Acetyl-Lysine抗体;Acetyl-Lysine Antibody—艾普蒂 新品

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     Western blot analysis of Acetyl-Lysine in HeLa lysates using Pan Acetyl-Lysine antibody.    

  
  

Acetyl-lysine antibodies are essential tools in studying protein acetylation, a key post-translational modification (PTM) involved in diverse cellular processes. Lysine acetylation, catalyzed by acetyltransferases (HATs) and reversed by deacetylases (HDACs), regulates protein function by neutralizing lysine's positive charge. This modification was first characterized in histones, where it modulates chromatin structure and gene expression by altering histone-DNA interactions. Beyond histones, acetylation impacts non-nuclear proteins, influencing metabolism, signal transduction, and protein stability.

The development of acetyl-lysine antibodies arose from the need to detect and map acetylation sites across proteomes. Early studies relied on radioactive labeling, but antibodies provided higher specificity and compatibility with routine techniques like Western blotting, immunoprecipitation, and immunofluorescence. These antibodies recognize the acetylated ε-amino group of lysine, irrespective of protein context, enabling broad applications. However, target-specific acetyl-antibodies (e.g., anti-acetyl-H3K9) were later developed for precise localization.

Acetyl-lysine antibodies have advanced research in epigenetics, cancer, and neurodegenerative diseases. They help identify acetylation dynamics under physiological or pathological conditions, such as HDAC inhibitor effects or metabolic stress responses. Challenges remain in ensuring epitope specificity, as cross-reactivity with similar PTMs (e.g., crotonylation) can occur. Despite this, these antibodies remain indispensable for dissecting acetylation's regulatory roles in health and disease.