The programmed cell death 2 (PDCD2) protein, also known as ZMYND2. is a conserved nuclear protein implicated in cellular apoptosis, differentiation, and proliferation. First identified through homology to the Drosophila melanogaster melanogaster protein Rp8. PDCD2 is ubiquitously expressed across tissues and plays roles in transcriptional regulation and cell cycle control. Structurally, it contains a MYND-type zinc finger domain, facilitating protein-protein interactions, particularly with chromatin-modifying complexes. Studies suggest PDCD2 interacts with factors like CoREST and NuRD, influencing gene expression programs critical for hematopoiesis, neurodevelopment, and tumor suppression.
PDCD2 antibodies are essential tools for investigating its expression patterns, subcellular localization, and molecular functions. These antibodies are widely used in techniques such as Western blotting, immunohistochemistry (IHC), and immunofluorescence (IF) to detect PDCD2 in both normal and pathological contexts. Research highlights PDCD2's dual roles: while its downregulation is associated with malignancies (e.g., leukemia, breast cancer) and poor prognosis, overexpression may promote apoptosis in certain cellular stresses. Additionally, PDCD2 is linked to ribosome biogenesis and p53-mediated pathways, underscoring its complexity in balancing cell survival and death. Antibodies targeting specific epitopes or post-translational modifications of PDCD2 further enable mechanistic studies, aiding in the exploration of its involvement in developmental disorders and cancer. Despite progress, its precise molecular mechanisms remain under investigation, necessitating reliable antibody reagents to advance functional and clinical research.