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WB: Acid-extracted proteins from exponentially growing HeLa cells were probed with Anti-phospho Histone H3 (Ser10), (0.03µg/ml) with the following mod ...
Anti-phospho-Histone H3 (Ser10), clone RR002
| Species Reactivity | Key Applications | Host | Format | Antibody Type |
|---|---|---|---|---|
| H, Vrt, Nem | WB, IC, IH | Mouse | Affinity Purified | Monoclonal 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:
Anti-phospho-Histone H3 (Ser10), clone RR002
Background Information:
Histone H3 is one of the five main histone proteins involved in the structure of chromatin in eukaryotic cells. Featuring a main globular domain and a long N-terminal tail, H3 is involved with the structure of the nucleosomes of the 'beads on a string' structure. The N-terminal tail of histone H3 protrudes from the globular nucleosome core and can undergo several different types of epigenetic modifications that influence cellular processes. These modifications include the covalent attachment of methyl or acetyl groups to lysine and arginine amino acids and the phosphorylation of serine or threonine
Clone:
RR002
Specificity:
Recognizes Histone H3 phosphorylated at Serine 10.
Key Applications:
- Western Blotting
- Immunocytochemistry
- Immunohistochemistry
Species Reactivity:
- Human
- Vertebrates
- Nematode
Isotype:
IgG
Immunogen:
peptide (ARK[pS]TGGKAPRKQL-C) corresponding to amino acids 7-20 of human histone H3
Modifications:
Phosphorylation
Molecular Weight:
17 kDa
Control:
UV-treated 293 cell extracts, UV-treated HeLa cell extracts, breast cancer tissue, HEPG2 cell extrats
Presentation:
Protein A Purified immunoglobulin in Immunoaffinity Purified immunoglobulin in 0.2M Tris-glycine, pH 7.4, 0.15M NaCl, 5mg/ml BSA, 0.05% sodium azide before the addition of glycerol to 30%
Storage Conditions:
Maintain for 2 years at -20°C from date of shipment. Aliquot to avoid repeated freezing and thawing. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Gene Symbol:
- H3F3A
- H3F3
- MGC87782
- H3.3B
- MGC87783
- H3F3B
- H3.3A
Quality Assurance:
routinely evaluated by immunoblot on acid extracted proteins from colcemid-arrested HeLa cells
Antibody Category:
Nuclear Function
Antibody Sub-Category:
Histones
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.
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.
Format Code:
APur
Trade Name:
Upstate (Millipore)
Purification Method:
Immunoaffinity Purified
Format:
Affinity Purified
Antibody Type:
Monoclonal Antibody
Host:
Mouse