RUVBL1抗体

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     Gel: 8%SDS-PAGE, Lysate: 40 μg, Lane 1-2: Raji and K562 cell lysates, Primary antibody: P09736(RUVBL1 Antibody) at dilution 1/2200, Secondary antibody: Goat anti rabbit IgG at 1/8000 dilution, Exposure time: 7 seconds    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human esophagus cancer tissue using P09736(RUVBL1 Antibody) at dilution 1/85. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human thyroid cancer tissue using P09736(RUVBL1 Antibody) at dilution 1/85. (Original magnification: ×200)    

  
  

RUVBL1 (RuvB-like AAA ATPase 1) is a conserved eukaryotic protein belonging to the AAA+ (ATPases Associated with Diverse Cellular Activities) superfamily. It functions as a helicase and ATP-dependent molecular chaperone, playing critical roles in chromatin remodeling, transcriptional regulation, DNA repair, and cellular signaling. RUVBL1 forms heterohexameric complexes with RUVBL2. serving as a core component of multiple macromolecular assemblies, including the INO80. SWR1. and TIP60 chromatin-remodeling complexes, as well as the mTOR and β-catenin pathways. Its involvement in oncogenic processes, such as cell proliferation and apoptosis evasion, has linked RUVBL1 overexpression to various cancers, making it a potential therapeutic target.

Antibodies targeting RUVBL1 are essential tools for studying its expression, localization, and interactions in normal and pathological contexts. These antibodies are typically raised against specific epitopes, such as the N-terminal or central regions of the human RUVBL1 protein (UniProt ID Q9Y265). Validated applications include Western blotting, immunoprecipitation (IP), immunofluorescence (IF), and immunohistochemistry (IHC). High-quality RUVBL1 antibodies exhibit specificity confirmed by knockout/knockdown controls and cross-reactivity with orthologs in common model organisms like mice and rats. Researchers utilize these reagents to explore RUVBL1's role in cancer biology, chromatin dynamics, and ATPase-dependent regulatory mechanisms, as well as to assess its potential as a biomarker or drug target in precision medicine approaches.