Phospho-HSP90AA1 (Thr5/7) Antibody Blocking Peptide(bs-3181P)-500ug

Phospho-HSP90AA1 (Thr5/7) Anti

body Blocking Peptide(bs-3181P)-500ug
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  • bs-3181P
  • 2025年10月16日
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      500ug

    产品编号bs-3181P
    英文名称Phospho-HSP90AA1 (Thr5/7) Antibody Blocking Peptide
    中文名称磷酸化热休克蛋白90α封闭多肽
    英文别名HSP90 alpha (Phospho-Thr5/7); HS90A_HUMAN; heat shock 90kDa protein 1 alpha; Heat shock protein 90kDa alpha cytosolic class A member 1; heat shock protein 90kDa alpha (cytosolic), class A member 2; Heat shock protein 90kDa alpha cytosolic class B member 1; Heat shock protein HSP 90 alpha; Heat shock protein HSP 90-alpha; Heat shock protein HSP 90 beta; HSP 84; HSP 86; Hsp 90; HSP84; HSP86; Hsp89; HSP89A; Hsp90; HSP90 Beta; HSP90A; HSP90AA1; HSP90AB1; HSP90B; HSP90N; HSPC1; HSPC2; HSPCA; HSPCAL1; HSPCAL3; HSPCAL4; HSPCB; HSPN; Heat shock 86 kDa; HSP90ALPHA; HSPN; LAP2; Lipopolysaccharide associated protein2; LPS associated protein 2; NY REN 38 antigen; Renal carcinoma antigen NY REN 38; Renal carcinoma antigen NY-REN-38; D6S182; FLJ26984; FLJ31884.
    纯化方法HPLC
    研究领域

    Cancer > Invasion/microenvironment > ECM > Extracellular matrix > MMPs

    Cancer > Tumor biomarkers

    Signal Transduction > Protein Trafficking > Chaperones > Heat Shock Proteins

    Signal Transduction > Protein Trafficking > Organelle Proteins

    亚基Homodimer. Interacts with AHSA1, FNIP1, HSF1, SMYD3 and TOM34. Interacts with TERT; the interaction, together with PTGES3, is required for correct assembly and stabilization of the TERT holoenzyme complex. Interacts with CHORDC1 and DNAJC7. Interacts with STUB1 and UBE2N; may couple the chaperone and ubiquitination systems.
    亚细胞定位Cytoplasm. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
    翻译后修饰ISGylated.
    S-nitrosylated; negatively regulates the ATPase activity and the activation of eNOS by HSP90AA1.
    相似性Belongs to the heat shock protein 90 family.
    功能Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function.
    保存条件Shipped at 4℃. Stored at -20℃ for one year. Avoid repeated freeze/thaw cycles.
    注意事项This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
    背景资料Hsp90 (heat shock protein 90) is a molecular chaperone and is one of the most abundant proteins in unstressed cells. It is an ubiquitous molecular chaperone found in eubacteria and all branches of eukarya, but it is apparently absent in archaea. Whereas cytoplasmic Hsp90 is essential for viability under all conditions in eukaryotes, the bacterial homologue HtpG is dispensable under non-heat stress conditions.

     

     

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