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48-602MAG
Buffer Detection Kit for Magnetic Beads
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Use Anti-monomethyl-Histone H4 (Lys20) Antibody, clone NL314 (rabbit monoclonal antibody) validated in WB, Mplex to detect monomethyl-Histone H4 (Lys20) also known as H4K20me1, Histone H4 (mono methyl K20).
More>>Use Anti-monomethyl-Histone H4 (Lys20) Antibody, clone NL314 (rabbit monoclonal antibody) validated in WB, Mplex to detect monomethyl-Histone H4 (Lys20) also known as H4K20me1, Histone H4 (mono methyl K20). Less<<
SDB (Sicherheitsdatenblätter), Analysenzertifikate und Qualitätszertifikate, Dossiers, Broschüren und andere verfügbare Dokumente.
Histones are highly conserved proteins that serve as the structural scaffold for the organization of nuclear DNA into chromatin. The four core histones, H2A, H2B, H3, and H4, assemble into an octamer (2 molecules of each). Histones are modified post-translationally by the actions of enzymes in both the nucleus and cytoplasm. These modifications, which include acetylation, phosphorylation, methylation, and ubiquitin-ation, occur predominantly on the N-terminal and C-terminal tails that extend beyond the nucleosome core particle. Trimethylation of histone H4 on lys20 (H4-K20me3) selectively marks constitutive pericentromeric hetero-chromatin and imprinting control regions, while mono- and dimethylation are broadly distributed but principally enriched in euchromatin regions. Although the biological function of H4K20me remains poorly understood, studies suggest that H4-K20me2 is involved in the guidance of DNA repair proteins to DNA strand breaks, whereas H4K20me1 is associated with chromatin condensation processes. PR-Set7 (also known as SET8) specifically catalyzes monomethylation of H4K20me1.
Use Anti-monomethyl-Histone H4 (Lys20) Antibody, clone NL314 (rabbit monoclonal antibody) validated in WB, Mplex to detect monomethyl-Histone H4 (Lys20) also known as H4K20me1, Histone H4 (mono methyl K20).
Key Applications
Western Blotting
Multiplexing
Application Notes
Immunoblot Analysis: A 1:4000 dilution of a previous lot detected methylated histone H3 in acid extracted proteins from HeLa cells. The antibody did not detect unmethylated recombinant Histone H3.
Multiplexing: Beadlyte® Histone-Peptide Specificity Assay: 1:2,000-1:30,000 dilutions of a previous lot were incubated with histone H4 peptides containing various modifications conjugated to Luminex® microspheres. Specificity to monomethyl-histone H4 (Lys20) was demonstrated (Figure C).
Biological Information
Immunogen
KLH-conjugated, synthetic peptide containing the sequence …HR[mmK]V…, in which mmK corresponds to monomethyl-lysine at residue 20 of human histone H4.
Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures. This gene is intronless and encodes a member of the histone H4 family. Transcripts from this gene lack polyA tails but instead contain a palindromic termination element. This gene is found in the large histone gene cluster on chromosome 6.
FUNCTION: SwissProt: P62805 # Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. SIZE: 103 amino acids; 11367 Da SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. SUBCELLULAR LOCATION: Nucleus. PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage (By similarity). & Ubiquitinated by the CUL4-DDB-RBX1 complex in response to ultraviolet irradiation. This may weaken the interaction between histones and DNA and facilitate DNA accessibility to repair proteins. SIMILARITY: SwissProt: P62805 ## Belongs to the histone H4 family.
Molecular Weight
10kDa
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Quality Assurance
Routinely evaluated by immunoblot analysis. Immunoblot Analysis: A 1:1000-1:2000 dilution of this lot detected monomethyl histone H4 (Lys20) in HeLa acid extracts. (Figure A).
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Storage and Shipping Information
Storage Conditions
Stable for 1 year at -20°C from date of receipt. For maximum recovery of product, centrifuge the vial prior to removing the cap.
Histones undergo post-translational modifications that are linked to important biological processes. Previous studies have indicated that lysine methylation correlating with closed or repressive chromatin is absent in the budding yeast Saccharomyces cerevisiae, including at H4 lysine 20 (K20). Here we provide functional evidence for H4 K20 monomethylation (K20me1) in budding yeast. H4 K20me1 is detectable on endogenous H4 by western analysis using methyl-specific antibodies, and the signal is abrogated by H4 K20 substitutions and by competition with H4 K20me1 peptides. Using chromatin immunoprecipitation, we show that H4 K20me1 levels are highest at heterochromatic locations, including subtelomeres, the silent mating type locus, and rDNA repeats, and lowest at centromeres within euchromatin. Further, an H4 K20A substitution strongly reduced heterochromatic reporter silencing at telomeres and the silent mating type locus and led to an increase in subtelomeric endogenous gene expression. The correlation between the location of H4 K20me1 and the effect of the H4 K20A substitution suggests that this modification plays a repressive function. Our findings reveal the first negative regulatory histone methylation in budding yeast and indicate that H4 K20me1 is evolutionarily conserved from simple to complex eukaryotes.
Certain and progressive methylation of histone H4 at lysine 20 during the cell cycle. Pesavento, James J, et al. Mol. Cell. Biol., 28: 468-86 (2008)
2008
Distinct histone lysine methylation marks are involved in transcriptional repression linked to the formation and maintenance of facultative heterochromatin, although the underlying mechanisms remain unclear. We demonstrate that the malignant-brain-tumor (MBT) protein L3MBTL1 is in a complex with core histones, histone H1b, HP1gamma, and Rb. The MBT domain is structurally related to protein domains that directly bind methylated histone residues. Consistent with this, we found that the L3MBTL1 MBT domains compact nucleosomal arrays dependent on mono- and dimethylation of histone H4 lysine 20 and of histone H1b lysine 26. The MBT domains bind at least two nucleosomes simultaneously, linking repression of transcription to recognition of different histone marks by L3MBTL1. Consistently, L3MBTL1 was found to negatively regulate the expression of a subset of genes regulated by E2F, a factor that interacts with Rb.
A trans-tail histone code defined by monomethylated H4 Lys-20 and H3 Lys-9 demarcates distinct regions of silent chromatin. Sims, Jennifer K, et al. J. Biol. Chem., 281: 12760-6 (2006)
2005
Millipore’s Histone H4 antibodies demonstrate specificity against linker histone H4. See below for H4 Antibodies, ChipAb+ Primer sets, and peptides, based on the expertise of Upstate & Chemicon. Weitere Informationen >>
