Anti-NIP human IgG1-M252Y/S254T/T246E/H433K/N434FSKU: P-117

General description: 

This is mouse-human chimeric IgG1 and 3 variants harboring human heavy chains and mouse lambda light chains with specificity for the hapten NIP (4-hydroxy-3-iodo-5-nitrophenylacetic acid). In addition to the WT variants, a panel of IgG1 Fc mutated variants is listed.
IgG1 with the N297A mutation removes the N-glycosylation motif and thus eliminates binding to the classical Fc gamma receptors. The IgG1 mutants H310A, H435A and H310A/H435A modulate or eliminate binding to the neonatal Fc receptor (FcRn).
The IgG1 antibodies with combination of mutations have been made based on published papers describing Fc- mutant variants with improved binding to human FcRn, however, here we have produced them with the same framework and specificity. The IgG1 variant containing M252Y/S254T/T246E/H433K/N434F (MST/HN) is a so-called “abdeg” molecule, which binds the receptor more strongly at both acidic as well as neutral pH and thus acts as a blocker for binding of competing IgG. IgG1-M252Y/S254T/T246E (MST or YTE), IgG1-H433K/N434F (MN) and IgG1-H433K/N434F (HN) contain Fc-mutations that improve pH dependent binding to FcRn, which give rise to extended serum half-life.

Construction of the anti-NIP antibodies is described here:
 Grevys A, Bern M, Foss S, Bratlie DB, Moen A, Gunnarsen KS, Aase A, Michaelsen TE, Sandlie I, Andersen JT. J Immunol. 2015 Jun 1;194(11):5497-508

References to the original papers describing the mutations are given in this publication.

About the scientist

Jan Terje Andersen

Associate Professor

The Laboratory for Adaptive Immunity and Homeostasis is studying the cellular processes and molecular interplay underlying the functions of the two most abundant proteins in the blood, albumin and IgG. By combining structural and biophysical approaches with cellular and in vivo studies, we use the insights to design novel albumin and IgG molecules with improved binding properties and cellular functions.

 

visit http://ous-research.no/andersen/

visit http://www.mn.uio.no/ibv/english/people/aca/janta/