Immunoglobulin J (IgJ), also known as the joining chain, is a crucial protein in the immune system. It is synthesized in B lymphocytes and plays a significant role in the formation of polymeric immunoglobulins, particularly IgM and IgA. The recombinant form of this protein, produced through genetic engineering techniques, has become an essential tool in research and therapeutic applications.
IgJ is a 137-amino acid protein that serves two primary functions:
The gene encoding IgJ is located on chromosome 4q21 in humans. This region is known for its genetic variability, including polymorphisms that can be useful in genetic linkage studies . The IgJ gene is adjacent to the CRLZ1 gene, and their expression is regulated in a stage-specific manner. IgJ is expressed in plasma cells, while CRLZ1 is expressed in pre-B cells .
Recombinant IgJ is produced using various expression systems, including bacterial, yeast, and mammalian cells. The recombinant form retains the functional properties of the native protein, making it valuable for research and therapeutic purposes. The production process involves cloning the IgJ gene into an expression vector, transforming the host cells, and purifying the expressed protein.