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Rabbit Anti-KDM1A Recombinant Antibody (CBYJL-233) (CBMAB-L0331-YJ)

Provided herein is a Rabbit monoclonal antibody, which binds to Lysine Demethylase 1A (KDM1A). The antibody can be used for immunoassay techniques, such as WB, IP, IHC-P, IF, ChIP.
See all KDM1A antibodies

Summary

Host Animal
Rabbit
Specificity
Human, Mouse, Rat, Monkey
Clone
CBYJL-233
Antibody Isotype
IgG
Application
WB, IP, IHC-P, IF, ChIP

Basic Information

Specificity
Human, Mouse, Rat, Monkey
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Buffer
PBS, pH 7.4
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Lysine Demethylase 1A
Introduction
KDM1A is a nuclear protein containing a FAD-binding motif, a SWIRM domain, and an amine oxidase domain. This protein is a component of several histone deacetylase complexes, even though it silences genes by functioning as a histone demethylase. Alternative splicing results in multiple transcript variants.
Entrez Gene ID
Human23028
Mouse99982
Rat500569
Monkey718609
UniProt ID
HumanO60341
MouseQ6ZQ88
RatB3STT9
MonkeyA0A1D5R152
Alternative Names
Lysine Demethylase 1A; Flavin-Containing Amine Oxidase Domain-Containing Protein 2; Amine Oxidase (Flavin Containing) Domain 2; BRAF35-HDAC Complex Protein BHC110; AOF2; KDM1; LSD1; FAD-Binding Protein BRAF35-HDAC Complex; 110 KDa Subunit; Lysine-Specific Histone Demethylase 1A
Function
Histone demethylase that can demethylate both 'Lys-4' (H3K4me) and 'Lys-9' (H3K9me) of histone H3, thereby acting as a coactivator or a corepressor, depending on the context (PubMed:15620353, PubMed:15811342, PubMed:16140033, PubMed:16079794, PubMed:16079795, PubMed:16223729).
Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed (PubMed:15620353, PubMed:15811342, PubMed:16079794, PubMed:21300290).
Acts as a corepressor by mediating demethylation of H3K4me, a specific tag for epigenetic transcriptional activation. Demethylates both mono- (H3K4me1) and di-methylated (H3K4me2) H3K4me (PubMed:15620353, PubMed:20389281, PubMed:21300290, PubMed:23721412).
May play a role in the repression of neuronal genes. Alone, it is unable to demethylate H3K4me on nucleosomes and requires the presence of RCOR1/CoREST to achieve such activity (PubMed:16140033, PubMed:16079794, PubMed:16885027, PubMed:21300290, PubMed:23721412).
Also acts as a coactivator of androgen receptor (AR)-dependent transcription, by being recruited to AR target genes and mediating demethylation of H3K9me, a specific tag for epigenetic transcriptional repression. The presence of PRKCB in AR-containing complexes, which mediates phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag that prevents demethylation H3K4me, prevents H3K4me demethylase activity of KDM1A (PubMed:16079795).
Demethylates di-methylated 'Lys-370' of p53/TP53 which prevents interaction of p53/TP53 with TP53BP1 and represses p53/TP53-mediated transcriptional activation. Demethylates and stabilizes the DNA methylase DNMT1. Required for gastrulation during embryogenesis. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Effector of SNAI1-mediated transcription repression of E-cadherin/CDH1, CDN7 and KRT8. Required for the maintenance of the silenced state of the SNAI1 target genes E-cadherin/CDH1 and CDN7 (PubMed:20389281).
Biological Process
Alternative mRNA splicing, via spliceosomeIEA:Ensembl
Cellular response to cAMPIEA:Ensembl
Cellular response to gamma radiationManual Assertion Based On ExperimentIMP:MGI
Cellular response to UVManual Assertion Based On ExperimentIDA:MGI
Cerebral cortex developmentIEA:Ensembl
Chromatin organizationIEA:UniProtKB-KW
Guanine metabolic processIEA:Ensembl
Histone H3-K4 demethylationManual Assertion Based On ExperimentIDA:UniProtKB
Histone H3-K9 demethylationManual Assertion Based On ExperimentIDA:UniProtKB
Muscle cell developmentBy SimilarityISS:BHF-UCL
Negative regulation of DNA binding1 PublicationIC:BHF-UCL
Negative regulation of DNA damage response, signal transduction by p53 class mediatorManual Assertion Based On ExperimentIMP:BHF-UCL
Negative regulation of DNA-binding transcription factor activityManual Assertion Based On ExperimentIDA:BHF-UCL
Negative regulation of histone H3-K4 methylationISS:ARUK-UCL
Negative regulation of histone H3-K9 methylationISS:ARUK-UCL
Negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediatorManual Assertion Based On ExperimentIMP:BHF-UCL
Negative regulation of protein bindingManual Assertion Based On ExperimentIMP:BHF-UCL
Negative regulation of transcription by RNA polymerase IIManual Assertion Based On ExperimentIMP:BHF-UCL
Negative regulation of transcription, DNA-templatedManual Assertion Based On ExperimentIDA:BHF-UCL
Neuron maturationIEA:Ensembl
Positive regulation of cell sizeIEA:Ensembl
Positive regulation of chromatin bindingIEA:Ensembl
Positive regulation of cold-induced thermogenesisBy SimilarityISS:YuBioLab
Positive regulation of DNA-binding transcription factor activityManual Assertion Based On ExperimentIDA:BHF-UCL
Positive regulation of histone ubiquitinationManual Assertion Based On ExperimentIMP:MGI
Positive regulation of neural precursor cell proliferationISS:ARUK-UCL
Positive regulation of neuroblast proliferationManual Assertion Based On ExperimentIMP:BHF-UCL
Positive regulation of neuron projection developmentIEA:Ensembl
Positive regulation of stem cell proliferationISS:ARUK-UCL
Positive regulation of transcription by RNA polymerase IIManual Assertion Based On ExperimentIDA:BHF-UCL
Protein demethylationManual Assertion Based On ExperimentIMP:BHF-UCL
Regulation of androgen receptor signaling pathwayTAS:Reactome
Regulation of DNA methylation-dependent heterochromatin assemblyManual Assertion Based On ExperimentIDA:UniProtKB
Regulation of double-strand break repair via homologous recombinationManual Assertion Based On ExperimentIMP:MGI
Regulation of protein localizationManual Assertion Based On ExperimentIMP:MGI
Regulation of transcription by RNA polymerase IIManual Assertion Based On ExperimentIMP:UniProtKB
Response to fungicideIEA:Ensembl
Cellular Location
Nucleus
Involvement in disease
Cleft palate, psychomotor retardation, and distinctive facial features (CPRF):
A syndrome characterized by cleft palate, developmental delay, psychomotor retardation, and facial dysmorphic features including a prominent forehead, slightly arched eyebrows, elongated palpebral fissures, a wide nasal bridge, thin lips, and widely spaced teeth. Cleft palate is a congenital fissure of the soft and/or hard palate, due to faulty fusion.
PTM
Polyubiquitinated by JADE2; which leads to its proteasomal degradation.

