- CITATIONS: 2
|Application ||WB, IHC-P, IF, E|
|Calculated MW||92903 Da|
|Antigen Region||819-852 aa|
|Other Names||Lysine-specific histone demethylase 1A, 1---, BRAF35-HDAC complex protein BHC110, Flavin-containing amine oxidase domain-containing protein 2, KDM1A, AOF2, KDM1, KIAA0601, LSD1|
|Target/Specificity||This LSD1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 819-852 amino acids from the C-terminal region of human LSD1.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||LSD1 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||AOF2, KDM1, KIAA0601, LSD1|
|Function||Histone demethylase that demethylates both 'Lys-4' (H3K4me) and 'Lys-9' (H3K9me) of histone H3, thereby acting as a coactivator or a corepressor, depending on the context. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. 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. 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. Also acts as a coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and mediating demethylation of H3K9me, a specific tag for epigenetic transcriptional repression. The presence of PRKCB in ANDR-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. 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.|
|Tissue Location||Ubiquitously expressed.|
Provided below are standard protocols that you may find useful for product applications.
LSD1 is a histone demethylase that specifically demethylates 'Lys-4' of histone H3, a specific tag for epigenetic transcriptional activation, thereby acting as a corepressor. LSD1 contains 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. It acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. LSD1 demethylates both mono- and tri-methylted 'Lys-4' of histone H3. This protein may play a role in the repression of neuronal genes. Alone, it is unable to demethylate H3 'Lys-4' on nucleosomes and requires the presence of RCOR1/CoREST to achieve such activity. It may also demethylate 'Lys-9' of histone H3, a specific tag for epigenetic transcriptional repression, thereby leading to derepression of androgen receptor target genes.
Forneris,F., et al. FEBS Lett. 579 (10), 2203-2207 (2005) Shi,Y., et al. Cell 119 (7), 941-953 (2004) Hakimi,M.A., et al. J. Biol. Chem. 278 (9), 7234-7239 (2003) Hakimi,M.A., et al. PNAS 99 (11), 7420-7425 (2002) Humphrey,G.W., et al. J. Biol. Chem. 276 (9), 6817-6824 (2001) Ota, T., et al., Nat. Genet. 36(1):40-45 (2004).
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