A 20aa synthetic peptide within the N-terminal domain of human AQPAP.
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.
Most recently, adipose specific AQP-adipose (342 aa; AQPAP or AQP7-like) has been cloned. It facilities water and glycerol transport. AQP families of proteins are predicted to contain six transmembrane domains. The N and C-terminus are predicted to be cytoplasmic.
仕様
Size：100ug
Source Antigen：Human synthetic peptide
Grade：Highly Purified
Purity：Highly purified
Form：Supplied as a liquid in PBS, pH 7.2, 0.09% sodium azide
Specificity：Unique to AQPAP without significant homology to any other AQPs. AQPAP from other species are yet to be cloned. Control peptides, because of their low MW (<3kD), are not suitable for Western. It should be used for ELISA or antibody blocking to confirm antibody specificity
