α-l-Arabinofuranosidase as an Orthogonal Enzyme for Human Cells-Reference-Cited by-同舟云学术

α-l-Arabinofuranosidase as an Orthogonal Enzyme for Human Cells

Published:2021-08-05 Issue:8 Volume:50 Page:1493-1495
ISSN:0366-7022
Container-title:Chemistry Letters
language:en
Short-container-title:Chem. Lett.

Author:

Kaneko Ryosuke¹,Oda Tsuyoshi²,Yoshida Ryosuke²,Tateishi Chuya²,Tanito Kenta²,Nii Teruki¹,Kishimura Akihiro¹²³⁴,Kamiya Noriho¹³,Mori Takeshi¹²³,Katayama Yoshiki¹²³⁴⁵

Affiliation:

1. Department of Applied Chemistry, Faculty of Engineering, Kyushu University, 744 Motooka, Nishi-ku, Fukuoka 819-0395, Japan

2. Graduate School of Systems Life Sciences, Kyushu University, 744 Motooka, Nishi-ku, Fukuoka 819-0395, Japan

3. Center for Future Chemistry, Kyushu University, 744 Motooka, Nishi-ku, Fukuoka 819-0395, Japan

4. International Research Center for Molecular Systems, Kyushu University, 744 Motooka, Nishi-ku, Fukuoka 819-0395, Japan

5. Department of Biomedical Engineering, Chung Yuan Christian University, 200 Chung Pei Rd., Chung Li, 32023 ROC, Taiwan

Publisher

The Chemical Society of Japan

Subject

General Chemistry

Link

http://www.journal.csj.jp/doi/pdf/10.1246/cl.210231

Reference20 articles.

1. Cell-ELISA using β-galactosidase conjugated antibodies

2. A solid-phase β-galactosidase ELISA for detecting and quantifying monoclonal antibody binding to dissociated cell cultures of postnatal rodent cerebellum

3. Fluorescence Signal Amplification by Using β-Galactosidase for Flow Cytometry; Advantages of an Endogenous Activity-Free Enzyme

4. Endogenous peroxidases in sputum interfere with horse-radish peroxidase-based ELISAs

5. Why are mammalian alkaline phosphatases much more active than bacterial alkaline phosphatases?

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