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Flow Cytometry Analysis:
Representative lot data. FC analysis using untreated HeLa cells stained with Anti-Ubiquityl Histone H2A PE antibody (ye...
Milli-Mark™ Anti-ubiquityl-Histone H2A-PE, clone E6C5
| Species Reactivity | Key Applications | Host | Format | Antibody Type |
|---|---|---|---|---|
| H | FC | Mouse | Phycoerythrin | Monoclonal Antibody |
Description:
Milli-Mark™ Anti-ubiquityl-Histone H2A-PE, clone E6C5
Trade Name:
Milli-Mark
Specificity:
Antibody recognizes Human Ubiquityl Histone H2A.
Molecular Weight:
14 kDa Calculated
Immunogen:
AMA (human epithelial amnion) cell residual nuclear pellet portions
Clone:
E6C5
Isotype:
IgM
Background Information:
Histones are highly conserved proteins that serve as the structural scaffold for the organization of nuclear DNA into chromatin. Histones are modified post-translationally by acetylation, phosphorylation, methylation, and ubiquitination and these modifications regulate DNA transcription, repair, recombination, and replication. Ubiquitylation usually targets the substrate for degradation, although histones H2A and H2B are actually stabilized by a single ubiquitin conjugation. Histone ubiquitination has been correlated with DNA repair and transcription, cellular differentiation, cell cycle regulation, spermatogenesis, protein trafficking, and response to stress. Histone H2A is monoubiquitinated at Lys119 by the PRC-1L complex (Polycomb repressive complex 1-like), which includes Ring1, Ring2, Bmi1 and HPH2. Ubiquitinated H2A normally represents about 15% of H2A, but this value can be as high as 50% in active chromatin. Ubiquitinyl histone H2A has also been associated with transcriptional silencing of large chromatin regions and linked to Polycomb silencing so the function of ubiquitinated H2A remains undefined.
Species Reactivity:
Human
Species Reactivity Note:
Tested and passed on Human.
Control:
HeLa cells
Quality Assurance:
Evaluated by flow cytometry using HeLa cells
Purification Method:
Ammonium Sulfate
Presentation:
Purified mouse monoclonal IgM conjugated to PE in PBS buffer with 15mg/mL BSA and sodium azide at 0.1%.
Storage Conditions:
Maintain refrigerated at 2-8°C protected from light for up to 6 months from date of receipt.
UniProt Number:
Entrez Gene Number:
Gene Symbol:
H2AFQ
Alternate Names:
- Histone H2A-GL101
- Histone H2A/q
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.
Key Applications:
Flow Cytometry
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 is intronless and encodes a member of the histone H2A family.
UniProt Summary:
FUNCTION: SwissProt: Q96QV6 # 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: 131 amino acids; 14234 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: The chromatin-associated form is phosphorylated on Thr-121 during mitosis (Probable). & Deiminated on Arg-4 in granulocytes upon calcium entry. & Monoubiquitination of Lys-120 by RING1 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3. Monoubiquitination of Lys-120 by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. & Phosphorylation on Ser-2 is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. & Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage (By similarity).
SIMILARITY: SwissProt: Q96QV6 ## Belongs to the histone H2A family.
SIZE: 131 amino acids; 14234 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: The chromatin-associated form is phosphorylated on Thr-121 during mitosis (Probable). & Deiminated on Arg-4 in granulocytes upon calcium entry. & Monoubiquitination of Lys-120 by RING1 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3. Monoubiquitination of Lys-120 by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. & Phosphorylation on Ser-2 is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. & Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage (By similarity).
SIMILARITY: SwissProt: Q96QV6 ## Belongs to the histone H2A family.
Protein/Isoform Description:
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.
Product Name:
Milli-Mark™ Anti-ubiquityl-Histone H2A-PE, clone E6C5
Antibody Type:
Monoclonal Antibody
Qty/Pk:
100 tests
Format:
Phycoerythrin
Host:
Mouse