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SRP0178

Sigma-Aldrich

Histone H4 full length human

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

Synonym(s):

HIST2H4A

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

biological source

human

recombinant

expressed in E. coli

assay

≥80% (SDS-PAGE)

form

aqueous solution

mol wt

12.1 kDa

packaging

pkg of 1 mg

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)

General description

Human Histone 4 (HIST2H4A) (GenBank Accession No. NM_003548), amino acids 2-104 (end) with N-terminal His-tag, MW = 12.1 kDa, expressed in an E. coli expression system.

Application

Suitable substrate for histone methyltransferases.

Biochem/physiol Actions

Histones H2B and H4 are found to become mobilized during an infection with HSV-1 (herpes simplex virus-1) and become available for binding to viral genome.

Physical form

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

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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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Recognition and classification of histones using support vector machine.
Bhasin M
Journal of Computational Biology : A Journal of Computational Molecular Cell Biology, 13, 102-112 (2006)
Core histones H2B and H4 are mobilized during infection with herpes simplex virus 1.
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Articles

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

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