Bjork, I., Petersson, B.A., and Sjoquist, J. (1972).
Some physiochemical properties of protein A from
Staphylococcus aureus. Eur. J. Biochem. 29,
579–584.
Canziani, G.A., Klakamp, S., and Myszka, D.G.
(2004). Kinetic screening of antibodies from crude
hybridoma samples using Biacore. Anal. Biochem.
325, 301–307.
Helmerhorst, E., Chandler, D.J., Nussio, M., and
Mamotte, C.D. (2012). Real-time and label-free biosensing of molecular interactions by surface
plasmon resonance: a laboratory medicine
perspective. Clin. Biochem. Rev. 33, 161–173.
Hermanson, G.T. (2013). Chapter 3 - the reactions
of bioconjugation. In Bioconjugate Techniques,
Third Edition, G.T. Hermanson, ed. (Academic
Press), pp. 229–258.
Krey, J.F., Krystofiak, E.S., Dumont, R.A.,
Vijayakumar, S., Choi, D., Rivero, F., Kachar, B.,
Jones, S.M., and Barr-Gillespie, P.G. (2016). Plastin
1 widens stereocilia by transforming actin filament
packing from hexagonal to liquid. J. Cell. Biol. 215,
467–482.
Kumaraswamy, S., and Tobias, R. (2015). Label-free
kinetic analysis of an antibody–antigen interaction
using biolayer interferometry. In Protein-Protein
Interactions: Methods and Applications, C.L.
Meyerkord and H. Fu, eds. (Springer New York),
pp. 165–182.
Chudakov, D.M., Matz, M.V., Lukyanov, S., and
Lukyanov, K.A. (2010). Fluorescent proteins and
their applications in imaging living cells and
tissues. Physiol. Rev. 90, 1103–1163.
Hnasko, R.M., and Stanker, L.H. (2015). Hybridoma
technology. In ELISA: Methods and Protocols, R.
Hnasko, ed. (Springer New York), pp. 15–28.
Cuatrecasas, P., and Parikh, I. (1972). Adsorbents
for affinity chromatography. Use of Nhydroxysuccinimide esters of agarose.
Biochemistry 11, 2291–2299.
Hugo, N., Weidenhaupt, M., Beukes, M., Xu, B.,
Janson, J.C., Vernet, T., and Altschuh, D. (2003). VL
position 34 is a key determinant for the engineering
of stable antibodies with fast dissociation rates.
Protein Eng. 16, 381–386.
Lad, L., Clancy, S., Kovalenko, M., Liu, C., Hui, T.,
Smith, V., and Pagratis, N. (2015). High-throughput
kinetic screening of hybridomas to identify highaffinity antibodies using bio-layer interferometry.
J. Biomol. Screen 20, 498–507.
Huh, J.H., White, A.J., Brych, S.R., Franey, H., and
Matsumura, M. (2013). The identification of free
cysteine residues within antibodies and a potential
role for free cysteine residues in covalent
aggregation because of agitation stress. J. Pharm.
Sci. 102, 1701–1711.
Liss, V., Barlag, B., Nietschke, M., and Hensel, M.
(2015). Self-labelling enzymes as universal tags for
fluorescence microscopy, super-resolution
microscopy and electron microscopy. Sci. Rep. 5,
17740.
Freund, J., Casals, J., and Hosmer, E.P. (1937).
Sensitization and antibody formation after injection
of tubercle bacilli and paraffin oil. Exp. Biol. Med.
37, 509–513.
Fukunaga, A., Maeta, S., Reema, B., Nakakido, M.,
and Tsumoto, K. (2018). Improvement of antibody
affinity by introduction of basic amino acid residues
into the framework region. Biochem. Biophys. Rep.
15, 81–85.
Gibbs, D.R., Kaur, A., Megalathan, A., Sapkota, K.,
and Dhakal, S. (2018). Build your own microscope:
step-by-step guide for building a prism-based TIRF
microscope. Methods Protoc. 1, 40.
Griffin, B.A., Adams, S.R., and Tsien, R.Y. (1998).
Specific covalent labeling of recombinant protein
molecules inside live cells. Science 281, 269–272.
Hayashi-Takanaka, Y., Yamagata, K., Wakayama, T.,
Stasevich, T.J., Kainuma, T., Tsurimoto, T.,
Tachibana, M., Shinkai, Y., Kurumizaka, H., Nozaki,
N., et al. (2011). Tracking epigenetic histone
modifications in single cells using Fab-based live
endogenous modification labeling. Nucl. Acids
Res. 39, 6475–6488.
22
Janeway, C.J., Travers, P., Walport, M., and MJ, S.
(2001). Immunobiology, 5th Edition: The Immune
System in Health and Disease (Garland Publishing).
Lyubimova, A., Itzkovitz, S., Junker, J.P., Fan, Z.P.,
Wu, X., and van Oudenaarden, A. (2013). Singlemolecule mRNA detection and counting in
mammalian tissue. Nat. Protoc. 8, 1743–1758.
Jungmann, R., Avendano, M.S., Woehrstein, J.B.,
Dai, M., Shih, W.M., and Yin, P. (2014). Multiplexed
3D cellular super-resolution imaging with DNAPAINT and exchange-PAINT. Nat. Methods 11,
313–318.
Mattheyses, A.L., Simon, S.M., and Rappoport, J.Z.
