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Key Documents

SAB4200353

Sigma-Aldrich

Anti-acetyl-Histone H4 [Ac-Lys12] antibody produced in rabbit

IgG fraction of antiserum

Synonym(s):

Anti-H4, Anti-H4K12ac, Anti-HIST4H4, Anti-Histone cluster 4

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~12 kDa

species reactivity

mouse, rat, human

technique(s)

immunohistochemistry: 1:100-1:200 using formalin-fixed paraffin-embedded human breast carcinoma
indirect immunofluorescence: 1:250-1:500 using HeLa cells
western blot: 1:500-1:1000 using NIH3T3 cell lysates

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

acetylation (Lys12)

Gene Information

human ... HIST3H3(8290)

General description

Histones H3 and H4 are the predominant histones subjected to extensive covalent modifications. It is an important component of chromatin structure.

Immunogen

synthetic peptide containing acetylated Lys12 of human histone H4, conjugated to KLH. The corresponding sequence is identical in many species including rat and mouse histone H4.

Application

Anti-acetyl-Histone H4 [Ac-Lys12] antibody produced in rabbit has been used in:
  • immunoblotting
  • immunofluorescence
  • immunohistochemistry

Biochem/physiol Actions

Histone H4 can be reversibly acetylated at lysine residues K5, K8, K12 and K16, and the acetylation occurs initially at K16 and then propagates in an N-terminal direction through K12, K8 and K5. Altered acetylation of histone H4 on Lys12 (H4- K12Ac) is linked to age-dependent memory impairment in mice. Histones are subjected to several covalent modifications, such as phosphorylation, methylation, acetylation and ubiquitination, that affect chromatin structure and regulate chromatin activity. Histone modifications plays an important role in cancer and disease.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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.

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Storage Class Code

10 - Combustible liquids

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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Altered histone acetylation is associated with age-dependent memory impairment in mice
Peleg S, et al.
Science, 328(5979), 753-756 (2010)
Robert Schneider et al.
Trends in biochemical sciences, 27(8), 396-402 (2002-08-02)
Enzymes that covalently modify histones control many cellular processes by affecting gene expression. A new class of these enzymes is the histone lysine methyltransferase family, whose catalytic activity lies within a conserved domain, the SET domain. This article surveys the
The language of covalent histone modifications
Strahl BD and Allis CD
Nature, 403(6765), 41-41 (2000)

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