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BCA-detected protein in EV suspensions and in <t>the</t> <t>300-kDa</t> flow-through after ultralow Triton X-100 exposure. (A) Normalized BCA (stress) for EV + 0.0001% Triton and EV + 0.001% Triton are shown. (B) Normalized BCA (stress + centrifuge) for EV + 0.0001% Triton and EV + 0.001% Triton are shown. Data are mean ± SD (n = 3 independent lots).
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BCA-detected protein in EV suspensions and in <t>the</t> <t>300-kDa</t> flow-through after ultralow Triton X-100 exposure. (A) Normalized BCA (stress) for EV + 0.0001% Triton and EV + 0.001% Triton are shown. (B) Normalized BCA (stress + centrifuge) for EV + 0.0001% Triton and EV + 0.001% Triton are shown. Data are mean ± SD (n = 3 independent lots).
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BCA-detected protein in EV suspensions and in <t>the</t> <t>300-kDa</t> flow-through after ultralow Triton X-100 exposure. (A) Normalized BCA (stress) for EV + 0.0001% Triton and EV + 0.001% Triton are shown. (B) Normalized BCA (stress + centrifuge) for EV + 0.0001% Triton and EV + 0.001% Triton are shown. Data are mean ± SD (n = 3 independent lots).
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BCA-detected protein in EV suspensions and in <t>the</t> <t>300-kDa</t> flow-through after ultralow Triton X-100 exposure. (A) Normalized BCA (stress) for EV + 0.0001% Triton and EV + 0.001% Triton are shown. (B) Normalized BCA (stress + centrifuge) for EV + 0.0001% Triton and EV + 0.001% Triton are shown. Data are mean ± SD (n = 3 independent lots).
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BCA-detected protein in EV suspensions and in <t>the</t> <t>300-kDa</t> flow-through after ultralow Triton X-100 exposure. (A) Normalized BCA (stress) for EV + 0.0001% Triton and EV + 0.001% Triton are shown. (B) Normalized BCA (stress + centrifuge) for EV + 0.0001% Triton and EV + 0.001% Triton are shown. Data are mean ± SD (n = 3 independent lots).
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BCA-detected protein in EV suspensions and in <t>the</t> <t>300-kDa</t> flow-through after ultralow Triton X-100 exposure. (A) Normalized BCA (stress) for EV + 0.0001% Triton and EV + 0.001% Triton are shown. (B) Normalized BCA (stress + centrifuge) for EV + 0.0001% Triton and EV + 0.001% Triton are shown. Data are mean ± SD (n = 3 independent lots).
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BCA-detected protein in EV suspensions and in <t>the</t> <t>300-kDa</t> flow-through after ultralow Triton X-100 exposure. (A) Normalized BCA (stress) for EV + 0.0001% Triton and EV + 0.001% Triton are shown. (B) Normalized BCA (stress + centrifuge) for EV + 0.0001% Triton and EV + 0.001% Triton are shown. Data are mean ± SD (n = 3 independent lots).
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BCA-detected protein in EV suspensions and in the 300-kDa flow-through after ultralow Triton X-100 exposure. (A) Normalized BCA (stress) for EV + 0.0001% Triton and EV + 0.001% Triton are shown. (B) Normalized BCA (stress + centrifuge) for EV + 0.0001% Triton and EV + 0.001% Triton are shown. Data are mean ± SD (n = 3 independent lots).

Journal: Frontiers in Bioengineering and Biotechnology

Article Title: Membrane lipid order predicts potency decline in therapeutic extracellular vesicles following handling, storage, and reconstitution stress

doi: 10.3389/fbioe.2026.1795387

Figure Lengend Snippet: BCA-detected protein in EV suspensions and in the 300-kDa flow-through after ultralow Triton X-100 exposure. (A) Normalized BCA (stress) for EV + 0.0001% Triton and EV + 0.001% Triton are shown. (B) Normalized BCA (stress + centrifuge) for EV + 0.0001% Triton and EV + 0.001% Triton are shown. Data are mean ± SD (n = 3 independent lots).

Article Snippet: Second, after Triton exposure, vortex mixing, freeze–thaw, or lyophilization-reconstitution treatments, samples were processed using a 300-kDa molecular-weight-cutoff centrifugal filter (Vivaspin; Sartorius, Ann Arbor, MI, United States) to physically separate vesicle-sized material from soluble, extravesicular components.

Techniques: