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Acid-extracted histones from Hela cells was resolved by electrophoresis, transferred to nitrocellulose and probed with anti trimethyl-Histone H3 (Lys2 ...
ChIPAb+ Trimethyl-Histone H3 (Lys27) antibody/primer set; 25 assays
| Species Reactivity | Key Applications | Host | Format | Antibody Type |
|---|---|---|---|---|
| H, M | ChIP, WB | Rabbit | null | Polyclonal Antibody |
UniProt Number:
UniProt Summary
FUNCTION: SwissProt: Q16695 # 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: 136 am ... see more »
SIZE: 136 am ... see more »
Entrez Gene Number:
Entrez Gene Summary
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 contains introns and its mRNA is polyad
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Description:
ChIPAb+ Trimethyl-Histone H3 (Lys27) antibody/primer set; 25 assays
Specificity:
trimethyl-Histone H3 (Lys27)
Key Applications:
- Chromatin Immunoprecipitation
- Western Blotting
Species Reactivity:
- Human
- Mouse
Species Reactivity Note:
Broad species cross-reactivity expected.
Immunogen:
KLH-conjugated, synthetic 2X-branched peptide containing the sequence ...AR(me3K)SAP... in which me3K corresponds to trimethyl-lysine at residue 27 of human Histone H3.
Molecular Weight:
17kDa
Control:
- 1 vial containing 75µl of 5µM of each control primer specific for mouse p16 promoter. Store at -20°C.
- FOR: ACA CTC CTT GCC TAC CTG AA
- REV: CGA ACT CGA GGA GAG CCA TC
Presentation:
1 vial containing 100µl serum.
Storage Conditions:
1 year at -20°C from date of shipment
Gene Symbol:
- H3F3A
- MGC87783
- H3.3A
- MGC87782
- H3F3
- H3.3B
- H3F3B
Quality Assurance:
Routinely evaluated by chromatin immunoprecipitation and immunoblot on HeLa nuclear lysate.
Components:
- Anti-trimethyl Histone H3(Lys27) polyclonal, 1 vial
- Polyclonal control rabbit serum, 1 vial
- Murine p16 promoter primer set, 1 vial
Antibody Category:
Nuclear Function
Antibody Sub-Category:
Histones
Descriptive Text:
Histones are highly conserved proteins that serve as the structural scaffold for the organization of nuclear DNA into chromatin. The histones have an amino terminal tail, a globular domain, and a carboxy-terminal tail. The four core histones, H2A, H2B, H3 and H4 assemble into the octamer (2 molecules of each). Subsequently, 146 base pairs of DNA are wrapped in a sequence-independent manner around the octamer, forming the basic subunit of chromatin, the nucleosome. The distance between nucleosomes varies from species to species but generally is between 180 and 200 base pairs for higher organisms. Histone H1, the most common form of linker histone, binds to nucleosomal DNA at the point from which the DNA exits the nucleosome, and is required for higher order packing of chromatin.
Histones are modified post-translationally by the actions of enzymes in both the nucleus and cytoplasm that deposit specific functional groups. These modifications help to regulate the processes that depend on DNA, such as transcription, DNA repair, recombination and replication. The most commonly studied and best understood modifications are acetylation, phosphorylation, methylation, and to a lesser extent ubiquitination. The modifications occur predominantly on the amino terminal tails that extend out beyond the nucleosome core particle, but certain modifications have also been identified on the C-terminal tails and globular domains of some histones. Acetylation occurs on the epsilon amino group of lysine residues of all four core histones, and increases in acetylation in are correlated strongly with increases in gene expression.
