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. 2018 Feb 27;19(3):663. doi: 10.3390/ijms19030663

Figure 1.

Figure 1

Schematic depicting the longest isoform of human tau (441), the antibodies employed and the tau fragment(s) recognized by immunoassays used in this study. (A) Domain structure of tau, including the 2 N-terminal inserts (I1 and I2), the proline-rich domain (P1 and P2), and the microtube-binding repeat domain (R1 to R4), which is required for tau aggregation. (B) Both our full-length ELISA and Simoa assays employ Tau12, a mAb to the extreme N-terminus of tau, and TauAB, a mAb to the extreme C-terminus. (C) Our mid-region assay employs mAbs BT2 and Tau5 which recognize epitopes in the proline-rich domain. This assay is highly similar to those used in clinical research. (D) The Innotest phospho-tau kit (from Fujirebio) employs 2 mid-region directed mAbs; HT7, which recognizes an epitope spanning residues 159–163, and AT270, a mAb specific for phosphorylated threonine 181. Epitopes for the antibodies are indicated by dark grey lines. Sequences of minimal predicted length recognized by a given ELISA are shown in filled boxes and other potentially detectable forms of tau are indicated with dashed lines.