Anti-TMEM16B ANO2 Antibody

Calcium-activated chloride channels (CaCC) are present in many cell types and mediate physiological functions such as epithelial secretion, sensory signal transduction, and smooth muscle contraction. Subunits of these CaCC's include the transmembrane proteins TMEM16A and TMEM16B. TMEM16B is predicted to have eight transmembrane domains with both the amino and carboxy termini in the cytoplasm and is expressed in several tissues including olfactory sensory neurons as well as photoreceptors in mammalian retina. Like TMEM16A, TMEM16B is thought to form at least part of CaCC's but has different biophysical characteristics such as voltage dependence and unitary conductance.

TMEM16B antibody was raised against a 19 amino acid synthetic peptide from near the amino terminus of human TMEM16B. The immunogen is located within the first 50 amino acids of TMEM16B.

Calcium-activated chloride channel (CaCC) which may play a role in olfactory signal transduction. Odorant molecules bind to odor-sensing receptors (OSRs), leading to an increase in calcium entry that activates CaCC current which amplifies the depolarization of the OSR cells, ANO2 seems to be the underlying chloride channel involved in this process. May mediate light perception amplification in retina.