Histone H3.2 (Nucleosome) protein (Biotin)
Quick Overview for Histone H3.2 (Nucleosome) protein (Biotin) (ABIN7939152)
Target
Protein Type
Origin
Source
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Protein Characteristics
- Nucleosome
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Purification tag / Conjugate
- Biotin
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Purpose
- Recombinant Mononucleosomes H3.2 - biotin
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Characteristics
- Recombinant Mononucleosomes H3.2 - biotin consist of a 167 bp of 601 DNA with 5' biotin tag and two molecules each of histones H2A that includes amino acids 1-130 (end) (accession number NM_003512), H2B that includes amino acids 1-126 (end) (accession number NM_003518), H3.2 that includes amino acids 1-136 (end) (accession number NM_021059.3), and H4 that includes amino acids 1-103 (end) (accession number NM_003548). All of these histones were expressed in E. coli cells. The molecular weight of the histone octamer is 108 kDa. Recombinant Mononucleosomes H3.2 - biotin are suitable for use as substrates for histone modification enzymes, or to generate chromatin in vitro.
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Application Notes
- Recombinant Mononucleosomes H3.2 - biotin are suitable for use as substrates for histone modification enzymes, or to generate chromatin in vitro.
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Restrictions
- For Research Use only
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Format
- Liquid
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Buffer
- Recombinant Mononucleosomes H3.2 - biotin is supplied in 10 mM Tris-HCl pH 8.0, 1 mM EDTA, 2 mM DTT, and 20 % glycerol.
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Preservative
- Dithiothreitol (DTT)
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Precaution of Use
- This product contains Dithiothreitol (DTT): a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
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Handling Advice
- Avoid repeated freeze/thaw cycles,keep on ice when not in storage
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Storage
- -80 °C
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Storage Comment
- Recombinant proteins in solution are temperature sensitive and must be stored at -80°C to prevent degradation. Avoid repeated freeze/thaw cycles and keep on ice when not in storage.
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- Histone H3.2
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Background
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Protein Background: In vivo, histones are wrapped around by DNA in chromatin. Therefore, nucleosomes are more physiologically relevant substrates than histones and histone-derived peptides for in vitro studies. More importantly, some histone methyltransferases are signifcantly more active, as well as specifc, when using nucleosomal substrates in HMT assays, such as DOT1L and NSD family enzymes. Nucleosomes are also widely used in histone methyltransferase screening assays to identify small molecular inhibitors for drug discovery. Nuclear core histone H3 exist as several variants: H3.1, H3.2, H3.3, CENP-A and H3t. These variants have been suggested to have specific functions in the regulation of gene expression and genome stability. In mammals, histone H3 non-centromeric variants, H3.1, H3.2 and H3.3, differ in their chromatin deposition patterns and PTMs despite having a high degree of sequence similarity. H3.1 and H3.2, which are enriched in repressive chromatin marks, are predominantly expressed during S-Phase and deposited in DNA synthesis-coupled fashion during DNA replication and repair. In contrast, H3.3 is enriched in active chromatin marks and is expressed throughout the cell cycle. Canonical histone H3.2 is expressed during S phase and differs by only one amino acid residue from th variant histone H3.1, and four amino acid residues from histone H3.3. According to some researches, H3.1 is preferentially acetylated and dimethylated on lysines 14 and 9, respectively, while H3.2 is preferentially subjected to trimethylation on lysine 27. Histones are linked to tumorigenesis primarily through alterations in their PTMs and the enzymes regulating these modifications, suggesting that they might disrupt the reading, writing, and/or erasing of these marks.
Short Description: Recombinant Mononucleosomes H3.2 - biotin consist of a 167 bp of 601 DNA with 5' biotin tag and two molecules each of histones H2A that includes amino acids 1-130 (end) (accession number NM_003512), H2B that includes amino acids 1-126 (end) (accession number NM_003518), H3.2 that includes amino acids 1-136 (end) (accession number NM_021059.3), and H4 that includes amino acids 1-103 (end) (accession number NM_003548). All of these histones were expressed in E. coli cells. The molecular weight of the histone octamer is 108 kDa.
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Molecular Weight
- 108 kDa
Target
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