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  • Title: Expression and purification of biologically active domain I of the human polymeric immunoglobulin receptor.
    Author: Bakos MA, Widen SG, Goldblum RM.
    Journal: Mol Immunol; 1994 Feb; 31(2):165-8. PubMed ID: 8309479.
    Abstract:
    Previous studies using proteolytic fragments and synthetic peptides have indicated that domain I of human polymeric immunoglobulin receptor (PIgR) is necessary for ligand binding. The expression in E. coli, and subsequent IgM-affinity purification of domain I of human PIgR is described. The recombinant domain I protein (rDI) was similar in structure to native SC domain I in that it bound specifically to MAb 6G11, an antibody which recognizes a critical portion of the PIg binding site in domain I. The biological activity of rDI was indicated by high affinity binding to PIgA (Kd = 1.6 x 10(-7) M) and IgM (Kd = 5.1 x 10(-7) M). Domain I of human SC is therefore sufficient for binding to PIg.
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