SELENBP1抗体

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     Gel: 8%SDS-PAGE, Lysate: 40 μg, Lane 1-2: Human fetal liver tissue and Mouse liver tissue lysates, Primary antibody: P09748(SELENBP1 Antibody) at dilution 1/250, Secondary antibody: Goat anti rabbit IgG at 1/8000 dilution, Exposure time: 20 seconds    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human liver cancer tissue using P09748(SELENBP1 Antibody) at dilution 1/20. (Original magnification: ×200)    

  
  

The SELENBP1 (Selenium Binding Protein 1) antibody is a tool used to detect and study the SELENBP1 protein, which plays diverse roles in cellular processes. SELENBP1 is a member of the selenium-binding protein family, though its exact functional relationship with selenium remains unclear. It is ubiquitously expressed, particularly in tissues like the liver, kidney, and gastrointestinal tract. The protein is implicated in intracellular redox regulation, sulfur metabolism, and detoxification pathways, potentially through its binding to selenium or selenium-containing compounds. SELENBP1 also interacts with methanethiol oxidase, linking it to hydrogen sulfide metabolism and mitochondrial function.

Research highlights its dual role in cancer: SELENBP1 is often downregulated in colorectal, lung, and breast cancers, suggesting tumor-suppressive properties, while elevated levels in prostate cancer and gliomas may indicate context-dependent oncogenic activity. Its expression is associated with oxidative stress responses, inflammation, and immune modulation, making it a potential biomarker for disease progression or therapeutic targeting.

SELENBP1 antibodies are widely used in techniques like Western blotting, immunohistochemistry, and immunofluorescence to analyze protein expression, localization, and interactions. These antibodies help elucidate SELENBP1’s role in pathological conditions, including cancer, neurodegenerative diseases, and metabolic disorders. However, variability in antibody specificity and cross-reactivity requires careful validation for experimental accuracy.

Structurally, SELENBP1 is a ~56 kDa protein containing a conserved selenium-binding domain. Post-translational modifications, such as oxidation, may influence its detection by antibodies. Ongoing studies aim to clarify its molecular mechanisms and therapeutic potential.