Key features and details
- Rabbit polyclonal to Hsp104
- Suitable for: WB, IHC-P
- Reacts with: Mouse, Hamster, Saccharomyces cerevisiae
- Isotype: IgG
存放说明Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C. Avoid freeze / thaw cycle.
存储溶液Preservative: 0.05% Sodium azide
Concentration information loading...
Primary antibody说明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.
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.
|WB||1/100 - 1/5000. Detects a band of approximately 100-105 kDa. 1/100 for Mammals and 1/500 for yeast.|
|IHC-P||1/100 - 1/200.|
相关性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.
细胞定位Cytoplasmic and Nuclear
- L0948 antibody
- Heat shock protein 104 antibody
- Hsp 104 antibody
ab2924 被引用在 7 文献中.
- 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