|Predicted||Bovine, Chicken, Human, Mouse, Pig, Zebrafish|
|Calculated MW||43 KDa|
|Other Names||Gap junction alpha-1 protein, Connexin-43, Cx43, Gap junction 43 kDa heart protein, Gja1, Cxn-43|
|Target/Specificity||Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser368 conjugated to KLH.|
|Format||Prepared from rabbit serum by affinity purification via sequential chromatography on phospho- and dephosphopeptide affinity columns.|
|Antibody Specificity||Specific for the ~43k connexin43 protein phosphorylated at Ser368.Immunolabeling is blocked by λ-phosphatase treatment.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Phospho-Ser368 Connexin43 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
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Provided below are standard protocols that you may find useful for product applications.
Gap junctional intercellular communication is thought to play a key role in development and may also be involved in epilepsy (Aronica et al., 2001). Connexin43 forms gap-junctional channels and regulates the permeability of these gap junctions to small organic molecules. Permeability of connexin43 is known to be regulated by phosphorylation at Ser368 by protein kinase C (Yogo et al., 2002; Bao et al., 2004a). Phosphorylation of Ser368 by PKC induces a conformational change of connexin43 that results in a decrease in gap junction permeability (Bao et al., 2004b).
Aronica E, Gorter JA, Jansen GH, Leenstra S, Yankaya B, Troost D (2001) Expression of connexin 43 and connexin
32 gap-junction proteins in epilepsy-associated brain tumors and in the perilesional epileptic cortex. Acta
Neuropathol (Berl) 101:449-459.
Bao X, Altenberg GA, Reuss L (2004a) Mechanism of regulation of the gap junction protein connexin 43 by protein
kinase C-mediated phosphorylation. Am J Physiol Cell Physiol 286:C647-C654.
Bao X, Reuss L, Altenberg GA (2004b) Regulation of purified and reconstituted connexin 43 hemichannels by protein
kinase C-mediated phosphorylation of Serine 368. J Biol Chem 279:20058-20066.
Yogo K, Ogawa T, Akiyama M, Ishida N, Takeya T (2002) Identification and functional analysis of novel
phosphorylation sites in Cx43 in rat primary granulosa cells. FEBS Lett 531:132-136.
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