Anti-SERPINA12 antibodies are used in the immunodetection of the protein serpin family A member 12. In humans, the canonical protein has a reported length of 414 amino acid residues and a mass of 47.2 kDa. It has been described to be a secreted protein. It is reported to be expressed in visceral adipose tissues. A member of the Serpin protein family, SERPINA12 is a reported adipokine that modulates insulin action by specifically inhibiting its target protease KLK7 in white adipose tissues. Post-translational modifications have been described, including glycosylation. Synonyms for this target antigen include serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 12, vaspin, and serine (or cysteine) proteinase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 12. SERPINA12 gene orthologs have been reported in the mouse, rat and chimpanzee species. A number of SERPINA12 antibodies have been mentioned in research publications and have associated citations. Western Blot is a widely used application for these antibodies. ELISA and Immunohistochemistry are also common applications.