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Key Documents

14-494

Sigma-Aldrich

Histone H3, human recombinant

Recombinant human histone H3.

Synonyma:

H3, Histone H3

Přihlásitk zobrazení cen stanovených pro organizaci a smluvních cen


About This Item

UNSPSC Code:
12352202
eCl@ss:
32160405
NACRES:
NA.32

biological source

human

Quality Level

recombinant

expressed in E. coli

mol wt

Mw ~17 kDa

manufacturer/tradename

Upstate®

technique(s)

activity assay: suitable

NCBI accession no.

UniProt accession no.

shipped in

dry ice

Gene Information

human ... H3F3B(3021)

General description

Product Source: human histone H3 produced in E. coli

Application

Recombinant human histone H3.

Packaging

also available in larger sizes, please inquire for pricing and availability.

Quality

routinely evaluated by its use as a substrate for in vitro enzymatic reactions, such as acetylation by PCAF

Physical form

FPLC agarose column
Lyophilized powder

Storage and Stability

Lyophilized: Stable for 2 years at -20°C from date of shipment. Rehydrated: Stable for 6 months at -20°C. Aliquot rehydrated solution to avoid repeated freezing and thawing

Other Notes

For Specific Activity data, refer to the Certificate of Analysis for individual lots of this enzyme.

Legal Information

UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Histones are the primary protein component of chromatin and are involved in virtually all DNA-templated processes. Histones are abundantly post-translationally modified by a variety of chromatin-modifying machinery. These post-translational modifications (PTMs) are recognized by a range of "reader" proteins, which
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