ZGPAT (Zinc Finger and G-Patch Domain-Containing Protein) is a nuclear protein encoded by the *ZGPAT* gene in humans. It contains conserved zinc finger motifs and a G-patch domain, suggesting roles in nucleic acid binding and protein interactions. ZGPAT is implicated in transcriptional regulation, chromatin remodeling, and DNA damage response pathways. Studies indicate it may act as a repressor by recruiting histone deacetylases (HDACs) to modulate gene expression, particularly at telomeric regions and repetitive DNA sequences.
ZGPAT antibodies are essential tools for investigating its expression, localization, and molecular functions. They enable detection via techniques like Western blotting, immunofluorescence, and chromatin immunoprecipitation (ChIP). Research using these antibodies has linked ZGPAT to cellular processes such as apoptosis, cell cycle control, and genome stability. Dysregulation of ZGPAT has been observed in certain cancers and autoimmune disorders, highlighting its potential relevance in disease mechanisms.
While ZGPAT's full biological significance remains under exploration, its conserved domains and nuclear activity position it as a critical player in epigenetic regulation. Antibodies against ZGPAT continue to support studies aiming to unravel its interactions with HDAC complexes, telomere-associated proteins, and other regulatory factors, offering insights into its role in health and disease.