A 16aa synthetic peptide within the C-terminal domain of rat AQP8. 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 CHIP-28 (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 (CAT-FR 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. A new water channel, AQP8, has been identified in rat pancreas and testis by homology cloning (1). AQP8 (263 aa, 28kD) is also found in liver, colon and salivary glands. AQP8 is expressed in all stages of spermatogenesis. Unlike other AQP, AQP8 has unusually long N-terminus and a short C-terminus. AQP families of proteins are predicted to contain six transmembrane domains. The N and C-terminus are predicted to be cytoplasmic. AQP8 has significant homology to various AQPs: g-TIP (plant water channel, 37%), AQP2 and MIP (37%), AQP1, AQP4, and AQP5 (30-34%), AQP3 (26%). AQP8 does not facilitate glycerol transport.
Reinheit:
Highly purified
Formulierung:
Supplied as a liquid in PBS, pH 7.2, 0.09% sodium azide
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