Immunoglobulin M

Athens Research

Immunoglobulin M

9

Structural Studies, Antisera Production

Research Use Only

≥98% by SDS-PAGE. No reaction by IEP to antisera to kappa or lambda

The Immunoglobulin M (IgM) Fc5u fragment, comprising the constant region (Cu2-Cu4 domains) of the u heavy chain, mediates critical immune functions despite lacking antigen-binding capacity. This fragment drives complement fixation via C1q binding, with studies showing its pentameric form in Waldenström macroglobulinemia exhibits 19-fold higher complement activation than intact IgM. Structurally, the Fc5u's conserved N-glycosylation at Asn-297 stabilizes its conformation and enables interactions with Fc receptors (FcuR) on B cells, T cells, and NK cells, modulating immune responses like phagocytosis and antibody-dependent cytotoxicity. While IgM typically lacks placental transfer due to its size, Fc5u's interaction with FcRn-a receptor critical for IgG transcytosis-hints at nuanced roles in maternal-fetal immunity, though this requires further elucidation.

more then 1 year

Source human plasma non-reactive for HBsAG, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests.

≤ -80° C

12352202