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Key Documents

12-359

Sigma-Aldrich

Acetyl-Histone H3 Peptide

Lys14

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About This Item

UNSPSC Code:
12352202
eCl@ss:
32160405
NACRES:
NA.41

product name

Acetyl-Histone H3 (Lys14) Peptide, Routinely evaluated by Dot Blot Assay. This peptide was recognized on a dot blot using Anti-acetyl Histone H3 (Lys14). The peptide was not recognized by anti-acetyl Histone H3 (Lys9) or anti-acetyl Histone H3 (Lys9,14).

Quality Level

100

manufacturer/tradename

Upstate®

technique(s)

immunocytochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable

NCBI accession no.

NM_002107.3

UniProt accession no.

Q16695

shipped in

dry ice

Gene Information

human ... H3F3B(3021)

Quality

Routinely evaluated by Dot Blot Assay. This peptide was recognized on a dot blot using Anti-acetyl Histone H3 (Lys14), (06-911). The peptide was not recognized by anti-acetyl Histone H3 (Lys9) or anti-acetyl Histone H3 (Lys9,14).

Physical form

Lyophilized powder

Storage and Stability

2 years at -20°C

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

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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Opening the way to gene activity
Pennisi, E
Science (New York, N.Y.), 275, 155-157 (1997)
A B Ruiz-García et al.
FEBS letters, 403(2), 186-190 (1997-02-17)
Enzymatic extracts from a gcn5 mutant and wild-type strains of Saccharomyces cerevisiae were chromatographically fractionated and the histone acetyltransferase activities compared. When free histones were used as substrate, extracts from wild-type cells showed two peaks of activity on histone H3
Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines.
Kuo, M H, et al.
Nature, 383, 269-272 (1996)

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