ID4 (Inhibitor of DNA Binding 4) is a member of the ID protein family, which regulates cell differentiation and proliferation by modulating transcriptional activity. ID proteins lack a DNA-binding domain but interact with basic helix-loop-helix (bHLH) transcription factors, thereby inhibiting their ability to bind DNA and regulate target genes. ID4. specifically, is implicated in diverse biological processes, including cell cycle control, stem cell maintenance, and tissue development. Dysregulation of ID4 has been linked to cancer, where it often exhibits dual roles as either a tumor suppressor or oncogene, depending on context. For instance, ID4 is frequently downregulated in cancers like breast, ovarian, and prostate cancer due to promoter hypermethylation, correlating with poor prognosis. Conversely, in glioblastoma and certain hematologic malignancies, ID4 overexpression promotes tumor growth and therapy resistance.
Research on ID4 antibodies has focused on understanding its expression patterns, interactions, and functional roles. These antibodies are critical tools for detecting ID4 in tissues or cell lines via techniques like Western blotting, immunohistochemistry, or flow cytometry. Recent studies explore ID4's involvement in epigenetic regulation, such as modulating DNA methylation or histone modifications, and its crosstalk with signaling pathways like TGF-β and Wnt. Additionally, ID4 is studied in developmental contexts, particularly in neurogenesis and organogenesis.
Therapeutic targeting of ID4 remains exploratory, with potential strategies including epigenetic reactivation in ID4-silenced cancers or inhibition in ID4-driven malignancies. Its context-dependent roles underscore the need for precise biomarker-driven approaches in clinical applications.