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     The image is immunohistochemistry of paraffin-embedded Human esophagus cancer tissue using P06351(DBP Antibody) at dilution 1/25. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human gastric cancer tissue using P06351(DBP Antibody) at dilution 1/25. (Original magnification: ×200)    

  
  

The vitamin D-binding protein (DBP), also known as gc-globulin, is a multifunctional plasma glycoprotein primarily synthesized in the liver. It serves as the main carrier of vitamin D metabolites, facilitating their transport in the bloodstream and delivery to target tissues. Structurally, DBP belongs to the albumin gene family and exhibits a high affinity for 25-hydroxyvitamin D and 1.25-dihydroxyvitamin D. Beyond vitamin D transport, DBP plays roles in immune modulation, actin scavenging, and fatty acid uptake.

Anti-DBP antibodies, often detected in autoimmune and liver diseases, are associated with conditions like autoimmune hepatitis, primary biliary cholangitis, and systemic lupus erythematosus. These autoantibodies may arise due to molecular mimicry, genetic predisposition, or exposure to modified DBP antigens during tissue injury. Their presence can interfere with DBP's functions, potentially altering vitamin D metabolism or exacerbating inflammatory responses. Research also explores their diagnostic and prognostic utility, though clinical significance remains under investigation. Current studies focus on understanding antibody heterogeneity, epitope specificity, and their mechanistic role in disease pathogenesis. DBP antibodies represent a growing area of interest in autoimmunity and metabolic disorder research.