Anti-Acetylated Lysine, rabbit polyclonal antibody that recognizes acetylated lysine in UV-treated HEK293 cells. It is validated for ELISA, Western blotting, immunoprecipitation, & paraffin sections.
Yu, X., et al. 2002. J. Natl. Cancer Inst.94, 504. Mal, A., et al. 2001. EMBO J.20, 1739. Sano, Y. and Ishii, S. 2001. J. Biol. Chem.276, 3674.
Informações legais
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Não está encontrando o produto certo?
Experimente o nosso Ferramenta de seleção de produtos.
Código de classe de armazenamento
10 - Combustible liquids
Classe de risco de água (WGK)
WGK 2
Certificados de análise (COA)
Busque Certificados de análise (COA) digitando o Número do Lote do produto. Os números de lote e remessa podem ser encontrados no rótulo de um produto após a palavra “Lot” ou “Batch”.
Já possui este produto?
Encontre a documentação dos produtos que você adquiriu recentemente na biblioteca de documentos.
The Journal of biological chemistry, 287(42), 34917-34926 (2012-08-25)
The MYST family of histone acetyltransferases (HATs) plays critical roles in diverse cellular processes, such as the epigenetic regulation of gene expression. Lysine autoacetylation of the MYST HATs has recently received considerable attention. Nonetheless, the mechanism and function of the
Ribosome biogenesis requires an enormous commitment of energy and resources in growing cells. In budding yeast, the transcriptional coactivator Ifh1p is an essential regulator of ribosomal protein (RP) gene transcription. Here, we report that Ifh1p is dynamically acetylated and phosphorylated
The 60-kDa HIV-Tat interactive protein (Tip60) is a key member of the MYST family of histone acetyltransferases (HATs) that plays critical roles in multiple cellular processes. We report here that Tip60 undergoes autoacetylation at several lysine residues, including a key
The conserved family of cohesin proteins that mediate sister chromatid cohesion requires Scc2, Scc4 for chromatin-association and Eco1/Ctf7 for conversion to a tethering competent state. A popular model, based on the notion that cohesins form huge ring-like structures, is that
The positive link between the SWI/SNF and the Gcn5 histone acetyltransferase in transcriptional activation has been well described. Here we report an inhibitory role for Gcn5 in SWI/SNF targeting. We demonstrate that Gcn5-containing complexes directly acetylate the Snf2 subunit of
Nossa equipe de cientistas tem experiência em todas as áreas de pesquisa, incluindo Life Sciences, ciência de materiais, síntese química, cromatografia, química analítica e muitas outras.