epitope mapping within an N-terminal extracellular domain of claudin-12 of human origin
recommended for detection of claudin-12 of mouse, rat and human origin by WB, IF and ELISA; also reactive with additional species, including equine, canine, bovine and porcine
claudin-12 Background Information The claudin superfamily consists of many structurally related proteins that are important structural and functional components of tight junctions. Claudin-12, also known as CLDN12, is a 244 amino acid multi-pass membrane protein that is expressed in the brain, duodenum, jejunum, ileum, and colon. Claudin-12 localizes to cell junctions and may be involved in tight junction integrity by regulating hyperammonemia. Ammonia can alter brain capillary endothelial cell gene expression and transporter function. Claudin-12 is upregulated in enterocytes through vitamin D receptors which strongly suggest that claudin-12 forms paracellular Ca(2+) channels in intestinal epithelia and may be critical for vitamin D-dependent calcium homeostasis.
