Please contact Steve Kerfoot (skerfoot@uwo.ca) directly with your requests for MOGtag protein expression systems.
Published versions of MOGtag family expression system are available to investigators based on the agreement that:
All shipping costs will be paid for by the requestor.
Material will not be distributed to third parties without permission.
Studies published using MOGtag systems will reference both the original description of the specific version of MOGtag and the protocol for its production. The appropriate references are listed below.
Unpublished versions of the MOGtag family may be available on a collaborative basis.
Note: sequence files can be opened using SnapGene Viewer, available for free here.
The following versions are available upon request:
mMOGtag
Based on the extracellular domain of mouse MOG (aa 1-125)
Codon optimized for bacterial expression
Contains thioredoxin tag for enhanced solubility
TEV protease removal of all tag sequences optional
Original Reference:
Dang AK, Tesfagiorgis Y, Jain RW, Craig HC, and Kerfoot SM. Meningeal infiltration of the spinal cord by non-classically activated B cells is associated with chronic disease course in a spontaneous B cell-dependent model of CNS autoimmune disease. Frontiers in Immunology, 2015; 6:470.
Production Reference:
Jain RW, Dang AK, and Kerfoot SM. Simple and effective production and purification of mouse Myelin Oligodendrocyte Glycoprotein for Experimental Autoimmune Encephalomyelitis. Journal of Visualized Experiments, 2016; 116:e54727
bMOGtag
HUMANIZED MOUSE MOG EXTRACELLULAR DOMAIN
Based on mMOGtag with a "humanized" 35-55 residue via an S42P mutation (as described for a similar reagent by Oliver et.al.).
Immunization with bMOGtag results in a B cell-dependent EAE
Codon optimized for bacterial expression
Contains thioredoxin tag for enhanced solubility
TEV protease removal of all tag sequences optional (note that the neurofilament M peptide is also removed).
Original Reference:
Whittaker Hawkins R, Patenaude A, Dumas A, Jain R, Tesfagiorgis Y, Kerfoot S, Matsui T, Gunzer M, Poubelle P, Larochelle C, Pelletier M, and Vallières L. ICAM1+ neutrophils promote chronic inflammation via ASPRV1 in B cell-dependent autoimmune encephalomyelitis. JCI Insight. 2017; 2(23); e96882.
Production Reference:
Jain RW, Dang AK, and Kerfoot SM. Simple and effective production and purification of mouse Myelin Oligodendrocyte Glycoprotein for Experimental Autoimmune Encephalomyelitis. Journal of Visualized Experiments, 2016; 116:e54727
nfMOGtag
“High Affinity” version of mouse MOG 1-125
Based on mMOGtag
An epitope derived from neurofilament M that is recognized with high affinity by a proportion of MOG35-55 – specific CD4+ T cells (as described by Krishnamoorthy et.al. and Rosenthal et.al.) has been added to the 5' end of mouse MOG 1-125.
Codon optimized for bacterial expression
Contains thioredoxin tag for enhanced solubility
TEV protease removal of all tag sequences optional (note that the neurofilament M peptide is also removed).
Original Reference:
Jain RW, Parham KA, Tesfagiorgis Y, Craig HC, Romanchik E, and Kerfoot SM. Autoreactive, low-affinity T cells preferentially drive differentiation of short-lived Memory B cells at the expense of germinal center maintenance. Cell Reports, 2018; 25(12);3342-3355.
Production Reference:
Jain RW, Dang AK, and Kerfoot SM. Simple and effective production and purification of mouse Myelin Oligodendrocyte Glycoprotein for Experimental Autoimmune Encephalomyelitis. Journal of Visualized Experiments, 2016; 116:e54727
The following versions may be available on a collaborative basis:
rMOGtag
Based on the extracellular domain of rat MOG (aa 1-125)
Codon optimized for bacterial expression
Contains thioredoxin tag for enhanced solubility
TEV protease removal of all tag sequences optional
Original Reference:
not yet published
Production Reference:
Jain RW, Dang AK, and Kerfoot SM. Simple and effective production and purification of mouse Myelin Oligodendrocyte Glycoprotein for Experimental Autoimmune Encephalomyelitis. Journal of Visualized Experiments, 2016; 116:e54727