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     Western blot analysis of SAMHD1 expression in MCF7 cell lysate.    

  
  

SAMHD1 (Sterile Alpha Motif and Histidine-Aspartate Domain-containing protein 1) is a nuclear protein with dual roles in innate immunity and nucleotide metabolism. It restricts HIV-1 and other viral infections by hydrolyzing deoxyribonucleoside triphosphates (dNTPs) into deoxynucleosides and inorganic triphosphate, thereby depleting dNTP pools essential for viral reverse transcription. Additionally, SAMHD1 regulates cellular DNA replication and repair by maintaining nucleotide homeostasis. Its activity is modulated through phosphorylation at residue T592. which influences its dNTPase function and protein stability. Dysregulation of SAMHD1 is linked to autoimmune disorders like Aicardi-Goutières syndrome (AGS) and cancers, where mutations or altered expression impair immune regulation or genomic stability.

SAMHD1 antibodies are critical tools for studying its expression, post-translational modifications, and interactions. These antibodies are widely used in techniques such as Western blotting, immunofluorescence, and flow cytometry to assess SAMHD1 levels in viral infection models, autoimmune disease research, and cancer studies. Specific clones or epitope-targeted antibodies help distinguish phosphorylated or truncated isoforms, aiding in functional analyses. For example, antibodies against the N-terminal domain often detect full-length protein, while phospho-specific antibodies clarify regulatory mechanisms. Validation using SAMHD1-knockout cell lines ensures antibody specificity. Both monoclonal and polyclonal variants are available, with monoclonal antibodies offering higher consistency for quantitative assays. Researchers also employ these antibodies to explore SAMHD1's role in antiviral signaling, its interplay with HIV-1 accessory proteins like Vpx, and its potential as a therapeutic target in oncology or autoimmune conditions.