Immunoglobulin J chain (IGJ) gene is involved in the polymerization of immunoglobulin (IgA and IgM. It gives polymeric IgA and pentameric IgM ability to bind the polymeric immunoglobulin receptor. In addition, it controls polymeric Ig structure.
J chain is a small glycopeptide and is structurally unrelated to heavy or light chains, but is synthesized by all plasma cells that secrete polymeric immunoglobulins. J chain is linked to IgA and IgM by disulfide bonds, however, it has been detected in IgG- and IgD-containing cells. J chains are present in a large proportion of the immunoglobulin-positive cells in the germinal centers of the tonsil and lymph node. B cells secrete J chain at an early stage of differentiation with the expression persisting in those cells destined to produce IgA or IgM.
Immunogen
Synthetic peptide near the internal region of human J-chain.
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Physical form
0.1 ml rabbit monoclonal antibody purified by protein A/G in PBS/1% BSA buffer pH 7.6 with less than 0.1% sodium azide.
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Scandinavian journal of immunology, 52(3), 240-248 (2000-09-06)
The joining (J) chain is a small polypeptide, expressed by mucosal and glandular plasma cells, which regulates polymer formation of immunoglobulin (Ig)A and IgM. J-chain incorporation into polymeric IgA (pIgA, mainly dimers) and pentameric IgM endows these antibodies with several
The J chain is a component of polymeric immunoglobulin (Ig) molecules and may play an important role in their polymerization and the transport of polymeric Ig across epithelial cells. In this study, the primary structure of the chicken J chain
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