ABSTRACT
This study characterizes three monoclonal antibodies (mAbs) developed against the constant (C) region of the immunoglobulin light (IgL) sigma chain isotype of the channel catfish, Ictalurus punctatus. Microsphere bead assays and Western blot analyses utilizing different recombinant (r) proteins show that these anti-catfish IgL sigma chain mAbs each specifically recognize the denatured form of IgL sigma. Importantly, Western blotting of catfish sera using the anti-IgL sigma mAbs also identified an IgL chain-sized immunoreactive band(s) of approximately 27kDa. It is anticipated that these mAbs in combination with the already existing anti-catfish Ig heavy (H) and IgL chain mAbs will be useful in future studies examining the functional roles of the different catfish IgL isotypes.
