The University of Southampton
University of Southampton Institutional Repository

Expression and secretion of T‐Cell receptor Vα and Vβ domains using Escherichia coli as a host

Expression and secretion of T‐Cell receptor Vα and Vβ domains using Escherichia coli as a host
Expression and secretion of T‐Cell receptor Vα and Vβ domains using Escherichia coli as a host

An expression system for the production of recombinant T‐cell receptor (TCR) variable domains would, inter alia, allow structural studies lo be carried out and provide protein for the generation of anti‐clonotypic antibodies, in this report the Vα and Vβ domain genes have been isolated from a T‐cell hybridoma which is associated with the pathogenesis of experimental allergic encephalomyelitis (EAE) In the H‐2 mouse. These have been expressed as secreted domains in Escherichia coli, using secretion vectors previously used for the production of immunoglobulin fragments. Both Vα and Vβ domains are secreted in milligram quantities into the culture supernatant, although the levels of the Vα domain are about 10‐20 Ibid higher than those of the Vβ domain. This expression system offers a rapid route for the production of recombinant TCRs in soluble form.

0300-9475
215-220
Ward, E. S.
b31c0877-8abe-485f-b800-244a9d3cd6cc
Ward, E. S.
b31c0877-8abe-485f-b800-244a9d3cd6cc

Ward, E. S. (1991) Expression and secretion of T‐Cell receptor Vα and Vβ domains using Escherichia coli as a host. Scandinavian Journal of Immunology, 34 (2), 215-220. (doi:10.1111/j.1365-3083.1991.tb01539.x).

Record type: Article

Abstract

An expression system for the production of recombinant T‐cell receptor (TCR) variable domains would, inter alia, allow structural studies lo be carried out and provide protein for the generation of anti‐clonotypic antibodies, in this report the Vα and Vβ domain genes have been isolated from a T‐cell hybridoma which is associated with the pathogenesis of experimental allergic encephalomyelitis (EAE) In the H‐2 mouse. These have been expressed as secreted domains in Escherichia coli, using secretion vectors previously used for the production of immunoglobulin fragments. Both Vα and Vβ domains are secreted in milligram quantities into the culture supernatant, although the levels of the Vα domain are about 10‐20 Ibid higher than those of the Vβ domain. This expression system offers a rapid route for the production of recombinant TCRs in soluble form.

This record has no associated files available for download.

More information

Published date: August 1991

Identifiers

Local EPrints ID: 425256
URI: http://eprints.soton.ac.uk/id/eprint/425256
ISSN: 0300-9475
PURE UUID: 64f6aef3-9b31-4225-8fd8-0db4f32e1bc7
ORCID for E. S. Ward: ORCID iD orcid.org/0000-0003-3232-7238

Catalogue record

Date deposited: 12 Oct 2018 16:30
Last modified: 16 Mar 2024 04:37

Export record

Altmetrics

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×