Acetylated Lysine (acetylated) antibody

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Antigen
Epitope
acetylated
36
15
Reactivity
Chemical
161
2
2
1
1
Host
Mouse
90
72
Clonality (Clone)
Monoclonal ()
Conjugate
Un-conjugated
12
12
7
7
5
4
4
3
3
3
3
3
3
3
3
3
2
2
2
2
2
2
2
2
2
2
2
1
1
1
1
Application
Enzyme Immunoassay (EIA), Immunohistochemistry (Frozen Sections) (IHC (fro)), Western Blotting (WB)
150
112
111
88
81
69
17
9
7
3
2
2
1
1
1
1
Options
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Clone 7F8
Isotype IgG1
Purification Affinity Chromatography on Protein G
Target Type Amino Acid
Background 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 N?-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). The regulation of protein acetylation status is impaired in the pathologies of cancer and polyglutamine diseases (4), and HDACs have become promising targets for anticancer drugs currently in development (5).Synonyms: AcK, acetyl Lysine, acetyl-Lysine
Research Area Metabolism
Application Notes Optimal working dilution should be determined by the investigator.
Restrictions For Research Use only
Concentration 1.0 mg/mL
Buffer PBS, pH 7.4 containing 0.09 % Sodium Azide in 50 % Glycerol
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Background publications Yang: "Multisite protein modification and intramolecular signaling." in: Oncogene, Vol. 24, Issue 10, pp. 1653-62, 2005 (PubMed).

Yang: "Lysine acetylation and the bromodomain: a new partnership for signaling." in: BioEssays : news and reviews in molecular, cellular and developmental biology, Vol. 26, Issue 10, pp. 1076-87, 2004 (PubMed).

Vigushin, Coombes: "Targeted histone deacetylase inhibition for cancer therapy." in: Current cancer drug targets, Vol. 4, Issue 2, pp. 205-18, 2004 (PubMed).

Hassig, Schreiber: "Nuclear histone acetylases and deacetylases and transcriptional regulation: HATs off to HDACs." in: Current opinion in chemical biology, Vol. 1, Issue 3, pp. 300-8, 1998 (PubMed).