Anti-serpin family B member 11 antibodies are used for the immunodetection of the protein encoded by the SERPINB11 gene. In humans, the canonical protein has a reported length of 392 amino acid residues and a mass of 44.1 kDa. Its subcellular localization is in the cytoplasm. Alternative splicing is reported to yield 3 different isoforms for this protein. It is notably expressed in a restricted number of tissues, including lung, placenta, prostate, and tonsil. A member of the Serpin protein family, it is known to have no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change. Other names for this target antigen include serpin peptidase inhibitor, clade B (ovalbumin), member 11, and serine (or cysteine) proteinase inhibitor, clade B (ovalbumin), member 11. Gene orthologs have been identified in the mouse, rat, bovine and chimpanzee species.