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. 2022 Jun 28;11:e77365. doi: 10.7554/eLife.77365

Figure 1. Functional study of recombinant calmodulin-regulated spectrin-associated protein 2 (CAMSAP2).

(A) Schematic representation of the full-length CAMSAP2 constructs used in this study. CH, calponin-homology domain; MBD, microtubule-binding domain; CC, coiled-coil domain; CKK, C-terminal domain common to CAMSAP1 and two other mammalian proteins, KIAA1078 and KIAA1543. (B) (C) Size exclusion chromatography and SDS-PAGE of the peak fraction of (B) full-length CAMSAP2 and (C) GFP-CAMSAP2. (D) Total internal reflection fluorescence images of polarity-marked microtubules (magenta) decorated with purified GFP-CAMSAP2 (green). The minus-end segment of the microtubule is brighter than the plus-end segment.

Figure 1—source data 1. Figure 1 SDS-PAGE gel of the full-length calmodulin-regulated spectrin-associated protein 2.

Figure 1.

Figure 1—figure supplement 1. Size exclusion chromatography with multi-angle light scattering of the calmodulin-regulated spectrin-associated protein 2-FL.

Figure 1—figure supplement 1.