Indeed, many histone acetyltransfease enzymes (HATs) form the catalytic subunits of transcriptional activating protein complexes. Histone deacetylases (HDACs) remove acetyl marks, antagonizing the activity of HATs and lead to decreases in transcription (see above). Phosphorylation occurs on serine residues in the amino termini of all four core histones and in multiple regions of H1. Phosphorylation of serines 10 and 28 of H3 occur during chromosome condensation in mitosis, and antibodies to these sites are excellent mitotic markers. H2B is phosphorylated at lysines 14 and 32 in cells undergoing apoptosis, and the histone variant H2A.X is phosphorylated at serine 139 in response to DNA damage. Histone methylation has recently become a popular research topic, and occurs on both lysine and arginine residues. Arginine methylation appears to be associated predominantly with transcriptional activation, whereas two specific lysine methylation events on histone H3 are hallmarks of either active chromatin (euchromatin) or silenced chromatin (heterochromatin). Ubiquitination is the least understood of the histone modifications and occurs on the C-terminal tails of H2A and H2B, and in some cases is a necessary precursor to specific histone methylation events.
Using a technique known as chromatin immunoprecipitation (ChIP), it is possible to analyze the variety of histone modifications present within a given promoter region or even an entire gene locus. Antibodies specific to the modification of interest are used to enrich for regions of chromatin (sheared to a manageable size and harvested from cells) that contain the modification, and various detection methods (Southern blot, PCR, microarray) are employed to detect specific DNA sequences within the enriched chromatin. This data is very useful in analyzing the involvement of a modification in specific biological processes.
Histones are modified post-translationally by the actions of enzymes in both the nucleus and cytoplasm that deposit specific functional groups. These modifications help to regulate the processes that depend on DNA, such as transcription, DNA repair, recombination and replication. The most commonly studied and best understood modifications are acetylation, phosphorylation, methylation, and to a lesser extent ubiquitination. The modifications occur predominantly on the amino terminal tails that extend out beyond the nucleosome core particle, but certain modifications have also been identified on the C-terminal tails and globular domains of some histones. Acetylation occurs on the epsilon amino group of lysine residues of all four core histones, and increases in acetylation in are correlated strongly with increases in gene expression.
Indeed, many histone acetyltransfease enzymes (HATs) form the catalytic subunits of transcriptional activating protein complexes. Histone deacetylases (HDACs) remove acetyl marks, antagonizing the activity of HATs and lead to decreases in transcription (see above). Phosphorylation occurs on serine residues in the amino termini of all four core histones and in multiple regions of H1. Phosphorylation of serines 10 and 28 of H3 occur during chromosome condensation in mitosis, and antibodies to these sites are excellent mitotic markers. H2B is phosphorylated at lysines 14 and 32 in cells undergoing apoptosis, and the histone variant H2A.X is phosphorylated at serine 139 in response to DNA damage. Histone methylation has recently become a popular research topic, and occurs on both lysine and arginine residues. Arginine methylation appears to be associated predominantly with transcriptional activation, whereas two specific lysine methylation events on histone H3 are hallmarks of either active chromatin (euchromatin) or silenced chromatin (heterochromatin). Ubiquitination is the least understood of the histone modifications and occurs on the C-terminal tails of H2A and H2B, and in some cases is a necessary precursor to specific histone methylation events.
Using a technique known as chromatin immunoprecipitation (ChIP), it is possible to analyze the variety of histone modifications present within a given promoter region or even an entire gene locus. Antibodies specific to the modification of interest are used to enrich for regions of chromatin (sheared to a manageable size and harvested from cells) that contain the modification, and various detection methods (Southern blot, PCR, microarray) are employed to detect specific DNA sequences within the enriched chromatin. This data is very useful in analyzing the involvement of a modification in specific biological processes.
Packaging:
25 assays per kit, ~4µl per chromatin immunoprecipitation.
Trade Name:
Upstate (Millipore)
Product Overview:
Every lot of the ChIPAb+ line of antibodies is individually validated for chromatin precipitation, in order to guarantee successful ChIP assays every time. Each antibody includes a control primer set for performance confirmation. Trimethyl-Histone H3 (Lys27) antibody is functionally validated in the precipitation of chromatin that carries trimethyl-Histone H3 (Lys27).
The qPCR primers included amplifies the mouse p16 promoter region where trimethyl-Histone H3 (Lys27) is enriched.
The qPCR primers included amplifies the mouse p16 promoter region where trimethyl-Histone H3 (Lys27) is enriched.
Antibody Type:
Polyclonal Antibody
Host:
Rabbit