Immunoglobulin J chain Protein, Mouse (P.pastoris, His)

The Immunoglobulin J chain links IgM or IgA monomers. In IgM, J chain-joined dimers nucleate the IgM pentamer, while in IgA, it induces dimer or polymer formation. It also binds these immunoglobulins to the secretory component. As part of the sIgA complex, it integrates with IgA monomers, the J chain, and the secretory component (PIGR proteolytic product). Immunoglobulin J chain Protein, Mouse (P.pastoris, His) is the recombinant mouse-derived Immunoglobulin J chain protein, expressed by P. pastoris , with N-His labeled tag. The total length of Immunoglobulin J chain Protein, Mouse (P.pastoris, His) is 138 a.a., with molecular weight of ~17.7 kDa.

The Immunoglobulin J chain serves as a crucial link connecting two monomer units of either IgM or IgA. In the context of IgM, the J chain-joined dimer acts as a nucleating unit for the IgM pentamer, while for IgA, it induces the formation of dimers and/or larger polymers. Additionally, the Immunoglobulin J chain plays a role in binding these immunoglobulins to the secretory component. It is an integral part of the secretory IgA (sIgA) complex, which comprises two, four, or five IgA monomers and two additional non-Ig polypeptides, namely the J chain and the secretory component (the proteolytic product of PIGR).

Mouse

P. pastoris

N-His

P01592 (22G-159D)

16069  [NCBI]

GDDEATILADNKCMCTRVTSRIIPSTEDPNEDIVERNIRIVVPLNNRENISDPTSPLRRNFVYHLSDVCKKCDPVEVELEDQVVTATQSNICNEDDGVPETCYMYDRNKCYTTMVPLRYHGETKMVQAALTPDSCYPD

Approximately 17.7 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.