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Methylated Lysine (meLys) antibody

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(15), (2), (1)
All Species
(19), (18), (1), (1), (1)
(37), (1)
(2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (1), (1)
Immunocytochemistry (ICC), Immunofluorescence (IF), Immunoprecipitation (IP), ELISA, Western Blotting (WB)
(38), (37), (35), (19), (17), (17), (16)
Pubmed 7 references available
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Quantity 400 μL
Shipping to United States ( )
Availability Will be delivered in 3 to 4 Business Days
Immunogen Methylated KLH Conjugated
Specificity Detects proteins containing methylated lysine residues.
Purification Protein A Purified
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 post-transcriptional 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). The regulation of protein acetylation status is impaired in the pathologies of cancer and polyglutamine diseases (4), and HDACs have become promising targets for anti-cancer drugs currently in development (5).
Research Area Metabolism
Application Notes Recommended Dilution: WB (1:5000), ICC/IF (1:50), optimal dilutions for assays should be determined by the user.
Restrictions For Research Use only
Format Liquid
Concentration 250 μg/mL
Buffer PBS, 50 % glycerol
Storage -20 °C
Product cited in: Dawson, Bell, Storey: "Purification and Properties of White Muscle Lactate Dehydrogenase from the Anoxia-Tolerant Turtle, the Red-Eared Slider, Trachemys scripta elegans." in: Enzyme research, Vol. 2013, pp. 784973, 2013 (PubMed).

Background publications Yang: "Multisite protein modification and intramolecular signaling." in: Oncogene, Vol. 24, Issue 10, pp. 1653-62, 2005 (PubMed).

Im, Park, Feng et al.: "Dynamic regulation of histone H3 methylated at lysine 79 within a tissue-specific chromatin domain." in: The Journal of biological chemistry, Vol. 278, Issue 20, pp. 18346-52, 2003 (PubMed).

Ng, Xu, Zhang et al.: "Ubiquitination of histone H2B by Rad6 is required for efficient Dot1-mediated methylation of histone H3 lysine 79." in: The Journal of biological chemistry, Vol. 277, Issue 38, pp. 34655-7, 2002 (PubMed).

Zegerman, Canas, Pappin et al.: "Histone H3 lysine 4 methylation disrupts binding of nucleosome remodeling and deacetylase (NuRD) repressor complex." in: The Journal of biological chemistry, Vol. 277, Issue 14, pp. 11621-4, 2002 (PubMed).

Bannister, Zegerman, Partridge et al.: "Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain." in: Nature, Vol. 410, Issue 6824, pp. 120-4, 2001 (PubMed).

Melcher, Schmid, Aagaard et al.: "Structure-function analysis of SUV39H1 reveals a dominant role in heterochromatin organization, chromosome segregation, and mitotic progression." in: Molecular and cellular biology, Vol. 20, Issue 10, pp. 3728-41, 2000 (PubMed).

Catalog No. ABIN361690
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