Acetylated lysine (25 ĩl, clone 7F8)

AS10 707-25  | Clonality: monoclonal  |  Host: Mouse  |  Reactivity: acetylated lysine

Acetylated lysine (25 ĩl, clone 7F8) in the group Antibodies Plant/Algal  / DNA/RNA/Cell Cycle / Epigenetics/DNA methylation at Agrisera AB (Antibodies for research) (AS10 707-25)
Acetylated lysine (25 ĩl, clone 7F8)


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Product Information


acetylated KLH

Host Mouse
Clonality Monoclonal
Subclass/isotype IgG1
Purity Total IgG fraction. Protein G purified.
Format Liquid
Quantity 25 ĩl
Storage Store lyophilized/reconstituted at -20°C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please remember to spin the tubes briefly prior to opening them to avoid any losses that might occur from material adhering to the cap or sides of the tube.
Tested applications ELISA (ELISA), Immunocytochmistry/Immunofluorescence (ICC/IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western blot (WB)
Recommended dilution 1 : 100 (IHC), 1 : 1000 (WB)


Confirmed reactivity Bovine, avian
Predicted reactivity Higher plants
Not reactive in No confirmed exceptions from predicted reactivity are currently known

Application examples

Additional information

Additional information Protein G purified IgG2B in PBS, pH 7,4 with 0,09 % sodium azide and 50 % glycerol at concentration 1 mg/mlantibody detects Proteins containing acetylated lysine residues in ELISA and WBs, Does not detect non-acetylated lysine residues

1 µg of this antibody is sufficient to detect acetylated chicken erythrocyte histones (sodium butyrate-treated) using 20 µg total protein and ECL detection system

Related products



Post-translational modifications of proteins play critical roles in the regulation and function of many known biological processes. Proteins can be post-translationally modified in many different ways, and a common posttranscriptional modification of Lysine involves acetylation (1). The conserved amino-terminal domains of the four core histones (H2A, H2B, H3 and H4) contain lysines that are acetylated by histone acetyltransferases (HATs) and deacetylated by histone deacetylases (HDACs) (2). Protein posttranslational reversible lysine Nε-acetylation and deacetylation have been recognized as an emerging intracellular signaling mechanism that plays critical roles in regulating gene transcription, cell-cycle progression, apoptosis, DNA repair, and cytoskeletal organization (3).  

Product citations

Selected references Vigushin & Coombes (2004). Targeted histone deacetylase inhibition for cancer therapy. Curr. Cancer Drug Targets 4: 205-218.

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