Affimer proteins are versatile and renewable affinity reagents.

C Tiede; R Bedford; SJ Heseltine; G Smith; I Wijetunga; R Ross; D AlQallaf; AP Roberts; A Balls; A Curd; RE Hughes; H Martin; S R Needham; L C Zanetti-Domingues; Y Sadigh; T P Peacock; A A Tang; N Gibson; H Kyle; G W Platt; N Ingram; T Taylor; L P  Coletta; I Manfield; M Knowles; S Bell; F Esteves; A Maqbool; R K Prasad; M Drinkhill; R S Bon; V Patel; S Goodchild; M Martin-Fernandez; R J Owens; J E  Nettleship; M E  Webb; M Harrison; J D  Lippiat; S Ponnambalam; M Peckham; A Smith; P K  Ferrigno; M Johnson; M J McPherson; D C  Tomlinson

doi:10.7554/elife.24903

Affimer proteins are versatile and renewable affinity reagents.

C Tiede, R Bedford, SJ Heseltine, G Smith, I Wijetunga, R Ross, D AlQallaf, AP Roberts, A Balls, A Curd, RE Hughes, H Martin, S R Needham, L C Zanetti-Domingues, Y Sadigh, T P Peacock, A A Tang, N Gibson, H Kyle, G W PlattN Ingram, T Taylor, L P Coletta, I Manfield, M Knowles, S Bell, F Esteves, A Maqbool , R K Prasad, M Drinkhill, R S Bon, V Patel, S Goodchild, M Martin-Fernandez, R J Owens, J E Nettleship, M E Webb, M Harrison, J D Lippiat, S Ponnambalam, M Peckham, A Smith, P K Ferrigno, M Johnson, M J McPherson, D C Tomlinson

Research output: Contribution to journal › Article › peer-review

138 Citations (Scopus)

74 Downloads (Pure)

Abstract

Molecular recognition reagents are key tools for understanding biological processes and are used universally by scientists to study protein expression, localisation and interactions. Antibodies remain the most widely used of such reagents and many show excellent performance, although some are poorly characterised or have stability or batch variability issues, supporting the use of alternative binding proteins as complementary reagents for many applications. Here we report on the use of Affimer proteins as research reagents. We selected 12 diverse molecular targets for Affimer selection to exemplify their use in common molecular and cellular applications including the (a) selection against various target molecules; (b) modulation of protein function in vitro and in vivo; (c) labelling of tumour antigens in mouse models; and (d) use in affinity fluorescence and super-resolution microscopy. This work shows that Affimer proteins, as is the case for other alternative binding scaffolds, represent complementary affinity reagents to antibodies for various molecular and cell biology applications.

Original language	English
Article number	e24903
Number of pages	35
Journal	eLife
Volume	6
DOIs	https://doi.org/10.7554/elife.24903
Publication status	Published - 27 Jun 2017
Externally published	Yes

Bibliographical note

This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited.

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.7554/elife.24903Licence: CC BY

elife-24903-v2Final published version, 6.96 MBLicence: CC BY

Cite this

Tiede, C., Bedford, R., Heseltine, SJ., Smith, G., Wijetunga, I., Ross, R., AlQallaf, D., Roberts, AP., Balls, A., Curd, A., Hughes, RE., Martin, H., Needham, S. R., Zanetti-Domingues, L. C., Sadigh, Y., Peacock, T. P., Tang, A. A., Gibson, N., Kyle, H., ... Tomlinson, D. C. (2017). Affimer proteins are versatile and renewable affinity reagents. eLife, 6, Article e24903. https://doi.org/10.7554/elife.24903

Tiede, C, Bedford, R, Heseltine, SJ, Smith, G, Wijetunga, I, Ross, R, AlQallaf, D, Roberts, AP, Balls, A, Curd, A, Hughes, RE, Martin, H, Needham, SR, Zanetti-Domingues, LC, Sadigh, Y, Peacock, TP, Tang, AA, Gibson, N, Kyle, H, Platt, GW, Ingram, N, Taylor, T, Coletta, LP, Manfield, I, Knowles, M, Bell, S, Esteves, F, Maqbool , A, Prasad, RK, Drinkhill, M, Bon, RS, Patel, V, Goodchild, S, Martin-Fernandez, M, Owens, RJ, Nettleship, JE, Webb, ME, Harrison, M, Lippiat, JD, Ponnambalam, S, Peckham, M, Smith, A, Ferrigno, PK, Johnson, M, McPherson, MJ & Tomlinson, DC 2017, 'Affimer proteins are versatile and renewable affinity reagents.', eLife, vol. 6, e24903. https://doi.org/10.7554/elife.24903

