**Background of EDD Antibodies**
EDD (E3 ubiquitin-protein ligase EDD), also known as UBR5 or Hp33. is a HECT domain-containing E3 ubiquitin ligase involved in protein ubiquitination and degradation via the proteasome. Initially identified as a hyperproliferation-associated protein in cervical cancer, EDD regulates diverse cellular processes, including DNA damage repair, cell cycle progression, and apoptosis. It interacts with key signaling pathways, such as the TGF-β and Wnt pathways, and plays roles in maintaining genomic stability by mediating responses to DNA double-strand breaks.
EDD antibodies are essential tools for studying its expression, localization, and function in both normal and pathological contexts. Overexpression or dysregulation of EDD has been linked to cancers (e.g., breast, ovarian, and prostate), where it may promote tumor growth, metastasis, or therapy resistance. Antibodies targeting EDD enable detection via techniques like Western blotting, immunohistochemistry, and immunofluorescence, aiding research into its oncogenic mechanisms. Additionally, EDD's role in fertility (e.g., oocyte maturation) and developmental disorders has spurred interest in its broader biological impact.
Validated EDD antibodies are critical for ensuring specificity, given structural similarities among HECT ligases. Their applications extend to exploring EDD as a potential biomarker or therapeutic target, particularly in cancers with aberrant ubiquitination pathways. Research continues to unravel EDD's complex interactome and its implications in disease pathogenesis.