Phospho-HDAC5 (Ser498)抗体;Phospho-HDAC5 (Ser498) Antibody—艾普蒂 新品

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     Western blot analysis of Phospho-HDAC5 (Ser498) in 293 lysates using Phospho-HDAC5 (Ser498) antibody.    

  
  

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     Immunohistochemistry analysis of paraffin-embedded Human breast carcinoma tissue using HDAC5(Phospho-Ser498) antibody.High-pressure and temperature Sodium Citrate pH 6.0 was used for antigen retrieval. Sample with blocking peptide on the right.    

  
  

Phospho-HDAC5 (Ser498) antibodies are essential tools for studying the regulation and function of histone deacetylase 5 (HDAC5), a class IIa HDAC involved in epigenetic modulation. HDAC5 primarily deacetylates histones, promoting chromatin condensation and transcriptional repression. Its activity is tightly regulated by post-translational modifications, particularly phosphorylation. The Ser498 residue, located in the nuclear regulatory domain, is a critical phosphorylation site targeted by kinases such as calcium/calmodulin-dependent kinase II (CaMKII) and protein kinase D (PKD). Phosphorylation at Ser498 triggers HDAC5 nuclear export via 14-3-3 protein binding, relieving its repressive effects on transcription factors like MEF2. which govern cellular processes such as cardiac hypertrophy, neuronal plasticity, and muscle differentiation.

These antibodies specifically recognize HDAC5 phosphorylated at Ser498. enabling researchers to assess its activation status in response to signaling pathways. They are widely used in techniques like Western blotting, immunofluorescence, and immunohistochemistry to investigate HDAC5 dynamics in diseases such as heart failure, cancer, and neurodegenerative disorders. Validated Phospho-HDAC5 (Ser498) antibodies are critical for elucidating how kinase-HDAC5 interactions influence gene expression and cellular adaptation to stress. Proper controls, including phosphorylation-deficient mutants or kinase inhibitors, are recommended to confirm specificity in experimental models.