Anti-Aquaporin 5

Anti-Aquaporin 5

Product#:

AQP-005

Sizes:

50 ml

0.2 ml

The importance of the Aquaporin water channels was underscored by awarding  the 2003 Nobel Prize in Chemistry to Peter Agre or the discovery of water channels?  Today, eleven mammalian proteins that belong to the Aquaporin family have been identified.  The proteins present a conserved structure of six transmembrane domains with intracellular N and C-termini. 



Aquaporin 5 (AQP5) is expressed in secretory glands, lung and eye, where it works in modulating the rate of fluid release. Since a number of pathological conditions including pulmonary edema, respiratory distress syndrome and congestive heart failure are characterized by disrupted fluid transport, it has been suggested that modulation of the expression of AQP5 could be a novel modality of treatment of the above illnesses. Indeed, several studies have shown that AQP5 expression is downregulated in animal models of acute lung infection.  



We now offering an Anti-AQP5 antibody raised against the last 16 amino acids of the rat protein. The chosen epitope is identical to the mouse AQP5 protein and the  reactivity of the antibody has been confirmed in both species.  

Host:

Rabbit

Epitope:

Peptide (C)DHREERKKTIELTAH corresponding to residues 251-265 of rat AQP5  (SwissProt accession number P47864 ).

Putative epitope location:

Intracellular, C-terminus.

Homology:

Mouse-identical, human - 10/16 residues identical.

Reactivity Confirmed:

Rat, mouse.

Applications:

Western Blotting:

.

Western blotting of mouse salivary gland (1 and 3) and rat lung (2 and 4):  1 and 2. Anti-AQP5 antibody (1:200). 3 and 4. Anti-AQP5 antibody,  preincubated with the control peptide antigen.

Immunohistochemistry:

Rat lungs were stained with Anti-Aquaporin 5 (#AQP-005) antibody (left panel). The strong staining in the alveoli (red brown) is consistent with type 1 pneumocytes (arrows).   Counterstain of cell nuclei appears blue.  A negative control is shown in the right panel.

References:

1. Agre, P. et al. (2002) J. Physiol. 542.1, 3.

2. Towne, J.E. et al. (2000) Am. J. Respir. Cell Mol. Biol. 22, 34.

3. Yang, F. et al. (2002) J. Biol. Chem. 278, 32173.