The connexin family of proteins form hexameric complexes called “connexons” that facilitate movement of low molecular weight proteins between cells via gap junctions. Connexin proteins share a common topology of 4 transmembrane alpha-helical domains, two extracellular loops, a cytoplasmic loop, and cytoplasmic N- and C-termini. Many of the key functional differences arise from specific amino-acid substitutions in the most highly conserved domains, the transmembrane and extracellular regions. Each of the approximately 20 connexin isoforms produces channels with distinct permeabilities and electrical and chemical sensitivities; therefore, one connexin usually cannot fully substitute for another. Consequently, a wide variety of malignant phenotypes associate with decreased connexin expression and gap junction communication, dependent on the particular connexin that is effected. For example, upregulation of connexin 40 following cardiac surgery can mark a susceptibility to post-operative atrial fibrillation.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of connexin 40 of human and, to a lesser extent, mouse and rat origin by WB, IP, IF and ELISA
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 231-346 mapping within a C-terminal cytoplasmic domain of connexin 40 of human origin
Tissue Specificity
epitope corresponding to amino acids 231-346 mapping within a C-terminal cytoplasmic domain of connexin 40 of human origin