Gap junctions are composed of transmembrane channels that link the cytoplasm of neighboring cells. They differ from other membrane channels since they exist between two cells. Gap junctions are relatively non-specific and allow passive diffusion of small molecules up to 1000 Dalton. The junctions exist in almost all vertebrate and non-vertebrates cells. It is believed that gap junction play an important for intercellular communications and affect growth and differentiation of cells. Absence of intercellular communication mediated by gap junction may lead to transformed or cancerous growth. Gap junctional channel is composed of a hemichannel (connexon) in the cell membrane of one cell joined in mirror symmetry with a connexon in the opposing cell. Each connexon is an oligomer of six protein subunits that define the axial aqueous pore. Molecular cloning studies have identified a family of at least 12 highly related Connexins that are designated according to mol. wt, Cx26-50. Hydropathy analyses of Cx sequences predicts 4 transmembrane domains, 2 extracellular (EC), and 3 cytoplasmic (CP) domains. The EC, TM, and N-terminal CP domains are well conserved among family members, while Central and C-terminal domains are highly variable in both sequence and size. The N and C-termini are predicted to be cytoplasmic.

ADI has produced highly specific rabbit antibodies for various Cx using specific peptide sequences. These antibodies do not crossreact with each other and can be used to study specific Cx in mouse, rat, and human tissues. Availability of multiple antibodies to the same protein should help select antibodies with more interspecies crossreactivity, and to achieve better results in a given technique. The control peptides, used for immunization, are also available to determine specificity of antibodies.