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Acetylated Lysine (acLys) antibody

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Amino Acid
(25), (2), (2), (2), (1), (1), (1)
(24), (5)
(2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
ELISA, Immunofluorescence (IF), Immunoprecipitation (IP), Western Blotting (WB)
(28), (27), (25), (24), (20), (7), (1), (1)
Pubmed 7 references available
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Quantity 400 μL
Shipping to United States ( )
Immunogen Acetylated KLH Conjugated
Isotype IgG
Specificity Detects proteins containing acetylated lysine residues in SDS PAGE immunoblots.
Target Type Amino Acid
Background Synonyms:
lysine, acetyl lysine
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 post-transcriptional modification of Lysine involves acetylation.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). 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. The regulation of protein acetylation status is impaired in the pathologies of cancer and polyglutamine diseases, and HDACs have become promising targets for anti-cancer drugs currently in development.
Research Area Cell Signaling
Application Notes Recommended Dilution: 1:250 (WB)
Restrictions For Research Use only
Format Liquid
Concentration 250 µg/ mL
Buffer PBS, 50 % glycerol, 0.09 % sodium azide
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Supplier Images
Image no. 1 for anti-Acetylated Lysine (acLys) antibody (ABIN361842) Acetylated Lysine, acetylated histone from TSA treated mouse spleen cell.
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).

Chan, Krstic-Demonacos, Smith et al.: "Acetylation control of the retinoblastoma tumour-suppressor protein." in: Nature cell biology, Vol. 3, Issue 7, pp. 667-74, 2001 (PubMed).

Martínez-Balbás, Bauer, Nielsen et al.: "Regulation of E2F1 activity by acetylation." in: The EMBO journal, Vol. 19, Issue 4, pp. 662-71, 2000 (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).

General Hughes: "Polyglutamine disease: acetyltransferases awry." in: Current biology : CB, Vol. 12, Issue 4, pp. R141-3, 2002 (PubMed).

Catalog No. ABIN361842

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