Mouse Anti-PRNP Recombinant Antibody (clone 3F4) (CAT#: PABW-089)

Figure 1 PrPC cleavage analysis.

Immunoblots of truncated proteins from the three PRNP codon 129 genotypes in PBMCs. After PNGase treatment, denatured lysates from 106 PBMCs were tested by Western Blot analysis using 4 antibodies to span the large PrP region: SAF32 (79–91), 8G8 (95–110), 3F4 (109–112) and PRI 917 (216–221). The 27–28 kDa band corresponds to the M.W. of the unglycosylated Full-Length (F.L.) protein, while the bands near 20 kDa and 18 kDa correspond to the C2 and C1 fragments, respectively.

Segarra, C. , Lehmann, S. , & Coste, J. . (2009). Prion protein expression and processing in human mononuclear cells: the impact of the codon 129 prion gene polymorphism. PLOS ONE, 4.

Figure 2 Confocal microscopy of Drosophila S2 cells transiently transfected with mouse 3F4 or hamster PrP constructs.

Drosophila S2 cells were transiently co-transfected with pUASTattB plasmids which contained insert DNA that encoded (a) mouse 3F4 PrP variants; (b) hamster PrP variants or (c) ovine VRQ(GPI), together with the pWA-GAL4-driver plasmid. Cells 24 h post-transfection were fixed with or without prior permeabilisation by treatment with Triton X-100. Mock-transfected cells were treated with the Effectene transfection reagent. Prepared cells were subsequently reacted with the anti-PrP monoclonal antibody 4H11, and additionally with the anti-Golgi polyclonal antibody GM130 in the case of permeabilised cells, prior to confocal microscopy. Nuclei were counterstained with Hoechst. Scale bar: 2 μm.

Thackray, A. M. , Cardova, A. , Wolf, H. , Pradl, L. , & Bujdoso, R. . (2017). Genetic human prion disease modelled in prp transgenic drosophila. Biochemical Journal, 474(19), BCJ20170462.

Figure 4 Fractions P3 prepared from whole brains of Tg(PG14) or Prnp0/0 mice were perfused for 5 min (bars) over the sensor surface of SPR chips on which antibody 15B3 (A) or 3F4 (B) had been immobilized.

The sensorgrams (time course of the SPR signal in Resonance Units, RU) refer to the specific binding to the antibody (binding was negligible on sensor surfaces without antibody). Significant binding was detected when P3 fractions containing PG14 PrP (black line) were flowed over the 15B3-coated chip (A), but not on the 3F4-coated chip (B). No binding was observed when a P3 fraction from Prnp0/0 mice was analyzed (gray line).