Mouse Monoclonal KDM1A Antibody

KDM1A (lysine-specific histone demethylase 1A), also known as LSD1. is an epigenetic enzyme critical for regulating gene expression by removing methyl groups from histone H3 lysine 4 (H3K4) and H3 lysine 9 (H3K9), depending on its interacting partners. Discovered in 2004. it belongs to the flavin adenine dinucleotide (FAD)-dependent amine oxidase family and plays a pivotal role in chromatin remodeling, stem cell maintenance, and cellular differentiation. Structurally, KDM1A contains a SWIRM domain for protein interactions and an amine oxidase-like domain for catalytic activity. Its function is tightly linked to oncogenesis, with overexpression observed in various cancers, including leukemia, breast, and prostate cancer, where it often promotes tumor growth by repressing tumor suppressor genes or activating oncogenic pathways. Conversely, KDM1A also exhibits tumor-suppressive roles in certain contexts, highlighting its complex regulatory mechanisms. Antibodies targeting KDM1A are essential tools in research for detecting its expression, localization, and interaction partners via techniques like Western blot, immunohistochemistry (IHC), and chromatin immunoprecipitation (ChIP-seq). They also aid in studying its therapeutic potential, as KDM1A inhibitors (e.g., tranylcypromine) are under clinical investigation for cancer treatment. Validated antibodies are crucial to ensure specificity, given structural similarities with other amine oxidases, and are available in various host species and clonal formats to support diverse experimental needs.