Zobrazeno 1 - 10
of 17
pro vyhledávání: '"David Paul Humphreys"'
Publikováno v:
BioTechniques, Vol 66, Iss 4, Pp 171-178 (2019)
Fractionation in Gram-negative bacteria is used to identify the subcellular localization of proteins, in particular the localization of exported recombinant proteins. The process of cell fractionation can be fraught with cross-contamination issues an
Externí odkaz:
https://doaj.org/article/172f1e98938c49359f826783c5a43cbe
Publikováno v:
BioTechniques. 66:171-178
Fractionation in Gram-negative bacteria is used to identify the subcellular localization of proteins, in particular the localization of exported recombinant proteins. The process of cell fractionation can be fraught with cross-contamination issues an
Autor:
Alastair D. G. Lawson, Ralph Adams, Joanne E. Compson, Tim Kopotsha, Michael Airey, Hanna Hailu, David Paul Humphreys, Oliver Zaccheo, Kaushik Sarkar, Mark Jairaj, Wild Gavin Barry, Andrew M. Ventom, Sarah L. Dugdale, Louis Christodoulou, Emma Dave, Sarah Malcolm, Diane Marshall, Alison Turner, Bruce Carrington, James T. Heads, Miren Zamacona, Sam Philip Heywood
Publikováno v:
mAbs
An antibody format, termed Fab-dsFv, has been designed for clinical indications that require monovalent target binding in the absence of direct Fc receptor (FcR) binding while retaining substantial serum presence. The variable fragment (Fv) domain of
Autor:
Mark Jairaj, Emma Dave, Ralph Adams, Shauna West, Laura Griffin, Oliver Zaccheo, Sam Philip Heywood, David Paul Humphreys, Tom Ceska, Joanne E. Compson, Alastair Dg. Lawson, Terry Baker
Publikováno v:
mAbs
We generated an anti-albumin antibody, CA645, to link its Fv domain to an antigen-binding fragment (Fab), thereby extending the serum half-life of the Fab. CA645 was demonstrated to bind human, cynomolgus, and mouse serum albumin with similar affinit
Autor:
Sarah E Lane, Leigh C Bowering, Sam Philip Heywood, David Paul Humphreys, Lloyd M. King, James P Turner
Publikováno v:
Protein Expression and Purification. 37:109-118
Escherichia coli is a widely used host for the heterologous expression of proteins of therapeutic and commercial interest. The scale and speed at which it can be cultured can result in the rapid generation of large quantities of product. However, to
Autor:
Lloyd M. King, Mukesh Sehdev, Alastair D. G. Lawson, Dominic G. Reeks, David Paul Humphreys, Leigh C Bowering, Ravindra Ganesh, Bryan J. Smith, Bruce Carrington, Andrew George Popplewell
Publikováno v:
Protein Expression and Purification. 26:309-320
We demonstrate the importance of optimizing the balance of light chain (LC) and heavy chain (HC) expression to achieve high level production of Fab' fragments in the Escherichia coli periplasm. The LC:HC balance has been controlled by varying the cod
Publikováno v:
FEMS Microbiology Letters. 174:179-184
The Dsb proteins are involved in disulfide bond formation, reduction and isomerisation in a number of Gram-negative bacteria. Mutations in dsbA or dsbB, but not dsbC, increase the proportion of proteins with free thiols in the periplasm compared to w
Autor:
Eve E. Weatherill, James T. Heads, Ralph Adams, Katharine Cain, Joanne E. Compson, David Paul Humphreys, Sam Philip Heywood
Publikováno v:
Protein engineering, designselection : PEDS. 25(7)
Engineered introduction of interface interchain disulphide bonds is perceived to be a simple method to increase the stability of single chain Fv (scFv). Six disulphide bond locations have been cited within the literature but the potential for the bro
Autor:
Leigh C Bowering, David Paul Humphreys
Publikováno v:
Therapeutic Monoclonal Antibodies
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ab780c90e7641acdc161e4119f3f4022
https://doi.org/10.1002/9780470485408.ch27
https://doi.org/10.1002/9780470485408.ch27