Mouse Anti-TTR Recombinant Antibody (clone 39-44) (CAT#: PABZ-128)

Figure 1 Immunoprecipitation of TTR mutants with mAb (39-44).

The three groups of lanes represent boiled samples of three different mutants: Ser77Tyr, Tyr78Phe and Trp79His, respectively. The frst lane of each group represents the original protein preparations (before immunoprecipitation) and the second and third lane of each group represent immunoprecipitated samples, with (‡+) or without (-) addition of β-mercaptoethanol. T, tetramer; M, monomer.

Redondo, C., Damas, A. M., Olofsson, A., Lundgren, E., & Saraiva, M. J. M. (2000). Search for intermediate structures in transthyretin fibrillogenesis: soluble tetrameric Tyr78Phe TTR expresses a specific epitope present only in amyloid fibrils1. Journal of molecular biology, 304(3), 461-470.

Figure 2 Interaction between mAb (39-44) coupled on a CM5 sensor chip, and a series of concentrations of soluble Tyr78Phe (2.3 μM - 9 nM). RU, resonance units

Redondo, C., Damas, A. M., Olofsson, A., Lundgren, E., & Saraiva, M. J. M. (2000). Search for intermediate structures in transthyretin fibrillogenesis: soluble tetrameric Tyr78Phe TTR expresses a specific epitope present only in amyloid fibrils1. Journal of molecular biology, 304(3), 461-470.

Figure 3 Immunodetection of TTR by sandwich ELISA with mAb (39-44) and anti-TTR polyclonal antibody (pAb).

Fractions were obtained after gel chromatography of both WT and Tyr78Phe preparations that passed on the BIAcore sensor chip. The A₂₈₀ profile obtained for both TTR preparations (not represented) overlapped immunodetection with pAb. The protein standards used to calibrate the column were: bovine serum albumin (67 kDa), ovalbumin (43 kDa), chymotrypsinogen A (25 kDa) and ribonuclease A (13.7 kDa).

Redondo, C., Damas, A. M., Olofsson, A., Lundgren, E., & Saraiva, M. J. M. (2000). Search for intermediate structures in transthyretin fibrillogenesis: soluble tetrameric Tyr78Phe TTR expresses a specific epitope present only in amyloid fibrils1. Journal of molecular biology, 304(3), 461-470.

Figure 4 Immunoreactivity of size variants of the TTRs53–55 mutant separated by size-exclusion HPLC.

Size-exclusion HPLC of TTRs53–55 mutant freshly prepared (A) or aggregated in 37°C for 24 h (B). Immunoblot from native PAGE of size-exclusion HPLC fractions with polyclonal antibody (C), mAb 56–61 (D), or mAb 39–44 (E). Lanes 1–4 and 6–8 correspond to HPLC fractions as indicated; lane 5 was loaded with wild-type TTR. Lanes: 1–4, fresh material; 6–8, aggregated TTR. Arrows indicate the position of TTR tetramer; OVA (ovalbumin) and BSA indicate size markers.

Goldsteins, G., Persson, H., Andersson, K., Olofsson, A., Dacklin, I., Edvinsson, Å., ... & Lundgren, E. (1999). Exposure of cryptic epitopes on transthyretin only in amyloid and in amyloidogenic mutants. Proceedings of the National Academy of Sciences, 96(6), 3108-3113.

Figure 5 SAP co-localizes with TTR-A in Drosophila eye and counteracts TTR-induced retinal degeneration.

(A–D) TTR-A was detected with a TTR-specific monoclonal antibody (Mab39–44; in red), and co-localized with SAP immunostaining (Epitomics; in green) in horizontal sections of heads of 2-week-old flies. (E–H) TTR-A was detected with TTR-specific polyclonal antibody (red). TTR-A aggregates were monitored with p-FTAA (green). (A, B) TTR-A secreted by the photoreceptors accumulated in the retinal compartment (E, F) and formed aggregates around the outer corneal layer (CL). This led to damage of the retinal array and leakage of TTR-A outside the CL. The two neighboring corneal lenses (arrows) are shown magnified at the upper left corner (insets). (C) SAP expressed alone in fly retina stayed soluble, as no p-FTAA aggregates were detected (G) and there were no degenerative changes. Co-localization of SAP with TTR-A prevented retinal damage in SAP/TTR-A fruit flies (D), and led to reduced p-FTAA staining in the CL (H). Drosophila genotypes: TTR-A/− (w; GMR-Gal4/+; UAS-TTR-A/+); TTR-A/TTR-A (w; GMR-Gal4/GMR-Gal4; UAS-TTR-A/UAS-TTR-A); −/SAP (w; GMR-Gal4/+; +/UAS-SAP); TTR-A/SAP (w; GMR-Gal4/+; UAS-SAP/TTR-A). Scale bar represents 50 µm.

Andersson, K., Pokrzywa, M., Dacklin, I., & Lundgren, E. (2013). Inhibition of TTR Aggregation-Induced Cell Death–A New Role for Serum Amyloid P Component. PLoS One, 8(2), e55766.