Overexpression of DsbC and DsbG markedly improves soluble and functional expression of single-chain Fv antibodies in Escherichia coli.
- Zhong Zhang, Zhi-hua Li, Hua-liang Huang
- BiologyProtein Expression and Purification
- 1 November 2002
Production of soluble and functional engineered antibodies in Escherichia coli improved by FkpA.
- Zhong Zhang, Li-ping Song, Hua-liang Huang
- BiologyBioTechniques
- 1 November 2003
It is reported that fusion or co-expression of FkpA, the E. coli periplasmic peptidyl-prolyl-isomerase with chaperone activity, substantially improves soluble and functional expression of scAbs.
Targeting TNF-α with a tetravalent mini-antibody TNF-TeAb
- Mengyuan Liu, Xiang-bin Wang, Hua-liang Huang
- Biology
- 1 September 2007
It is shown that multimerization of the antibody fragment by a self-association peptide is an efficient way to increase its avidity and that TNF-TeAb has potential applicability for anti-TNF-α therapy.
Targeting TNF-alpha with a tetravalent mini-antibody TNF-TeAb.
- Mengyuan Liu, Xiang-bin Wang, Hua-liang Huang
- BiologyBiochemical Journal
- 2007
It is shown that multimerization of the antibody fragment by a self-association peptide is an efficient way to increase its avidity and that TNF-TeAb has potential applicability for anti-TNF-alpha therapy.
Construction of a fully synthetic human scFv antibody library with CDR3 regions randomized by a split-mix-split method and its application.
- Chang-cheng Yin, Lifen Ren, Xichong Yan
- BiologyJournal of Biochemistry (Tokyo)
- 1 November 2008
The results proved the feasibility of the split-mix-split DNA randomization strategy in library construction and site-directed mutagenesis and the utility was demonstrated by screening of scFv clones against BHL.
One‐step on‐column purification and refolding of a single‐chain variable fragment (scFv) antibody against tumour necrosis factor α
- Mengyuan Liu, Xiang-bin Wang, Hua-liang Huang
- BiologyBiotechnology and applied biochemistry
- 1 March 2006
Activity assays showed that refolded TNF‐scFv could bind to rhTNFα (recombinant human TNFα) specifically with high affinity and could inhibit rhT NFα from binding to TNF receptors and neutralize the cytolytic activity of rhTNIα against L929 cells effectively.
A novel bivalent single‐chain variable fragment (scFV) inhibits the action of tumour necrosis factor α
- Mengyuan Liu, Xiang-bin Wang, Hua-liang Huang
- BiologyBiotechnology and applied biochemistry
- 1 August 2008
A bivalent scFv (single‐chain variable fragment) fragment, named TNF‐BAb, was engineered by fusing two anti‐TNFα scFV fragments in tandem via a long and flexible linking peptide derived from human serum albumin and produced in functional form from Escherichia coli inclusion bodies to demonstrate the ability to inhibit the biological action of TNFα.
CONSTRUCTION AND EXPRESSION OF A RESHAPED VH DOMAIN AGAINST HUMAN CD28 MOLECULES
- Julong Cheng, Xiang-bin Wang, Zhong Zhang, Hua-liang Huang
- BiologyPreparative Biochemistry & Biotechnology
- 10 January 2002
Two most homologous sequences of human antibodies were pulled out from Genbank and one of them was used as the main template for the framework regions of the reshaped VH domain, which retained a high antigen binding affinity after being expressed in E. coli BL21 (DE3).
Characterization of an anti-human ovarian carcinomaxanti-human CD3 bispecific single-chain antibody with an albumin-original interlinker.
- M. Fang, Rui Zhao, Hua-liang Huang
- Biology, MedicineGynecologic Oncology
- 2004
A new model of trispecific antibody resulting the cytotoxicity directed against tumor cells.
- Li-ping Song, Julong Cheng, Hua-liang Huang
- Biology, MedicineSheng wu hua xue yu sheng wu wu li xue bao Acta…
- 1 June 2003
It was demonstrated that this new type of recombinant scFv antibody set up a new technological platform for T cells based immunotherapy against cancer, especially with the failure on MHC antigen presentation or absence of costimulating signal.
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