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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
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Lysine-specific demethylase 1 (KDM1A), also widely known as LSD1, is a chromatin-associated histone demethylase involved in transcriptional regulation, lineage specification, and epigenetic control of gene expression. KDM1A / LSD1 Antibody / Histone Demethylase is suitable for studies examining histone modification enzymes, chromatin remodeling complexes, and nuclear transcriptional regulation pathways. KDM1A belongs to the flavin adenine dinucleotide-dependent amine oxidase family and regulates chromatin state by removing methyl groups from lysine residues on histone proteins.
KDM1A antibody, also referred to as LSD1 antibody, Lysine-specific demethylase 1 antibody, Histone lysine demethylase antibody, and BHC110 antibody in the literature, recognizes a nuclear enzyme that functions within transcriptional repression and activation complexes. KDM1A was among the first histone demethylases identified and remains a central epigenetic regulator of chromatin accessibility, transcription factor recruitment, and cell identity programs. It is commonly associated with CoREST-containing repressor complexes and other chromatin regulatory assemblies that coordinate histone modification with transcriptional output.
KDM1A participates in pathways controlling proliferation, differentiation, epithelial-mesenchymal transition, stem cell maintenance, and developmental gene expression. By modulating histone H3 lysine methylation states, KDM1A can influence both transcriptional repression and activation depending on chromatin context and protein complex composition. Its nuclear localization and enzymatic role make KDM1A an important target for studies of epigenetic transcriptional control, cancer-associated chromatin remodeling, and histone demethylase biology.
Dysregulated KDM1A/LSD1 expression has been reported in multiple malignancies, including leukemia, prostate cancer, breast cancer, neuroblastoma, small cell lung cancer, and gastrointestinal tumors. Because LSD1-associated chromatin remodeling can influence tumor cell plasticity, differentiation state, and therapeutic response, this enzyme is widely investigated in cancer epigenetics and drug discovery research. LSD1 inhibitors are also being studied as tools for modifying transcriptional programs and promoting differentiation-associated responses in selected tumor contexts.
Western blot analysis with clone DID-11 detects a predominant KDM1A/LSD1 band near the expected apparent range in human SAHA, SH-SY5Y, and HepG2 cell lysates, supporting detection of this nuclear histone demethylase across multiple cell types. Immunohistochemistry analysis of FFPE human colon tissue demonstrates nuclear HRP-DAB brown staining in epithelial cells, consistent with the chromatin-associated localization expected for KDM1A/LSD1. This recombinant rabbit monoclonal antibody can support investigations involving histone demethylation, chromatin remodeling, transcriptional repression complexes, and cancer-associated epigenetic regulation.
For broader validation data and epigenetic regulation context, explore our LSD1 Antibody / Epigenetic Regulation Marker page featuring IHC, FACS, and HuProt microarray specificity validation.
Optimal dilution of the KDM1A / LSD1 Antibody / Histone Demethylase should be determined by the researcher.
A synthetic peptide specific to human Lysine-specific histone demethylase 1A was used as the immunogen for the KDM1 / LSD1 antibody.
Store the KDM1 / LSD1 antibody at -20oC.
KDM1A antibody, LSD1 antibody, Lysine-specific demethylase 1 antibody, Histone lysine demethylase antibody, BHC110 antibody
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