Application
We recommend the use of 0.5-1% milk in all primary/secondary dilutions in order to suppress non-specific bands.
Western blot: 1-10 µg/mL using Chemiluminescence technique
ELISA: 0.5-1.0 µg/mL
Optimal working dilutions must be determined by end user.
Detect Aquaporin 0 using this Anti-Aquaporin 0 Antibody validated for use in ELISA & WB.
Immunogen
A 17 AA synthetic peptide within the carboxy terminal domain of human Aquaporin-0 (Shiels et al. 1988; Kent et al. 1990; Pisano et al. 1991; Shiels et al. 1996) was selected for antibody production. This domain is predicted to be cytoplasmic.
Legal Information
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
Other Notes
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
Specificity
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. Aquaporin-0 or MIP26 (major intrinsic protein 26 kDa), and Aquaporin-1 (purified from red cells) also called CHIP-28 (channel forming integral protein, 28 kDa; 268 AA; gene locus 7p14) has been the foundation of the growing family of aquaporins. The lens specific Aquaporin-0 represents up to 80% of total lens membrane protein. Defects in MIP26 are a 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 AA substitution that inhibits targeting of MIP to the cell membrane. Human Aquaporin-0 is a 263 amino acid transmembrane protein belonging to the MIP family. Aquaporin families of proteins are predicted to contain six transmembrane domains. The N and C-terminus are predicted to be cytoplasmic.
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