Alomone Labs is pleased to offer the Connexin & Pannexin Antibody Explorer Kit (#AK-425). This Explorer Kit includes connexin and pannexin antibodies with their respective peptide control antigen. An ideal tool for screening purposes.
|Product Name||Cat #||Size|
|ACC-212||1 x 50 µl|
|ACC-223||1 x 50 µl|
|ACC-213||1 x 50 µl|
|ACC-211||1 x 50 µl|
|ACC-209||1 x 50 µl|
|ACC-204||1 x 50 µl|
|ACC-205||1 x 50 µl|
|ACC-201||1 x 50 µl|
|ACC-207||1 x 50 µl|
|ACC-234||1 x 50 µl|
|ACC-232||1 x 50 µl|
|ACC-233||1 x 50 µl|
Gap junctions are usually found in clusters and enable intercellular communication by allowing the passage of small molecules between cells1. They play important roles in different biological processes. These include differentiation, cell cycle synchronization, cellular development, neuronal activity and the immune response2-4.
Proteins involved in gap junction formation are composed of four transmembrane domains, 2 extracellular loops and one intracellular loop and intracellular N- and C-termini5,6. Several consensus cysteine residues are in the extracellular loop and are essential and necessary for intercellular docking of gap junction hemichannels in the opposing cell membrane5-7.
Pannexins (Pannexin 1, Pannexin 2 and Pannexin 3) belong to the superfamily of gap junction proteins. Pannexin 1 (PANX1) is ubiquitously expressed, Pannexin 2 (PANX2) is specifically expressed in the human brain and widespread in rodents and Pannexin 3 (PANX3) is also detected in the brain8.
Connexins are transmembrane proteins, which oligomerize into hexameres adjusting in hemi-channels (connexons). The docking of connexons between two neighboring cells results in the formation of intercellular channels, which are permeable to ions and small molecules9. These channels, which are also known as gap junctions, are characterized by distinct electrophysiological properties. Various physiological and pathological conditions regulate the opening and closing of the channels10. Several genetic disorders have been identified in which specific connexin genes are mutated11.
- Chew, S.S. et al. (2010) Exp. Neurol. 225, 250.
- Nakagawa, S. et al. (2010) Curr. Opin. Struct. Biol. 20, 423.
- Trexler, E.B. et al. (1996) Proc. Natl. Acad. Sci. U.S.A. 93, 5836.
- Hu, X. et al. (2006) Biophys. J. 90, 140.
- Shestopalov, V.I. et al. (2008) Cell. Mol. Life Sci. 65, 376.
- Unger, V.M. et al. (1999) Science 283, 1176.
- Falk, M.M. (2000) Eur. J. Cell. Biol. 79, 564.
- Panchin, Y.V. (2005) J. Exp. Biol. 208, 1415.
- Beyer, E.C. et al. 1993. Int. Rev. Cytol. 137C, 1.
- Evans, W.H. et al. 2002. Mol. Membr. Biol. 19, 121.
- Kelsell, D.P. et al. 2001. Trends Cell Biol. 11, 2.