IMPDH2抗体

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     Gel: 8%SDS-PAGE, Lysate: 40 μg, Lane: A549 cells, Primary antibody: P01478(IMPDH2 Antibody) at dilution 1/650, Secondary antibody: Goat anti rabbit IgG at 1/8000 dilution, Exposure time: 3 minutes    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human lung cancer tissue using P01478(IMPDH2 Antibody) at dilution 1/60. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human liver cancer tissue using P01478(IMPDH2 Antibody) at dilution 1/60. (Original magnification: ×200)    

  
  

IMPDH2 (Inosine-5'-monophosphate dehydrogenase 2) is a key enzyme in the de novo biosynthesis of guanine nucleotides, catalyzing the conversion of inosine monophosphate (IMP) to xanthosine monophosphate (XMP). This rate-limiting step is critical for maintaining cellular GTP and dGTP pools, particularly in rapidly proliferating cells such as activated lymphocytes and cancer cells. IMPDH2. the predominant isoform in most human tissues, has drawn significant attention due to its role in cell cycle progression, metabolic adaptation, and disease pathogenesis.

Antibodies targeting IMPDH2 are widely used in research to investigate its expression patterns, subcellular localization, and functional regulation. Studies have linked IMPDH2 dysregulation to various conditions, including cancer progression, antiviral responses, and autoimmune disorders. Its overexpression in certain tumors has prompted exploration of IMPDH2 as a potential therapeutic target or biomarker. Additionally, IMPDH2 serves as the major target of immunosuppressive drugs like mycophenolic acid, underscoring its relevance in immunology and transplantation research.

IMPDH2 antibodies are commonly employed in techniques such as Western blotting, immunohistochemistry, and immunofluorescence to assess protein levels in disease models or drug-treated cells. Recent research also focuses on its non-catalytic functions, including interactions with cytoskeletal proteins and involvement in nucleotide metabolism-independent pathways. The high conservation of IMPDH2 across species enhances its utility in translational studies using experimental models.