- Heat shock protein 104 antibody
- Hsp 104 antibody
Protocols
Datasheets and documents
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Datasheet download
References (8)
ab2924 has been referenced in 8 publications.
- Yu CI & King CY Forms and abundance of chaperone proteins influence yeast prion variant competition. Mol Microbiol 111:798-810 (2019). PubMed: 30582872
- Jamar NH et al. Loss of mRNA surveillance pathways results in widespread protein aggregation. Sci Rep 8:3894 (2018). PubMed: 29497115
- Hamdan N et al. ER stress causes widespread protein aggregation and prion formation. J Cell Biol 216:2295-2304 (2017). WB ; Saccharomyces cerevisiae . PubMed: 28630146
- Park YN et al. Hsp104 overexpression cures Saccharomyces cerevisiae [PSI+] by causing dissolution of the prion seeds. Eukaryot Cell 13:635-47 (2014). WB . PubMed: 24632242
- Liu CR et al. Spt4 is selectively required for transcription of extended trinucleotide repeats. Cell 148:690-701 (2012). PubMed: 22341442
- Park YN et al. Differences in the Curing of [PSI(+)] Prion by Various Methods of Hsp104 Inactivation. PLoS One 7:e37692 (2012). WB ; Saccharomyces cerevisiae . PubMed: 22719845
- Singh LR & Kruger WD Functional rescue of mutant human cystathionine beta-synthase by manipulation of Hsp26 and Hsp70 levels in Saccharomyces cerevisiae. J Biol Chem 284:4238-45 (2009). WB ; Saccharomyces cerevisiae . PubMed: 19074437
- Parsell DA et al. Hsp104 is a highly conserved protein with two essential nucleotide-binding sites. Nature 353:270-3 (1991). PubMed: 1896074