Anti-Aquaporin 3/AQP3 Antibody Picoband® Fluoro647 Conjugated

This gene encodes the water channel protein aquaporin 3. Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein, also known as aquaporin 0. Aquaporin 3 is localized at the basal lateral membranes of collecting duct cells in the kidney. In addition to its water channel function, aquaporin 3 has been found to facilitate the transport of nonionic small solutes such as urea and glycerol, but to a smaller degree. It has been suggested that water channels can be functionally heterogeneous and possess water and solute permeation mechanisms. Alternative splicing of this gene results in multiple transcript variants encoding different isoforms.

A synthetic peptide corresponding to a sequence at the C-terminus of human Aquaporin 3, different from the related rat and mouse sequences by one amino acid.

Widely expressed in epithelial cells of kidney (collecting ducts) and airways, in keratinocytes, immature dendritic cells and erythrocytes. Isoform 2 is not detectable in erythrocytes at the protein level.

Water channel required to promote glycerol permeability and water transport across cell membranes. Acts as a glycerol transporter in skin and plays an important role in regulating SC (stratum corneum) and epidermal glycerol content. Involved in skin hydration, wound healing, and tumorigenesis. Provides kidney medullary collecting duct with high permeability to water, thereby permitting water to move in the ion of an osmotic gradient. Slightly permeable to urea and may function as a water and urea exit mechanism in antidiuresis in collecting duct cells. It may play an important role in gastrointestinal tract water transport and in glycerol metabolism (By similarity) . .

1. Dibas AI, Mia AJ, Yorio T (1998) . Aquaporins (water channels) : role in vasopressin-activated water transport. Proc. Soc. Exp. Biol. Med. 219 (3) : 183–99. 2. Roudier N, Ripoche P, Gane P, Le Pennec PY, Daniels G, Cartron JP, Bailly P (2002) . AQP3 deficiency in humans and the molecular basis of a novel blood group system, GIL. J. Biol. Chem. 277 (48) : 45854–9. 3. Sasaki S, Ishibashi K, Marumo F (1998) . Aquaporin-2 and -3: representatives of two subgroups of the aquaporin family colocalized in the kidney collecting duct. Annu. Rev. Physiol. 60: 199–220.