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Key Documents

SRP0161

Sigma-Aldrich

Histone H4 peptide (1-21) human

≥90% (HPLC)

Sinónimos:

HIST2H4A

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

biological source

human

assay

≥90% (HPLC)

form

aqueous solution

mol wt

~2 kDa

packaging

pkg of 160 nmol

storage condition

avoid repeated freeze/thaw cycles

concentration

>0.02 mg/mL

NCBI accession no.

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... HIST2H4A(8370)

Application

Study enzyme kinetics, and screen small molecular inhibitors of Histone 3 R3 methyltransferases for drug discovery and HTS applications

Biochem/physiol Actions

H4 (histone 4) is a core histone protein which is mobilized during herpes simplex virus 1 (HSV1) infection. This leads to elevated pools of free H2B and H4 and decreased rate of H2B fast chromatin exchange. Free H4 associates with HSV1 genomes, and this mobilization is also linked with the organization of H2A-H2B and H3-H4 dimers into unstable nucleosomes with HSV-1 genomes. The histone chaperone nuclear autoantigenic sperm protein (NASP) is responsible for maintaining a reservoir of soluble H3-H4 histones, where it regulates the activity of heat shock proteins Hsc70 and Hsp90, which target H3-H4 for degradation by chaperone-mediated autophagy. This reservoir level, in turn, depends upon the level of NASP.

Physical form

Supplied as water solution, 800 μM

Preparation Note

Thaw on ice. Upon first thaw, briefly spin tube to recover full content of the tube. Aliquot into single use aliquots. Store remaining product in aliquots at -70°C. Note: Avoid freeze/thaw cycles.

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

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A specific function for the histone chaperone NASP to fine-tune a reservoir of soluble H3-H4 in the histone supply chain.
Molecular Cell, 44(6), 918-927 (2011)
Core histones H2B and H4 are mobilized during infection with herpes simplex virus 1.
Conn KL, et al.
Journal of Virology, 85(24), 13234-13252 (2011)
The histone variant H3.3 marks active chromatin by replication-independent nucleosome assembly.
Ahmad K and Henikoff S
Molecular Cell, 9(6), 1191-1200 (2002)
A comprehensive view of the epigenetic landscape part I: DNA methylation, passive and active DNA demethylation pathways and histone variants.
Sadakierska-Chudy A
Neurotoxicity Research, 27(1), 84-97 (2015)

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