Anti-Hsp104 抗体 (ab2924)

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Key features and details

  • Rabbit polyclonal to Hsp104
  • Suitable for: WB
  • Reacts with: Saccharomyces cerevisiae
  • Isotype: IgG

製品の概要

  • 製品名

    Anti-Hsp104 antibody
    Hsp104 一次抗体 製品一覧

  • 製品の詳細

    Rabbit polyclonal to Hsp104

  • 由来種

    Rabbit

  • アプリケーション

    適用あり: WBmore details

  • 種交差性

    交差種: Saccharomyces cerevisiae
    非交差種: Drosophila melanogaster, Plants, Escherichia coli

  • 免疫原

    Synthetic peptide corresponding to Saccharomyces cerevisiae Hsp104 aa 894-908 (C terminal).
    Sequence:

    DDDNEDSMEIDDDLD

    Run BLAST with BLAST the sequence with ExPASy Run BLAST with BLAST the sequence with NCBI

  • 特記事項

    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

製品の特性

  • 製品の状態

    Liquid

  • 保存方法

    Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C. Avoid freeze / thaw cycle.

  • バッファー

    Preservative: 0.05% Sodium azide
  • Concentration information loading...

  • 精製度

    Whole antiserum

  • 一次抗体 備考

    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.

  • ポリ/モノ

    ポリクローナル

  • アイソタイプ

    IgG

  • 研究分野

アプリケーション

The Abpromise guarantee

Abpromise保証は、 次のテスト済みアプリケーションにおけるab2924の使用に適用されます

アプリケーションノートには、推奨の開始希釈率がありますが、適切な希釈率につきましてはご検討ください。

アプリケーション Abreviews 特記事項
WB
1/5000. Detects a band of approximately 100-105 kDa.
特記事項
WB
1/5000. Detects a band of approximately 100-105 kDa.

ターゲット情報

  • 関連性

    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.

  • 細胞内局在

    Cytoplasmic and Nuclear

  • 参照データベース

    • 別名

      • L0948 antibody
      • Heat shock protein 104 antibody
      • Hsp 104 antibody

    参考文献 (7)

    ab2924 を使用した論文を発表された方は、こちらまでお知らせください。データシートに掲載させていただきます。

    ab2924 は 7 報の論文で使用されています。

    • 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

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