@article{80458aa7acdc4eb59ffd7bd43ed1a5ac,

title = "Affimer proteins are versatile and renewable affinity reagents.",

abstract = "Molecular recognition reagents are key tools for understanding biological processes and are used universally by scientists to study protein expression, localisation and interactions. Antibodies remain the most widely used of such reagents and many show excellent performance, although some are poorly characterised or have stability or batch variability issues, supporting the use of alternative binding proteins as complementary reagents for many applications. Here we report on the use of Affimer proteins as research reagents. We selected 12 diverse molecular targets for Affimer selection to exemplify their use in common molecular and cellular applications including the (a) selection against various target molecules; (b) modulation of protein function in vitro and in vivo; (c) labelling of tumour antigens in mouse models; and (d) use in affinity fluorescence and super-resolution microscopy. This work shows that Affimer proteins, as is the case for other alternative binding scaffolds, represent complementary affinity reagents to antibodies for various molecular and cell biology applications.",

author = "C Tiede and R Bedford and SJ Heseltine and G Smith and I Wijetunga and R Ross and D AlQallaf and AP Roberts and A Balls and A Curd and RE Hughes and H Martin and Needham, {S R} and Zanetti-Domingues, {L C} and Y Sadigh and Peacock, {T P} and Tang, {A A} and N Gibson and H Kyle and Platt, {G W} and N Ingram and T Taylor and Coletta, {L P} and I Manfield and M Knowles and S Bell and F Esteves and A Maqbool and Prasad, {R K} and M Drinkhill and Bon, {R S} and V Patel and S Goodchild and M Martin-Fernandez and Owens, {R J} and Nettleship, {J E} and Webb, {M E} and M Harrison and Lippiat, {J D} and S Ponnambalam and M Peckham and A Smith and Ferrigno, {P K} and M Johnson and McPherson, {M J} and Tomlinson, {D C}",

note = "This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited. ",

year = "2017",

month = jun,

day = "27",

doi = "10.7554/elife.24903",

language = "English",

volume = "6",

journal = "eLife",

issn = "2050-084X",

publisher = "eLife Sciences Publications",

}

TY - JOUR

T1 - Affimer proteins are versatile and renewable affinity reagents.

AU - Tiede, C

AU - Bedford, R

AU - Heseltine, SJ

AU - Smith, G

AU - Wijetunga, I

AU - Ross, R

AU - AlQallaf, D

AU - Roberts, AP

AU - Balls, A

AU - Curd, A

AU - Hughes, RE

AU - Martin, H

AU - Needham, S R

AU - Zanetti-Domingues, L C

AU - Sadigh, Y

AU - Peacock, T P

AU - Tang, A A

AU - Gibson, N

AU - Kyle, H

AU - Platt, G W

AU - Ingram, N

AU - Taylor, T

AU - Coletta, L P

AU - Manfield, I

AU - Knowles, M

AU - Bell, S

AU - Esteves, F

AU - Maqbool , A

AU - Prasad, R K

AU - Drinkhill, M

AU - Bon, R S

AU - Patel, V

AU - Goodchild, S

AU - Martin-Fernandez, M

AU - Owens, R J

AU - Nettleship, J E

AU - Webb, M E

AU - Harrison, M

AU - Lippiat, J D

AU - Ponnambalam, S

AU - Peckham, M

AU - Smith, A

AU - Ferrigno, P K

AU - Johnson, M

AU - McPherson, M J

AU - Tomlinson, D C

N1 - This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited.

PY - 2017/6/27

Y1 - 2017/6/27

N2 - Molecular recognition reagents are key tools for understanding biological processes and are used universally by scientists to study protein expression, localisation and interactions. Antibodies remain the most widely used of such reagents and many show excellent performance, although some are poorly characterised or have stability or batch variability issues, supporting the use of alternative binding proteins as complementary reagents for many applications. Here we report on the use of Affimer proteins as research reagents. We selected 12 diverse molecular targets for Affimer selection to exemplify their use in common molecular and cellular applications including the (a) selection against various target molecules; (b) modulation of protein function in vitro and in vivo; (c) labelling of tumour antigens in mouse models; and (d) use in affinity fluorescence and super-resolution microscopy. This work shows that Affimer proteins, as is the case for other alternative binding scaffolds, represent complementary affinity reagents to antibodies for various molecular and cell biology applications.

AB - Molecular recognition reagents are key tools for understanding biological processes and are used universally by scientists to study protein expression, localisation and interactions. Antibodies remain the most widely used of such reagents and many show excellent performance, although some are poorly characterised or have stability or batch variability issues, supporting the use of alternative binding proteins as complementary reagents for many applications. Here we report on the use of Affimer proteins as research reagents. We selected 12 diverse molecular targets for Affimer selection to exemplify their use in common molecular and cellular applications including the (a) selection against various target molecules; (b) modulation of protein function in vitro and in vivo; (c) labelling of tumour antigens in mouse models; and (d) use in affinity fluorescence and super-resolution microscopy. This work shows that Affimer proteins, as is the case for other alternative binding scaffolds, represent complementary affinity reagents to antibodies for various molecular and cell biology applications.

UR - http://europepmc.org/abstract/med/28654419

U2 - 10.7554/elife.24903

DO - 10.7554/elife.24903

M3 - Article

C2 - 28654419

SN - 2050-084X

VL - 6

JO - eLife

JF - eLife

M1 - e24903

ER -

Affimer proteins are versatile and renewable affinity reagents.

Abstract

Bibliographical note

UN SDGs

Access to Document

Other files and links

Fingerprint

Cite this