Datasheet

Biological Description

Specificity	KDM1/LSD1 (Nuclear Marker) Antibody [P12K1] detects endogenous levels of total KDM1/LSD1 protein.
Background	KDM1A, also known as lysine-specific demethylase 1 (LSD1), is a flavin adenine dinucleotide (FAD)-dependent histone demethylase belonging to the amine oxidase family, playing a pivotal role in epigenetic regulation. LSD1 catalyzes the removal of mono- and di-methyl groups from lysine residues on histone H3, primarily H3K4me1/2 and H3K9me1/2, thereby functioning as a transcriptional co-repressor or co-activator depending on cellular context. LSD1 features three conserved domains: an N-terminal SWIRM domain that mediates chromatin targeting and protein-protein interactions; a central, LSD1-specific Tower domain that facilitates binding to the CoREST corepressor complex; and a C-terminal amine oxidase domain containing the catalytic site for FAD-dependent oxidative demethylation. The enzymatic reaction involves hydride transfer and the formation of an imine intermediate to excise methyl groups, with cofactors like CoREST required for efficient nucleosomal demethylation. LSD1 regulates gene expression programs involved in hematopoiesis, embryogenesis, and neuronal differentiation. It also demethylates non-histone proteins such as p53 and DNMT1, influencing cellular proliferation, DNA repair, and epigenetic stability. Additionally, LSD1 contributes to epithelial-to-mesenchymal transition (EMT) by repressing epithelial markers and is implicated in cancers. LSD1 is localized in the nucleus, serving as a nuclear marker fundamental to chromatin remodeling and transcriptional control.

Specificity

KDM1/LSD1 (Nuclear Marker) Antibody [P12K1] detects endogenous levels of total KDM1/LSD1 protein.

Background

KDM1A, also known as lysine-specific demethylase 1 (LSD1), is a flavin adenine dinucleotide (FAD)-dependent histone demethylase belonging to the amine oxidase family, playing a pivotal role in epigenetic regulation. LSD1 catalyzes the removal of mono- and di-methyl groups from lysine residues on histone H3, primarily H3K4me1/2 and H3K9me1/2, thereby functioning as a transcriptional co-repressor or co-activator depending on cellular context. LSD1 features three conserved domains: an N-terminal SWIRM domain that mediates chromatin targeting and protein-protein interactions; a central, LSD1-specific Tower domain that facilitates binding to the CoREST corepressor complex; and a C-terminal amine oxidase domain containing the catalytic site for FAD-dependent oxidative demethylation. The enzymatic reaction involves hydride transfer and the formation of an imine intermediate to excise methyl groups, with cofactors like CoREST required for efficient nucleosomal demethylation. LSD1 regulates gene expression programs involved in hematopoiesis, embryogenesis, and neuronal differentiation. It also demethylates non-histone proteins such as p53 and DNMT1, influencing cellular proliferation, DNA repair, and epigenetic stability. Additionally, LSD1 contributes to epithelial-to-mesenchymal transition (EMT) by repressing epithelial markers and is implicated in cancers. LSD1 is localized in the nucleus, serving as a nuclear marker fundamental to chromatin remodeling and transcriptional control.

Usage Information

Application

WB,IP, IHC, IF, FCM, ChIP

Dilution

WB	IP	IHC	IF	FCM	CHIP
1:10000 - 1:50000	1:10 - 1:100	1:50 - 1:250	1:450	1:20	5 µg for 25 µg chromatin

Reactivity

Mouse, Rat, Human

Source

Rabbit Monoclonal Antibody

MW

92 kDa, 155 kDa

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

Exprimental Methods

References

https://pubmed.ncbi.nlm.nih.gov/27479862/
https://pubmed.ncbi.nlm.nih.gov/36188536/

KDM1/LSD1 (Nuclear Marker) Antibody [P12K1]

Biological Description

Usage Information

References

Application Data