Phospho-Jun/JunD (Ser73/Ser100)抗体;Phospho-Jun/JunD (Ser73/Ser100) Antibody—艾普蒂

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     Western blot analysis of Jun (Phospho-Ser73)/JunD (Phospho-Ser100) in A549, HL-60, U251, U87-MG lysates using Phospho-Jun/JunD (Ser73/Ser100) antibody.    

  
  

The Phospho-Jun/JunD (Ser73/Ser100) antibody is designed to detect Jun and JunD proteins when phosphorylated at specific serine residues (Ser73 in c-Jun and Ser100 in JunD). These transcription factors belong to the AP-1 family, which regulates gene expression involved in cell proliferation, differentiation, and apoptosis. Phosphorylation at these sites serves as a critical regulatory mechanism. For Jun (c-Jun), Ser73 phosphorylation is primarily mediated by stress-activated protein kinases (SAPKs), such as JNK, in response to cellular stress, cytokines, or growth factors. This modification enhances c-Jun’s transcriptional activity, promoting AP-1-driven gene expression.

JunD, a more stable and ubiquitously expressed AP-1 member, is phosphorylated at Ser100 by kinases like ERK, often in response to mitogenic signals. This phosphorylation modulates JunD’s ability to activate or repress target genes, depending on cellular context. The Phospho-Jun/JunD (Ser73/Ser100) antibody is widely used in research to study AP-1 activation dynamics in processes like inflammation, oncogenesis, and cellular stress responses. It enables specific detection of these post-translational modifications via techniques like Western blotting, immunofluorescence, or immunohistochemistry. Researchers utilize this tool to investigate signaling pathways (e.g., MAPK/JNK), evaluate drug effects on kinase activity, or explore disease mechanisms where AP-1 dysregulation is implicated, such as cancer or autoimmune disorders. Proper controls are essential to ensure specificity, as cross-reactivity with non-target phospho-proteins may occur.