Anti-GC vitamin D binding protein antibodies are used for the immunodetection of the protein encoded by the GC gene. In humans, the canonical protein has a reported length of 474 amino acid residues and a mass of 52.9 kDa. It is known to be a secreted protein. Alternative splicing is reported to yield 3 different isoforms for this protein. It is reported to be expressed in the liver. A member of the ALB/AFP/VDB protein family, it is known to be involved in vitamin D transport and storage, scavenging of extracellular G-actin, enhancement of the chemotactic activity of C5 alpha for neutrophils in inflammation and macrophage activation. Post-translational modifications have been described, including O-glycosylation and N-glycosylation. Other names for this target antigen include DBP-maf, DBP/GC, GRD3, Gc-MAF, GcMAF, HEL-S-51, VDB, and DBP. Gene orthologs have been identified in the mouse, rat, bovine, frog, zebrafish, chimpanzee and chicken species.