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Key Documents

SRP0158

Sigma-Aldrich

Histone H3 (2-58) human

recombinant, expressed in E. coli, ≥70% (SDS-PAGE)

Sinonimo/i:

HIST1H3E, Histone H3.1

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About This Item

Codice UNSPSC:
12352200
NACRES:
NA.32

Origine biologica

human

Ricombinante

expressed in E. coli

Saggio

≥70% (SDS-PAGE)

Forma fisica

aqueous solution

PM

32 kDa

Confezionamento

pkg of 500 μg

Condizioni di stoccaggio

avoid repeated freeze/thaw cycles

Concentrazione

>0.02 mg/mL

N° accesso NCBI

N° accesso UniProt

Condizioni di spedizione

dry ice

Temperatura di conservazione

−70°C

Informazioni sul gene

human ... HIST1H3E(8353)

Descrizione generale

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.

Applicazioni

Suitable substrate for histone methyltransferases

Azioni biochim/fisiol

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.

Stato fisico

Formulated in 25 mM Tris-HCl, pH 8.0, 100 mM NaCl, 0.05% Tween-20, 20% glycerol and 3 mM DTT.

Nota sulla preparazione

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.

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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

Articoli

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

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