Hober S - Search Results

1

Antibody performance in western blot applications is context-dependent.

Algenäs C, Agaton C, Fagerberg L, Asplund A, Björling L, Björling E, Kampf C, Lundberg E, Nilsson P, Persson A, Wester K, Pontén F, Wernérus H, Uhlén M, Ottosson Takanen J, Hober S. Algenäs C, et al. Among authors: hober s. Biotechnol J. 2014 Mar;9(3):435-45. doi: 10.1002/biot.201300341. Epub 2014 Jan 29. Biotechnol J. 2014. PMID: 24403002

2

Expression and characterization of a tripartite fusion protein consisting of chimeric IgG-binding receptors and beta-galactosidase.

Strandberg L, Hober S, Uhlén M, Enfors SO. Strandberg L, et al. Among authors: hober s. J Biotechnol. 1990 Jan;13(1):83-96. doi: 10.1016/0168-1656(90)90133-v. J Biotechnol. 1990. PMID: 1368543

3

Folding of insulin-like growth factor I is thermodynamically controlled by insulin-like growth factor binding protein.

Hober S, Hansson A, Uhlén M, Nilsson B. Hober S, et al. Biochemistry. 1994 Jun 7;33(22):6758-61. doi: 10.1021/bi00188a003. Biochemistry. 1994. PMID: 7515683

4

Disulfide exchange folding of disulfide mutants of insulin-like growth factor I in vitro.

Hober S, Uhlén M, Nilsson B. Hober S, et al. Biochemistry. 1997 Apr 15;36(15):4616-22. doi: 10.1021/bi9611265. Biochemistry. 1997. PMID: 9109671

5

Insulin-like growth factors I and II are unable to form and maintain their native disulfides under in vivo redox conditions.

Hober S, Lundström Ljung J, Uhlén M, Nilsson B. Hober S, et al. FEBS Lett. 1999 Jan 29;443(3):271-6. doi: 10.1016/s0014-5793(98)01737-2. FEBS Lett. 1999. PMID: 10025946 Free article.

Insulin-like growth factor (IGF) I does not quantitatively form its three native disulfide bonds in the presence of 10 mM reduced and 1 mM oxidized glutathione in vitro [Hober, S. et al. (1992) Biochemistry 31, 1749-1756]. In this paper, we show (i) that both IGF-I …

Insulin-like growth factor (IGF) I does not quantitatively form its three native disulfide bonds in the presence of 10 mM reduced and 1 mM o …

6

Protein engineering of an IgG-binding domain allows milder elution conditions during affinity chromatography.

Gülich S, Uhlén M, Hober S. Gülich S, et al. Among authors: hober s. J Biotechnol. 2000 Jan 21;76(2-3):233-44. doi: 10.1016/s0168-1656(99)00197-2. J Biotechnol. 2000. PMID: 10656338

7

Stability towards alkaline conditions can be engineered into a protein ligand.

Gülich S, Linhult M, Nygren P, Uhlén M, Hober S. Gülich S, et al. Among authors: hober s. J Biotechnol. 2000 Jun 23;80(2):169-78. doi: 10.1016/s0168-1656(00)00259-5. J Biotechnol. 2000. PMID: 10908797

8

Charge engineering of a protein domain to allow efficient ion-exchange recovery.

Gräslund T, Lundin G, Uhlén M, Nygren PA, Hober S. Gräslund T, et al. Among authors: hober s. Protein Eng. 2000 Oct;13(10):703-9. doi: 10.1093/protein/13.10.703. Protein Eng. 2000. PMID: 11112509

9

Overexpression, rapid isolation, and biochemical characterization of Escherichia coli single-stranded DNA-binding protein.

Ehn M, Nilsson P, Uhlén M, Hober S. Ehn M, et al. Among authors: hober s. Protein Expr Purif. 2001 Jun;22(1):120-7. doi: 10.1006/prep.2001.1426. Protein Expr Purif. 2001. PMID: 11388809

10

Mutational analysis of the interaction between albumin-binding domain from streptococcal protein G and human serum albumin.

Linhult M, Binz HK, Uhlén M, Hober S. Linhult M, et al. Among authors: hober s. Protein Sci. 2002 Feb;11(2):206-13. doi: 10.1110/ps.02802. Protein Sci. 2002. PMID: 11790830 Free PMC article.

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