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. 2018 Feb 9;9:602. doi: 10.1038/s41467-018-02956-z

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© The Author(s) 2018

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 2 — Printed hydrogels can immobilize molecules of varying sizes. a Retention of fluorescein (F, ~332 Da) printed in hydrogel (POA+(POH+F)) following washing in 0.1 M NaOH + 0.1% Tween 20 and fluorescein isothiocyanate-labeled bovine serum albumin (FITC-BSA, ~66 kDa) printed in hydrogel (POA+(POH+BSA)) following washing in 10 mM PBS for 30 min. The high retained fluorescence signal confirms the efficacy of gel inks for protein immobilization. The three adjacent images in each series are replicates, confirming the reproducibility of the result. b FITC-BSA printed in a gelling ink (POA+POH) and a non-gelling ink (PO+POH) imaged by fluorescence microscopy following washing in 10 mM PBS for 30 min (20× magnification). c–e Residual activity of enzymes (E) following washing of samples in 10 mM PBS for 10 min, normalized relative to the corresponding unwashed control. c Alkaline phosphatase (~69 kDa). d Urease (~546 kDa). e β-lactamase (~29 kDa). Values are represented as mean ± SD (n = 3)