Anti-Hsp104抗体(ab2924)
Key features and details
- Rabbit polyclonal to Hsp104
- Suitable for: WB
- Reacts with: Saccharomyces cerevisiae
- Isotype: IgG
概述
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产品名称
Anti-Hsp104抗体
参阅全部 Hsp104 一抗 -
描述
兔多克隆抗体to Hsp104 -
宿主
Rabbit -
经测试应用
适用于: WBmore details -
种属反应性
与反应: Saccharomyces cerevisiae
不与反应: Drosophila melanogaster, Plants, Escherichia coli -
免疫原
Synthetic peptide corresponding to Saccharomyces cerevisiae Hsp104 aa 894-908 (C terminal).
Sequence:DDDNEDSMEIDDDLD
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常规说明
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
性能
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形式
Liquid -
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... -
纯度
Whole antiserum -
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. -
克隆
多克隆 -
同种型
IgG -
研究领域
相关产品
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Compatible Secondaries
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Isotype control
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Recombinant Protein
应用
| 应用 | Ab评论 | 说明 |
|---|---|---|
| WB |
1/5000. Detects a band of approximately 100-105 kDa.
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| 说明 |
|---|
|
WB
1/5000. Detects a band of approximately 100-105 kDa. |
靶标
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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 -
数据库链接
- Entrez Gene: 850633 Saccharomyces cerevisiae
- SwissProt: P31539 Saccharomyces cerevisiae
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别名
- L0948 antibody
- Heat shock protein 104 antibody
- Hsp 104 antibody
数据表及文件
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Datasheet download
文献 (8)
ab2924 被引用在 8 文献中.
- 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
