ALEXA FLUOR 488 Rabbit anti-Human, Mouse AQP7 Polyclonal Antibody, ALEXA FLUOR 488 Conjugated [IgG]

AQP9; AQP7L; AQPap; GLYCQTL; Aquaporin-7; AQP-7; Aquaglyceroporin-7; Aquaporin adipose; Aquaporin-7-like; AQP7

Water is a critical component of all living cells. Interestingly, tissue membranes show a great degree of water permeability. Mammalian red cells, renal proximal tubules, and descending thin limb of Henle are extraordinarily permeable to water. Water crosses hydrophobic plasma membranes either by simple diffusion or through a facilitative transport mechanism mediated by special protein "aquaporin". Over the last decade, genes for several members of aquaporin family have been cloned, expressed, and their distribution studied in many tissues. AQP0 or MIP26 (major intrinsic protein 26kD), and Aquaporin 1 (AQP1, purified from red cells) also called CHIP28 (channel forming integral protein, 28kD; 268aa; gene locus 7p14) has been the foundation of the growing family of aquaporin. The lens specific AQP0 represents up to 80% of total lens membrane protein. Defects in MIP26 are cause of autosomal dominant cataract. The cataract Fraser mutation (CATFR or Shriveled) is a transposon induced splicing error that substitutes a long terminal repeat sequence for the C terminus of MIP. The lens opacity mutation (LOP) is an amino acid substitution that inhibits targeting of MIP to the cell membrane.