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.
Suitable for use in ELISA and Western Blot. Other applications not tested.
Western Blot:1:1000-1:5000 (ECL).
ELISA: 1:100,000. Control peptide can be used to coat ELISA plates at 50-100ng/well.
Optimal dilutions to be determined by the researcher.
Recommended Control Peptide:
A3000-55: Aquaporin 9, Rat, Control Peptide (AQP9)
Storage and Stability:
May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
| Not Determined|
|Synthetic peptide corresponding to 18aa within the C-terminal cytoplasmic domain of rat AQP9, conjugated to KLH. Species Sequence Homology: mouse; 94%; human; 72%.|
|Supplied as a liquid in PBS, 0.05% sodium azide.|
|Recognizes rat Aquaporin 9. |
|Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.|
1. Koyama, Yu, et al., JBC 272: 30329 (1997). 2. Ishibashi, K., et al., BBRC 714: 714-718 (1997). 3. Okada, S.: Aquaporin-9 is expressed in a mucus-secreting goblet cell subset in the small intestine, FEBS Letters 540: 157-162 (2003). 4. Barcroft, L.C.: Aquaporin proteins in murine trophectoderm mediate transepithelial water movements during cavitation. Developmental Biology 256: 342-354 (2003). 5. Hubert, C., et al.: Expression and Localization of Aquaporin Water Channels in Rat Hepatocytes. Evidence for a role in canalicular bile secretion. J. Biol. Chem 277: 22710-22717 (2002). 6. Liu, Z., et al,: Arsenite transport by mammalian aquaglyceroporins AQP7 and AQP9. PNAS 99: 6053-6058 (2002). 7. Nicchia, G.P.: Tissue Distribution and Membrane Localization of Aquaporin-9 Water Channel: Evidence for Sex-linked Differences in Liver. J. Histochem. Cytochem. 49: 1547-1556 (2001). 8. Badaut, J.: Distribution of Aquaporin 9 in the adult rat brain: Preferential expression in catecholaminergic neurons and in glial cells. Neuroscience (2004). 9. Liu, Z.: Arsenic trioxide uptake by human and rat aquaglyceroporins, BBRC 316: 1178-1185 (2004). 10. Wang, Am. J. of Ob. Gynecol. 191: 2160 (2002). 11. Kenney, J. Histochem. Cytochem. 52: 1341-1350 (2004).|