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Validated All-in-One™ qPCR Primer for KDM1A(NM_001009999.3) Search again
Product ID:
HQP170604
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
AOF2, BHC110, CPRF, KDM1, LSD1
Gene Description:
lysine demethylase 1A
Target Gene Accession:
NM_001009999.3(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Summary
This gene encodes a nuclear protein containing a SWIRM domain, a FAD-binding motif, and an amine oxidase domain. This protein is a component of several histone deacetylase complexes, though it silences genes by functioning as a histone demethylase.
Gene References into function
- results thus identify a histone demethylase conserved from S. pombe to human and reveal dynamic regulation of histone methylation by both histone methylases and demethylases
- in vivo LSD1 might not necessarily function as an oxidase, but it might use alternative electron acceptors
- nucleosomal demethylation is the result of CoREST enhancing the association between BHC110 and nucleosomes
- LSD1 interacts with androgen receptor in vitro and in vivo, and stimulates androgen-receptor-dependent transcription
- Results suggest that LSD1-mediated histone demethylation is regulated dynamically in vivo, and may have profound effects on gene expression under both physiological and pathological conditions.
- LSD1 is a chromatin-modifying enzyme, which is able to read different epigenetic marks on the histone N-terminal tail and can serve as a docking module for the stabilization of the associated corepressor complex(es) on chromatin
- Crystal structure of LSD1 at 2.9-A resolution. LSD1 forms a highly asymmetric, closely packed domain structure from which a long helical 'tower' domain protrudes.
- The shape and dimension of LSD1-CoREST crystal structure suggest its bivalent binding to nucleosomes, allowing efficient H3-K4 demethylation.
- These studies reveal an intimate link between the histone demethylase and deacetylase enzymes but also identify histone demethylation as a secondary target of Histone deacetylase (HDAC) inhibitors.
- Results describe the 2.8-A-resolution crystal structure of the human lysine-specific demethylase 1 (LSD1) and suggest that LSD1 defines a new subfamily of FAD-dependent oxidases.
- Epigenetic modifications on histone H3 need to be removed before Lys4 demethylation can efficiently occur.
- Data suggest that LSD1 may serve as novel biomarker predictive for prostate cancer with aggressive biology and point to a role of LSD1 in constitutive activation of AR-mediated growth signals.
- JMJD2C and LSD1 interact and both demethylases cooperatively stimulate androgen receptor-dependent gene transcription.
- Tranylcypromine is a mechanism-based inactivator of LSD1.
- LSD1 has a pro-oncogenic function by modulating pro-survival gene expression and p53 transcriptional activity
- This review underscores the involvement of the first histone demethylase, lysine-specific demethylase-1, in transcriptional regulation and describes a dynamic view of histone methylation by an array of other antagonizing histone-modifying enzymes.
- Pull down of spiked and endogenous LSD1 from HeLa cell nuclear extracts, set the stage for activity-based demethylase proteomics.
- The LSD1 active site cannot productively accommodate more than three residues on the N-terminal side of the methyllysine, explaining its histone H3-K4 specificity.
- findings couple the function of BHC80 to that of LSD1, and indicate that unmodified H3K4 is part of the 'histone code'
- the histone lysine-specific demethylase LSD1 interacts with p53 to repress p53-mediated transcriptional activation and to inhibit the role of p53 in promoting apoptosis
- represses hTERT transcription via demethylating H3-K4 in normal and cancerous cells, and together with HDACs, participates in the establishment of a stable repression state of the hTERT gene in normal or differentiated malignant cells
- These findings indicate that Epstein-Barr virus C promoter (Cp) is a cell cycle-regulated promoter that is under the control of Rb and the histone demethylase LSD1 in multiple latency types.
- LSD1 has multifaceted functions in chromatin regulation [review]
- Study established a requirement for LSD1 in directing specific interchromosomal interaction loci to distinct interchromatin granules and show that these interactions are required for enhanced transcription of specific estrogen-receptor target genes.
- LSD1 is a histone demethylase that is the prime corepressor for TLX
- ZNF198, through its multiple protein-protein interaction interfaces, helps to maintain the intact LSD1-CoREST-HDAC1 complex on specific, non-REST-responsive promoters and may also prevent SUMO-dependent dissociation of HDAC1
- The histone lysine demethylase, LSD1, is required for these ligand-induced interactive loci to associate with distinct interchromatin granules, long thought to serve as "storage" sites for the splicing machinery
- inhibition of LSD1 reprograms the transcriptome of neuroblastoma cells and inhibits neuroblastoma xenograft growth.