Figure S2: Site-specific O-GlcNAc-CRMP2 antibody (OG-CRMP2) recognises Ser517 O-GlcNAcylated CRMP2 in vitro and in vivo.; Figure S3 from Loss of CRMP2 O-GlcNAcylation leads to reduced novel object recognition performance in mice
Figure S2: Site-specific O-GlcNAc-CRMP2 antibody (OG-CRMP2) recognises Ser517 O-GlcNAcylated CRMP2 in vitro and in vivo.; Figure S3 from Loss of CRMP2 O-GlcNAcylation leads to reduced novel object recognition performance in mice
Figure S2: Site-specific O-GlcNAc-CRMP2 antibody (OG-CRMP2) recognises Ser517 O-GlcNAcylated CRMP2 in vitro and in vivo. (a) Western blot on in vitro glycosylated recombinant CRMP2 using the OG-CRMP2 antibody. Lack of signal on non-O-GlcNAcylated and Ser517Ala CRMP2 samples indicates that the antibody is specific. (b) Western blot on mouse brain lysate using the OG-CRMP2 antibody showing that the antibody detects O-GlcNAcylated CRMP2 from complex samples. CpOGA treatment removes O-GlcNAc from proteins and the Ser517Ala mutation abolishes O-GlcNAcylation on CRMP2.Supplementary Figure S3: O-GlcNAc-CRMP2 levels in samples from Alzheimer's disease patients. (a) Western blotting for O-GlcNAc-CRMP2 (OG-CRMP2) on post-mortem hippocampus samples from Alzheimer's disease patients (AD) and age-matched non-Alzheimer's disease individuals (CTL) (n = 5, 75-80 years old).
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