IgA is a member of the antibody class of the immunoglobulin superfamily. There are several classes and subclasses (isotypes) of antibody, the antibody isotype being defined by the immunoglobulin heavy chain present in the molecule. The basic structure of an immunoglobulin molecule consists of two identical heavy chains (gamma , mu, alpha , delta , epsilon) and two identical light chains, either kappa or lambda. IgA contains the alpha -chain and may be present in a serum or secretory form. In serum, 90% of IgA is monomeric, while in its secretory form it is the main immunoglobulin found in secretions including tears, saliva, intestinal and bronchial mucous, sweat, colostrum, and secretions from the prostate and respiratory epithelia, where it has the job of defending exposed external surfaces of the body against attack from micro organisms. Secretory IgA is synthesized locally by plasma cells and dimerized intracellularly with a cysteine-rich J-chain.
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Clone N1CLA was developed to produce reduced background staining that is associated with polyclonal antibodies on paraffin sections.
Immunoglobulin A is recommended for the detection of specific antigens of interest in normal and neoplastic tissues, as an adjunct to conventional histopathology using non-immunologic histochemical stains.