SRP0158
Histone H3 (2-58) human
recombinant, expressed in E. coli, ≥70% (SDS-PAGE)
Synonym(s):
HIST1H3E, Histone H3.1
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About This Item
UNSPSC Code:
12352200
NACRES:
NA.32
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biological source
human
recombinant
expressed in E. coli
Assay
≥70% (SDS-PAGE)
form
aqueous solution
mol wt
32 kDa
packaging
pkg of 500 μg
storage condition
avoid repeated freeze/thaw cycles
concentration
>0.02 mg/mL
NCBI accession no.
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... HIST1H3E(8353)
General description
The mammalian chromatin is present in nucleosomes, made of histone octamers (H2A,H2B,H3,H4)2. Mammals contain three main classes of histone H3 variants: the replicative histones (H3.1 and H3.2), the replacement histone (H3.3) and the centromeric histone (Cenp-A).
Human Histone 3 (GenBank Accession No. NM_003532), (amino acid 2-58) with N-terminal GST tag, MW = 32kDa, expressed in an Escherichia coli expression system.
Human Histone 3 (GenBank Accession No. NM_003532), (amino acid 2-58) with N-terminal GST tag, MW = 32kDa, expressed in an Escherichia coli expression system.
Application
Suitable substrate for histone methyltransferases
Biochem/physiol Actions
Histone proteins are basic building blocks of chromatin. H3.1 (also referred to as HIST1H3E) is mainly expressed in the S phase and is termed as replication-dependent histone. Selective methylation of H3.1 controls replication in heterochromatin area.
Physical form
Formulated in 25 mM Tris-HCl, pH 8.0, 100 mM NaCl, 0.05% Tween-20, 20% glycerol and 3 mM DTT.
Preparation Note
Thaw on ice. Upon first thaw, briefly spin tube containing enzyme to recover full content of the tube. Aliquot enzyme into single use aliquots. Store remaining undiluted enzyme in aliquots at -70°C. Note: Enzyme is very sensitive to freeze/thaw cycles.
Certificates of Analysis (COA)
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Selective methylation of histone H3 variant H3.1 regulates heterochromatin replication.
Jacob Y, et al.
Science, 343, 1249-1249 (2014)
Topography of the histone octamer surface: repeating structural motifs utilized in the docking of nucleosomal DNA.
Arents G and Moudrianakis EN
Proceedings of the National Academy of Sciences of the USA, 90, 10489-10489 (1993)
Genome-wide analysis of histone H3 lysine 4 trimethylation in peripheral blood mononuclear cells of minimal change nephrotic syndrome patients.
Zhang L, et al.
American Journal of Nephrology, 30, 505-505 (2009)
Eric I Campos et al.
Nature structural & molecular biology, 17(11), 1343-1351 (2010-10-19)
The mechanism by which newly synthesized histones are imported into the nucleus and deposited onto replicating chromatin alongside segregating nucleosomal counterparts is poorly understood, yet this program is expected to bear on the putative epigenetic nature of histone post-translational modifications.
Alejandra Loyola et al.
Molecular cell, 24(2), 309-316 (2006-10-21)
Histone posttranslational modifications (PTMs) and sequence variants regulate genome function. Although accumulating evidence links particular PTM patterns with specific genomic loci, our knowledge concerning where and when these PTMs are imposed remains limited. Here, we find that lysine methylation is
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