Zhang, W., Ruan, X., Li, Y., Zhi, J., Hu, L., Hou, X., ... & Gao, M. (2022). KDM1A promotes thyroid cancer progression and maintains stemness through the Wnt/β-catenin signaling pathway. Theranostics, 12(4), 1500.

Zhang, X., Wang, X., Wu, T., Yin, W., Yan, J., Sun, Y., & Zhao, D. (2022). Therapeutic potential of targeting LSD1/KDM1A in cancers. Pharmacological research, 175, 105958.

Agarwal, S., Bonefas, K. M., Garay, P. M., Brookes, E., Murata-Nakamura, Y., Porter, R. S., ... & Iwase, S. (2021). KDM1A maintains genome-wide homeostasis of transcriptional enhancers. Genome Research, 31(2), 186-197.

Zhou, M., Venkata, P. P., Viswanadhapalli, S., Palacios, B., Alejo, S., Chen, Y., ... & Sareddy, G. R. (2021). KDM1A inhibition is effective in reducing stemness and treating triple negative breast cancer. Breast cancer research and treatment, 185, 343-357.

Hou, X., Li, Q., Yang, L., Yang, Z., He, J., Li, Q., & Li, D. (2021). KDM1A and KDM3A promote tumor growth by upregulating cell cycle-associated genes in pancreatic cancer. Experimental Biology and Medicine, 246(17), 1869-1883.

Fu, D. J., Li, J., & Yu, B. (2021). Annual review of LSD1/KDM1A inhibitors in 2020. European Journal of Medicinal Chemistry, 214, 113254.

Maes, T., Mascaró, C., Rotllant, D., Lufino, M. M. P., Estiarte, A., Guibourt, N., ... & Buesa Arjol, C. (2020). Modulation of KDM1A with vafidemstat rescues memory deficit and behavioral alterations. PLoS One, 15(5), e0233468.

Fang, Y., Liao, G., & Yu, B. (2019). LSD1/KDM1A inhibitors in clinical trials: advances and prospects. Journal of hematology & oncology, 12(1), 1-14.

Karakaidos, P., Verigos, J., & Magklara, A. (2019). LSD1/KDM1A, a gate-keeper of cancer stemness and a promising therapeutic target. Cancers, 11(12), 1821.

Ismail, T., Lee, H. K., Kim, C., Kwon, T., Park, T. J., & Lee, H. S. (2018). KDM1A microenvironment, its oncogenic potential, and therapeutic significance. Epigenetics & chromatin, 11(1), 1-15.

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For research use only. Not intended for any clinical use.

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