GSTZ1抗体

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     Gel: 12%SDS-PAGE, Lysate: 40 μg, Lane 1-2: Mouse liver tissue and HepG2 cell lysates, Primary antibody: P09867(GSTZ1 Antibody) at dilution 1/1200, Secondary antibody: Goat anti rabbit IgG at 1/5000 dilution, Exposure time: 1 minute    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human thyroid cancer tissue using P09867(GSTZ1 Antibody) at dilution 1/100. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human cervical cancer tissue using P09867(GSTZ1 Antibody) at dilution 1/100. (Original magnification: ×200)    

  
  

The glutathione S-transferase zeta 1 (GSTZ1) antibody is a tool used to detect and study the GSTZ1 protein, a member of the glutathione S-transferase (GST) superfamily. GSTZ1. also known as maleylacetoacetate isomerase (MAAI), plays a critical role in tyrosine catabolism and detoxification processes. It catalyzes the isomerization of maleylacetoacetate to fumarylacetoacetate in the phenylalanine/tyrosine degradation pathway and participates in the metabolism of halogenated compounds, such as dichloroacetic acid (DCA). Dysregulation of GSTZ1 is linked to metabolic disorders, including hereditary tyrosinemia type III, and its expression may influence drug metabolism and toxicity.

GSTZ1 antibodies are widely used in research to analyze protein expression, localization, and function via techniques like Western blotting, immunohistochemistry (IHC), and immunofluorescence (IF). They help investigate GSTZ1's role in liver function, cancer biology (e.g., altered expression in certain tumors), and interactions with environmental toxins or therapeutics. Species-specific GSTZ1 antibodies (human, mouse, rat) are available, with monoclonal antibodies offering high specificity and polyclonal antibodies providing broader epitope recognition.

Quality validation of GSTZ1 antibodies often includes knockout cell line controls to confirm specificity. Studies also explore GSTZ1's unique structural features, such as its homodimeric configuration and lack of a canonical glutathione-binding site, distinguishing it from other GST classes. Understanding GSTZ1's biological and pathological significance remains a key focus in metabolic and pharmacological research.