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Merck

SRP0177

Histone H3 full length human

recombinant, expressed in E. coli, ≥80% (SDS-PAGE)

Sinónimos:

HIST1H3E, Histone H3.1

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1 MG

US$ 905,00

US$ 905,00

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NACRES:
NA.32
UNSPSC Code:
12352200

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Nombre del producto

Histone H3 full length human, recombinant, expressed in E. coli, ≥80% (SDS-PAGE)

biological source

human

recombinant

expressed in E. coli

assay

≥80% (SDS-PAGE)

form

aqueous solution

mol wt

15.4 kDa

packaging

pkg of 1 mg

storage condition

avoid repeated freeze/thaw cycles

concentration

>0.02 mg/mL

technique(s)

activity assay: suitable

solubility

water: soluble

suitability

suitable for molecular biology

NCBI accession no.

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... HIST1H3E(8353)

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Este artículo
SRP0158SRP0160H2292
recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

-

recombinant

expressed in E. coli

assay

≥80% (SDS-PAGE)

assay

≥70% (SDS-PAGE)

assay

≥90% (HPLC)

assay

-

technique(s)

activity assay: suitable

technique(s)

-

technique(s)

-

technique(s)

MALDI-TOF: suitable

biological source

human

biological source

human

biological source

human

biological source

human

concentration

>0.02 mg/mL

concentration

>0.02 mg/mL

concentration

>0.02 mg/mL

concentration

1 mg/mL

form

aqueous solution

form

aqueous solution

form

aqueous solution

form

liquid

Application

Histone H3 full-length human has been used as a substrate in in vitro kinase assay for Aurora-A (AURKA) kinase and Tousled-Like Kinase 2(TLK2)[1]. Histone H3 full-length human has been used in the generation of antibodies in chickens.[2] It has also been used in in vitro methylation assay.[3]

Biochem/physiol Actions

Histones are important for proper organization and modification of chromatin.[4] HIST1H3E (histone 3, also referred to as H3.1) is mainly associated with DNA synthesis during DNA replication and might also be involved in DNA repair.[5] It is added to the chromatin at the time of DNA replication-associated chromatin assembly. During HSV-1 (herpes simplex virus 1) infection, differential movement of HIST1H3E is associated with the assembly of viral chromatin.[6]

General description

Research area: Cell signaling. The gene HIST1H3E (histone 3, also referred to as H3.1) is mapped to human chromosome 6p22.[7] It is a variant of histone 3 and is also called the replicative histone.[8] HIST1H3E is mainly expressed in the S-phase.[9] In the process of cellular differentiation, HIST1H3E mRNA levels go down as cell division slows down.[5]Human HIST1H3E, GenBank Accession No. NM_003532, amino acids 2-137 (end) with N-terminal His-tag, MW = 15.4kDa, expressed in an Escherichia coli expression system.

Physical form

Formulated in 10 mM PBS, pH 7.4, 130 mM NaCl, 10% glycerol and 1 mM DTT.

Preparation Note

Thaw on ice. Upon first thaw, briefly spin tube containing protein to recover full content of the tube. Aliquot protein into single use aliquots. Store remaining undiluted protein in aliquots at -70°C. Note: Protein is very sensitive to freeze/thaw cycles.

Clase de almacenamiento

10 - Combustible liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis.
Tagami H
Cell, 116, 51-61 (2004)
The human histone H3 complement anno 2011.
Ederveen TH
Biochimica et Biophysica Acta, 1809, 577-586 (2011)
Jona Merx et al.
Scientific reports, 12(1), 19251-19251 (2022-11-11)
Posttranslational modifications (PTMs) on histone tails regulate eukaryotic gene expression by impacting the chromatin structure and by modulating interactions with other cellular proteins. One such PTM has been identified as serine and threonine glycosylation, the introduction of the ß-N-acetylglucosamine (GlcNAc)
Kami Ahmad et al.
Molecular cell, 9(6), 1191-1200 (2002-06-28)
Two very similar H3 histones-differing at only four amino acid positions-are produced in Drosophila cells. Here we describe a mechanism of chromatin regulation whereby the variant H3.3 is deposited at particular loci, including active rDNA arrays. While the major H3
Kristen L Conn et al.
PLoS pathogens, 9(10), e1003695-e1003695 (2013-10-17)
During lytic infections, HSV-1 genomes are assembled into unstable nucleosomes. The histones required for HSV-1 chromatin assembly, however, are in the cellular chromatin. We have shown that linker (H1) and core (H2B and H4) histones are mobilized during HSV-1 infection

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