SRP0408
Histone Octamer full length human
recombinant, expressed in E. coli, ≥90% (SDS-PAGE)
Szinonimák:
Histone Octamer
Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez
Összes fotó(1)
About This Item
UNSPSC kód:
12352200
NACRES:
NA.32
Az árazás és az elérhetőség jelenleg nem elérhető
Javasolt termékek
biológiai forrás
human
rekombináns
expressed in E. coli
Teszt
≥90% (SDS-PAGE)
Forma
aqueous solution
molekulatömeg
113.8 kDa
kiszerelés
pkg of 100 μg
technika/technikák
cell based assay: suitable
oldhatóság
water: soluble
kiszállítva
dry ice
tárolási hőmérséklet
−70°C
Géninformáció
human ... HIST1H2BG(8339) , HIST2H2AC(8338) , HIST3H3(8290) , HIST4H4(121504)
Általános leírás
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.[1]
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.[1]
Alkalmazás
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.[2]
Biokémiai/fiziológiai hatások
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.[3] 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.[4]
Tárolási osztály kódja
10 - Combustible liquids
WGK
WGK 1
Lobbanási pont (F)
Not applicable
Lobbanási pont (C)
Not applicable
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Az ügyfelek ezeket is megtekintették
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
Covalent histone modification by an electrophilic derivative of the anti-HIV drug nevirapine
Harjivan SG, et al.
Molecules (Basel), 26(5), 1349-1349 (2021)
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)
Histone chaperones and nucleosome assembly
Akey CW and Luger K
Current Opinion in Structural Biology, 13(1), 6-14 (2003)
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