FACS binding assay for analysing GDNF interactions.
Quintino, Luis LU
; Baudet, Aurelie
LU
; Larsson, Jonas
LU
and Lundberg, Cecilia
LU
(2013)
In Journal of Neuroscience Methods
218(1).
p.25-28
- Abstract
- Glial cell-line derived neurotrophic factor (GDNF) is a secreted protein with great therapeutic potential. However, in order to analyse the interactions between GDNF and its receptors, researchers have been mostly dependent of radioactive binding assays. We developed a FACS-based binding assay for GDNF as an alternative to current methods. We demonstrated that the FACS-based assay using TGW cells allowed readily detection of GDNF binding and displacement to endogenous receptors. The dissociation constant and half maximal inhibitory concentration obtained were comparable to other studies using standard binding assays. Overall, this FACS-based, simple to perform and adaptable to high throughput setup, provides a safer and reliable... (More)
- Glial cell-line derived neurotrophic factor (GDNF) is a secreted protein with great therapeutic potential. However, in order to analyse the interactions between GDNF and its receptors, researchers have been mostly dependent of radioactive binding assays. We developed a FACS-based binding assay for GDNF as an alternative to current methods. We demonstrated that the FACS-based assay using TGW cells allowed readily detection of GDNF binding and displacement to endogenous receptors. The dissociation constant and half maximal inhibitory concentration obtained were comparable to other studies using standard binding assays. Overall, this FACS-based, simple to perform and adaptable to high throughput setup, provides a safer and reliable alternative to radioactive methods. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3804530
- author
- Quintino, Luis
LU
; Baudet, Aurelie
LU
; Larsson, Jonas
LU
and Lundberg, Cecilia
LU
- organization
- publishing date
- 2013
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Neuroscience Methods
- volume
- 218
- issue
- 1
- pages
- 25 - 28
- publisher
- Elsevier
- external identifiers
-
- wos:000322692900004
- pmid:23669067
- scopus:84878743571
- pmid:23669067
- ISSN
- 1872-678X
- DOI
- 10.1016/j.jneumeth.2013.04.006
- language
- English
- LU publication?
- yes
- id
- 7267bcc9-ef3f-494d-b8fe-34125ae72c0a (old id 3804530)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/23669067?dopt=Abstract
- date added to LUP
- 2016-04-01 09:52:40
- date last changed
- 2022-02-17 04:26:54
@article{7267bcc9-ef3f-494d-b8fe-34125ae72c0a,
abstract = {{Glial cell-line derived neurotrophic factor (GDNF) is a secreted protein with great therapeutic potential. However, in order to analyse the interactions between GDNF and its receptors, researchers have been mostly dependent of radioactive binding assays. We developed a FACS-based binding assay for GDNF as an alternative to current methods. We demonstrated that the FACS-based assay using TGW cells allowed readily detection of GDNF binding and displacement to endogenous receptors. The dissociation constant and half maximal inhibitory concentration obtained were comparable to other studies using standard binding assays. Overall, this FACS-based, simple to perform and adaptable to high throughput setup, provides a safer and reliable alternative to radioactive methods.}},
author = {{Quintino, Luis and Baudet, Aurelie and Larsson, Jonas and Lundberg, Cecilia}},
issn = {{1872-678X}},
language = {{eng}},
number = {{1}},
pages = {{25--28}},
publisher = {{Elsevier}},
series = {{Journal of Neuroscience Methods}},
title = {{FACS binding assay for analysing GDNF interactions.}},
url = {{http://dx.doi.org/10.1016/j.jneumeth.2013.04.006}},
doi = {{10.1016/j.jneumeth.2013.04.006}},
volume = {{218}},
year = {{2013}},
}