Phospho-NDRG1 (Ser330)抗体;Phospho-NDRG1 (Ser330) Antibody—艾普蒂 新品

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     Western blot analysis of Phospho-NDRG1 (Ser330) in mouse kidney lysates using Phospho-NDRG1 (Ser330) antibody.    

  
  

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     Western blot analysis of Phospho-NDRG1(Ser330) in Hela, A549, MCF-7, 239T, C2C12 lysates using Phospho-NDRG1(Ser330) antibody    

  
  

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     Immunocytochemistry analysis of Phospho-NDRG1 (Ser330) (green) in 293T using Phospho-NDRG1 (Ser330) antibody,and DAPI(blue).    

  
  

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     Immunohistochemistry analysis of paraffin-embedded Human Cholangiocarcinoma using NDRG1 (Phospho-Ser330) antibody.High-pressure and temperature Sodium Citrate pH 6.0 was used for antigen retrieval.    

  
  

The Phospho-NDRG1 (Ser330) antibody detects N-myc downstream-regulated gene 1 (NDRG1) when phosphorylated at serine 330. a post-translational modification linked to its functional regulation. NDRG1 is a stress-responsive protein involved in cell differentiation, growth arrest, and tumor suppression. Its activity is modulated by phosphorylation through various kinases, including serum/glucocorticoid-regulated kinase 1 (SGK1) and protein kinase C (PKC). Phosphorylation at Ser330 is associated with cellular responses to hypoxia, DNA damage, or hormonal signaling, such as androgen receptor pathways in prostate cancer. This modification may influence NDRG1’s role in inhibiting metastasis, regulating metal ion homeostasis, or mediating stress adaptation.

The antibody is widely used in cancer research, particularly in studies exploring NDRG1’s tumor-suppressive functions in prostate, breast, and colorectal cancers. It helps assess phosphorylation status via techniques like Western blotting, immunofluorescence, or immunohistochemistry, providing insights into pathway activation or disease progression. Dysregulated NDRG1 phosphorylation has been implicated in chemoresistance, poor prognosis, and metastatic behavior, making this antibody a tool for studying biomarkers or therapeutic targets. Specificity for the phosphorylated Ser330 epitope ensures accurate detection of active NDRG1 conformations, aiding mechanistic studies in both physiological and pathological contexts.