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Key Documents

SRP0158

Sigma-Aldrich

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

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.

NM_003532

UniProt accession no.

P68431

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.

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)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Selective methylation of histone H3 variant H3.1 regulates heterochromatin replication.
Jacob Y, et al.
Science, 343, 1249-1249 (2014)
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)
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)
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
View All Related Papers

Articles

Histone Modification and Chromatin Remodeling | Epigenetics

Epigenetic modifications are thought to occur through two key interconnected processes—DNA methylation and the covalent modification of histones.

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