(2010). Imaging with total internal reflection
fluorescence microscopy for the cell biologist.
J. Cell. Sci. 123, 3621–3628.
Kamat, V., Rafique, A., Huang, T., Olsen, O., and
Olson, W. (2020). The impact of different human
IgG capture molecules on the kinetics analysis of
antibody-antigen interaction. Anal. Biochem. 593,
113580.
Metlagel, Z., Krey, J.F., Song, J., Swift, M.F., Tivol,
W.J., Dumont, R.A., Thai, J., Chang, A., Seifikar, H.,
Volkmann, N., et al. (2019). Electron cryotomography of vestibular hair-cell stereocilia.
J. Struct. Biol. 206, 149–155.
Kiuchi, T., Higuchi, M., Takamura, A., Maruoka, M.,
and Watanabe, N. (2015). Multitarget superresolution microscopy with high-density labeling
by exchangeable probes. Nat. Methods 12,
743–746.
Miyoshi, T., Zhang, Q., Miyake, T., Watanabe, S.,
Ohnishi, H., Chen, J., Vishwasrao, H.D.,
Chakraborty, O., Belyantseva, I.A., Perrin, B.J., et al.
(2021). Semi-automated single-molecule
microscopy screening of fast-dissociating specific
STAR Protocols 2, 100967, December 17, 2021
A Self-archived copy in
Kyoto University Research Information Repository
https://repository.kulib.kyoto-u.ac.jp
ll
Protocol
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antibodies directly from hybridoma cultures. Cell.
Rep. 34, 108708.
antigen interactions in parallel using Biacore A100.
Anal. Biochem. 353, 181–190.
Myszka, D.G. (1999). Improving biosensor analysis.
J. Mol. Recognit. 12, 279–284.
Schneider, C.A., Rasband, W.S., and Eliceiri, K.W.
(2012). NIH Image to ImageJ: 25 years of image
analysis. Nat. Methods 9, 671–675.
Nikolovska-Coleska, Z. (2015). Studying proteinprotein interactions using surface plasmon
resonance. In Protein-Protein Interactions:
Methods and Applications, C.L. Meyerkord and H.
Fu, eds. (Springer New York), pp. 109–138.
Peciak, K., Laurine, E., Tommasi, R., Choi, J.W., and
Brocchini, S. (2019). Site-selective protein
conjugation at histidine. Chem. Sci. 10, 427–439.
Sado, Y., Inoue, S., Tomono, Y., and Omori, H.
(2006). Lymphocytes from enlarged iliac lymph
nodes as fusion partners for the production of
monoclonal antibodies after a single tail base
immunization attempt. Acta Histochem.
Cytochem. 39, 89–94.
Sado, Y., and Okigaki, T. (1996). A novel method for
production of monoclonal antibodies. Evaluation
and expectation of the rat lymph node method in
cell and molecular biology. Cell. Biol. Int. 20, 7–14.
Safsten, P., Klakamp, S.L., Drake, A.W., Karlsson, R.,
and Myszka, D.G. (2006). Screening antibody-
Schuchner, S., Behm, C., Mudrak, I., and Ogris, E.
(2020). The Myc tag monoclonal antibody 9E10
displays highly variable epitope recognition
dependent on neighboring sequence context. Sci.
Signal 13.
Schueder, F., Strauss, M.T., Hoerl, D., Schnitzbauer,
J., Schlichthaerle, T., Strauss, S., Yin, P., Harz, H.,
Leonhardt, H., and Jungmann, R. (2017). Universal
super-resolution multiplexing by DNA exchange.
Angew. Chem. Int. Ed. Engl. 56, 4052–4055.
Sekerkova, G., Richter, C.P., and Bartles, J.R. (2011).
Roles of the espin actin-bundling proteins in the
morphogenesis and stabilization of hair cell
stereocilia revealed in CBA/CaJ congenic jerker
mice. PLoS Genet. 7, e1002032.
Skwarczynski, M., and Toth, I. (2016). Peptidebased synthetic vaccines. Chem. Sci. 7, 842–854.
Son, K.K., Tkach, D., and Rosenblatt, J. (2001).
Delipidated serum abolishes the inhibitory effect of
serum on in vitro liposome-mediated transfection.
Biochim. Biophys. Acta (Bba) - Biomembranes
1511, 201–205.
Song, H.N., Kim, D.H., Park, S.G., Lee, M.K., Paek,
S.H., and Woo, E.J. (2015). Purification and
characterization of Fab fragments with rapid
reaction kinetics against myoglobin. Biosci.
Biotechnol. Biochem. 79, 718–724.
Stils, H.F. (2005). Adjuvants and antibody
production: dispelling the myths associated with
freund’s complete and other adjuvants. ILAR J. 46,
280–293.
Vauquelin, G., and Charlton, S.J. (2013). Exploring
avidity: understanding the potential gains in
functional affinity and target residence time of
bivalent and heterobivalent ligands. Br. J.
Pharmacol. 168, 1771–1785.
Wallace, T.J. (2002). Reactions of thiols with metals.
I. Low-temperature oxidation by metal oxides1.
J. Org. Chem. 31, 1217–1221.
Ylera, F., Harth, S., Waldherr, D., Frisch, C., and
Knappik, A. (2013). Off-rate screening for selection
of high-affinity anti-drug antibodies. Anal Biochem.
441, 208–213.
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