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IgG and IgM antibodies to the refolded MOG(1-125) extracellular domain in humans.

Journal of neuroimmunology (2011-01-11)
Francesca Gori, Barbara Mulinacci, Lara Massai, Carlo Avolio, Mariantonietta Caragnano, Elisa Peroni, Silvia Lori, Mario Chelli, Anna Maria Papini, Paolo Rovero, Francesco Lolli
ABSTRACT

Antibodies to MOG in serum have a dubious prognostic value in multiple sclerosis. The MOG recombinant protein conformational properties relevant to the antigenic activity are unknown. We employed a solid-phase ELISA based on a product (rMOG(ED)(His)(6)) expressed in E. coli after subcloning the cDNA of the extracellular domain of rat MOG, performing a refolding procedure on column and affinity purification. The far-UV Circular Dichroism (CD) spectra of rMOG(ED)(His)(6) showed a β-sheet, a characteristic feature of the Ig-fold. However, in MS sera and controls we failed to detected IgM or IgG antibodies.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Anti-Human IgG (γ-chain specific), F(ab′)2 fragment−Alkaline Phosphatase antibody produced in goat, affinity isolated antibody, buffered aqueous glycerol solution
Sigma-Aldrich
Anti-Human IgM (μ-chain specific)−Alkaline Phosphatase antibody produced in goat, affinity isolated antibody, buffered aqueous glycerol solution

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