GCSH抗体—艾普蒂

+ +

•  

   

     The image is immunohistochemistry of paraffin-embedded Human liver cancer tissue using P10269(GCSH Antibody) at dilution 1/60. (Original magnification: ×200)    

  
  

•  

   

     The image is immunohistochemistry of paraffin-embedded Human colorectal cancer tissue using P10269(GCSH Antibody) at dilution 1/60. (Original magnification: ×200)    

  
  

The glycine cleavage system H-protein (GCSH) is a mitochondrial enzyme component of the glycine cleavage system (GCS), a multienzyme complex critical for glycine catabolism. GCSH acts as a shuttle, transferring methylamine groups between the GCS's constituent enzymes (P-, T-, and L-proteins) during glycine degradation. This process generates 5.10-methylenetetrahydrofolate, essential for one-carbon metabolism, nucleotide synthesis, and cellular redox regulation. Dysregulation of GCSH is linked to nonketotic hyperglycinemia (NKH), a rare autosomal recessive disorder characterized by glycine accumulation, leading to severe neurological impairments.

GCSH antibodies are immunological tools used to study the expression, localization, and function of GCSH in research contexts. They enable detection via techniques like Western blotting, immunohistochemistry, and immunofluorescence, aiding investigations into mitochondrial metabolism, inborn errors of metabolism, and diseases with perturbed glycine levels. Commercially available GCSH antibodies are typically raised in rabbits or mice against recombinant protein epitopes, validated for specificity across human and model organisms. Recent studies also explore GCSH's potential roles beyond metabolism, including cancer progression, where altered glycine metabolism may influence tumor proliferation.

Understanding GCSH biology via antibody-based approaches contributes to elucidating metabolic pathways, developing diagnostic biomarkers for NKH, and identifying therapeutic targets for glycine-related disorders.