OGA抗体 新品

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     Black line: Control Antigen (100 ng); Purple line: Antigen(10ng); Blue line: Antigen (50 ng); Red line: Antigen (100 ng);    

  
  

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     Immunofluorescence analysis of HepG2 cells using CSF1R mouse mAb (green). Blue: DRAQ5 fluorescent DNA dye. Secondary antibody from Fisher (Cat#: 35503)    

  
  

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     Immunohistochemical analysis of paraffin-embedded human pancreas tissues using CSF1R mouse mAb with DAB staining.    

  
  

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     Immunohistochemical analysis of paraffin-embedded human esophageal tissues using CSF1R mouse mAb with DAB staining.    

  
  

O-GlcNAcase (OGA) is a glycoside hydrolase responsible for the removal of O-linked β-N-acetylglucosamine (O-GlcNAc) post-translational modifications from proteins. This dynamic modification, regulated by OGA and its opposing enzyme O-GlcNAc transferase (OGT), plays critical roles in cellular processes such as nutrient sensing, transcriptional regulation, and stress response. Dysregulation of O-GlcNAc cycling has been implicated in metabolic disorders, neurodegenerative diseases (e.g., Alzheimer’s), and cancer, driving interest in OGA as a therapeutic target.

OGA-specific antibodies are essential tools for studying its expression, localization, and activity. They enable detection via techniques like Western blotting, immunohistochemistry, and immunofluorescence, aiding in the exploration of OGA's tissue distribution and disease-associated alterations. Additionally, these antibodies support research on OGA inhibitors, which are being investigated for modulating O-GlcNAc levels in pathological conditions. Recent studies also highlight OGA's involvement in epigenetic regulation and immune function, expanding its biomedical relevance. However, antibody specificity remains a challenge due to structural similarities among glycosidases, necessitating rigorous validation. Continued development of high-affinity, isoform-selective OGA antibodies is crucial for advancing both basic research and clinical applications targeting O-GlcNAc signaling.