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Safety Information

SRP0408

Sigma-Aldrich

Histone Octamer full length human

recombinant, expressed in E. coli, ≥90% (SDS-PAGE)

Synonym(s):

Histone Octamer

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

biological source

human

recombinant

expressed in E. coli

Assay

≥90% (SDS-PAGE)

form

aqueous solution

mol wt

113.8 kDa

packaging

pkg of 100 μg

technique(s)

cell based assay: suitable

solubility

water: soluble

shipped in

dry ice

storage temp.

−70°C

General description

Human recombinant histone octamer consisting of 2 molecules each of histones H2A (GenBank Accession No. NM_033445) amino acids 2-130(end) with a N-terminal His-tag, H2B (GenBank Accession No. NM_003528) amino acids 2-126(end) with a N-terminal His-tag, H3 (GenBank Accession No. NM_003532) amino acids 2-137(end) with a N-terminal His-tag, and H4 (GenBank Accession No. NM_003548) amino acids 2-103(end) with a N-terminal His-tag, expressed in an E. coli expression system.
Research Area: Cell Signaling
The histone octamer is a versatile protein assembly that has evolved to serve two opposing functions within the cell. It is required to bind and bend DNA to achieve fivefold compaction and partial charge neutralization of DNA, while also needing to release specific segments of DNA in a coordinated manner to allow the access of DNA-processing enzymes at the appropriate time. A modular assembly of histone dimers (consisting of either H2A and H2B or H3 and H4) binds to approximately 30 bp of DNA and is connected in a flexible yet stable manner to form a fundamental superhelical ′ramp′ with evenly spaced DNA-binding platforms.

Application

Histone Octamer full length human has been used to incubate with 12-mesyloxy-NVP along with recombinant human histone H4 to investigate the potential of histones as targets for covalent adduct formation by drug-derived electrophiles.

Biochem/physiol Actions

The nuclear DNA in eukaryotes is found to be associated with histones to form a compact complex called nucleosome. Histones neutralize the electrostatic nature of DNA and function as scaffolding proteins. Each core nucleosome contains two copies each of the core histones H2A, H2B, H3, and H4 to form an octameric complex. This octameric complex contains a central (H3-H4)2 tetramer flanked on both sides with H2A-H2B dimers. The octamer complex function in various stages of chromosome function, chromatin assembly and nucleosome formation. The histone dimer-tetramer interactions are also important in RNA transcription.

Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

PDSCL

Deleterious substance

JAN Code

SRP0408-100UG:


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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Kyle M Miller et al.
Biochemical Society transactions, 40(2), 370-376 (2012-03-23)
Inherited or acquired defects in detecting, signalling or repairing DNA damage are associated with various human pathologies, including immunodeficiencies, neurodegenerative diseases and various forms of cancer. Nuclear DNA is packaged into chromatin and therefore the true in vivo substrate of
Vishal V Raut et al.
Annals of botany, 108(7), 1235-1246 (2011-09-08)
In eukaryotes, chromatin remodelling complexes are shown to be responsible for nucleosome mobility, leading to increased accessibility of DNA for DNA binding proteins. Although the existence of such complexes in plants has been surmised mainly at the genetic level from
The nucleosomal core histone octamer at 3.1 A resolution: a tripartite protein assembly and a left-handed superhelix.
Arents G
Proceedings of the National Academy of Sciences of the USA, 88, 10148-10152 (1991)
Histone octamer function in vivo: mutations in the dimer-tetramer interfaces disrupt both gene activation and repression.
Santisteban MS
The Embo Journal, 16, 2493-2506 (1997)

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