Abstract
This study characterizes three monoclonal antibodies (mAbs) developed against the constant (C) region of the immunoglobulin light (IgL) σ 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 σ chain mAbs each specifically recognize the denatured form of IgL σ. Importantly, Western blotting of catfish sera using the anti-IgL σ mAbs also identified an IgL chain-sized immunoreactive band(s) of ∼27 kDa. 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.
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