This mouse anti-connexin 43 monoclonal antibody is specific to mouse and rat connexin 43. Anti-connexin 43 monoclonal antibody recognizes the expressed product of the Gja1 gene. Connexin 43 is phosphorylated at multiple serine residues in vivo; this observation may have direct bearing on the regulation of gap junctional communication via protein kinase C, protein kinase A, and MAP kinase. Validated applications for this connexin 43 monoclonal antibody are Western blotting and ELISA.

Antibody Attributes:

• Applications: Validated applications for this connexin 43 monoclonal antibody are Western blotting and ELISA.
• Host Species and Isotype: The host species and isotype of this connexin 43 monoclonal antibody is mouse IgG1.
• Clone ID of Monoclonal Antibody (mAb): The connexin 43 monoclonal antibody clone is 3D8A5.
• Reactivity: This connexin 43 monoclonal antibody detects rat and mouse Connexin 43.
• Product Size: Connexin 43 monoclonal antibody is available in a 100 µg pack size.

Intracellular communication mediated by gap junctions plays an important role in a variety of cellular processes, including homeostasis, morphogenesis, cell differentiation, and growth control. Gap junctions are transmembrane channels that serve to directly link neighboring cells by mediating the exchange of low molecular weight metabolites, ions, and second messengers. They are formed by the interaction of connexons, or hemichannels, on adjacent cells. The connexon itself is composed of a hexameric assembly of proteins referred to as connexins. Connexins are highly homologous proteins encoded by a multigene family whose members exhibit similar structural features, including a cytoplasmic amino-terminal region, four transmembrane domains, two extracellular loops, and a carboxy-terminal cytoplasmic tail of varying length. Comparison of the amino acid sequences of the various connexin family members demonstrates divergence in the intracellular loop connecting the second and third TM domains and the carboxy-terminal tail. These domains are thought to mediate connexin type-specific properties, including phosphorylation, response to gating stimuli, assembly, and membrane turnover. Modulation of gap junction communication may be achieved by multiple mechanisms, including alterations in transcription, translation, stability, posttranslational processing (especially phosphorylation), gating, and insertion or removal from the plasma membrane. Interestingly, reduction or alterations in the levels or types of connexin expressed in a given cell type has been found to correlate with tumor progression and metastasis.

The precise regulation of gap junction channels is critical for the passage of signals between cells at the appropriate time and place. Immunostaining of gap junctions in cultured cells indicates that both phosphorylated and unphosphorylated Connexin 43 (Cx43) are present in certain assembled gap junctions, suggesting that assembled proteins do not contain the phosphorylated form of the protein exclusively. The phosphorylation of gap junction proteins appears to regulate channel function and the rates of channel assembly and turnover. Cx43 is phosphorylated at multiple serine residues in vivo; this observation may have direct bearing on the regulation of gap junctional communication via protein kinase protein kinase and MAP kinase. Phosphorylation of Cx43 is not viewed as a requirement for the formation of channels, since truncated versions lacking the apparent phosphorylatable serines can form channels. However, the phosphorylation of Cx43 does appear to regulate the trafficking of Cx43 into gap junctional structures, single channel behavior and Cx43 degradation.