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HSP90 alpha Protein

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  • SignalChem
  • 加拿大
  • 2025年06月29日
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      安诺伦(北京)生物科技有限公司

    研究领域:Cancer, Neurobiology,

    存储温度:Store product at –70oC. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles.

    靶点/蛋白质:Full-length recombinant human ASH2L was expressed in E. coli cells using an N-terminal GST tag.

    来源:E.coli

    存储溶液:50mM Tris-HCl, pH 7.5, 150mM NaCl, 10mM glutathione, 0.1mM EDTA, 0.25mM DTT, 0.1mM PMSF, 25% glycerol.

    参考文献:1. Patel A, et al: On the mechanism of multiple lysine methyla-tion by the human mixed lineage leukemia protein-1 (MLL1) core complex. J Biol Chem. 2009 284(36):24242-56. 2. Qi J, et al: Absent, small or homeotic 2-like protein (ASH2L) enhances the transcription of the estrogen receptor α gene through GATA-binding protein 3 (GATA3). J Biol Chem. 2014 289(45):31373-81.

    别名:ASH2L2

    应用:Methyltransferase Assay

    官网链接:https://www.signalchem.com/product_details.php?id=12728

    商品关键词:ASH2L Protein,A372-30BG-20,SignalChem

    简单描述:Full-length recombinant human ASH2L was expressed in E. coli cells using an N-terminal GST tag.

    Species: Human

    Tag: GST tag

    Sequence: Full length

    Genbank Number: BC015882

    Purity: Sample Purity Data. For specific information on a given lot, see related technical data sheet. 

    Molecular Weight: ~130 kDa 


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    图标文献和实验
    相关实验
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      Heat-shock protein 90 (Hsp90) is a molecular chaperone that assists in the maturation of a limited set of substrate proteins that are collectively referred to as clients. The majority of identified Hsp90 clients are involved in signal

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      The molecular chaperone HSP90 is currently under investigation as a promising target for anticancer drug discovery. It constitutes 1–2% of total cellular protein and is present in the cell as a dimer in association with a number

    • Detecting HSP90 Phosphorylation

      Heat-shock protein 90 (HSP90 ) is an essential molecular chaperone in eukaryotes. It is important for chaperoning proteins that are important determinants of multistep carcinogenesis. HSP90 ’s ATPase activity is associated with its chaperone

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