School of Biotechnology
Proteomics
Achievements

  In vivo stabilization of recombinant proteins
Research groups
Summary
Human protein atlas
Mycoplasma mycoides
Antibody proteomics
Alkali stabilization
Tree genomics
Pyrosequencing
Single cell analysis
Affibodies
Biosensor (DNA)
Bioautomation
Surface display
Protein folding
In vivo stabilization
Solid phase methods
Protein G
Protein A
Affinity tags



Human serum albumin (HSA) is the most abundant protein in human serum. The circulation half-life of this stable protein is extremely long (over three weeks), a feature which has been exploited to obtain in vivo stabilization of recombinant proteins.
Using a serum albumin binding domain (ABD) derived from streptococcal protein G as fusion partner for proteins of therapeutic value, a strategy for production of engineered biotherapeutics with increased in vivo stability have been developed. The serum albumin binding activity of the ABD fusion partner results, after injection into the blood stream, in the formation of long-lived complexes with HSA.

Key (own) publications:
1.
Nygren, P.-Å., Flodby, P., Andersson, R., Wigzell, H. and Uhlén, M. [1991] “In vivo stabilization of a human recombinant CD4 derivative by fusion to a serum-albumin-binding receptor” Vaccines 91, Cold Spring Harbor Laboratory. 363-368.
2.
Makrides, S., Nygren, P.-Å., Andrews, B., Ford, P., Evans, K.S., Hayman, E.G., Adari, H., Levin, J., Uhlén, M. and Toth, C.A. (1996) "Extended in vivo half-life of human soluble complement receptor type I fused to serum albumin-binding receptor" J. Pharm. Exp. Therap. 277, 534-541.
Last updated: 2010-12-22