The monoclonal antibodies and the recombinant antibody fragments are widely used in the biotechnology studies and in medicine as a powerful therapeutic and diagnostic tool. The most commonly used recombinant antibody fragments are single-chain fragment variable (scFv) because of their small size and minimal immunogenicity while still retaining high-affinity antigen binding. A wide range of expression systems such as bacterial and eukaryotic cell systems enable the sufficient production of scFv antibodies. However, their stable expression in soluble form and correct protein folding are often insufficient. In the present study, we present the autoinduction as a key element of the optimized scheme for heterologous expression of human monoclonal scFv antibodies (clones A1 and A12) in Escherichia coli HB2151, which resulted in two-fold increase of the total protein yield in 24 h.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1007/s12033-021-00363-2 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
A Granzyme B-Cleavable T Cell-Targeted Bispecific Cell Vesicle Connector for Reversing New-Onset Type 1 Diabetes.
J Am Chem Soc
January 2025
State Key Laboratory of Advanced Drug Delivery and Release Systems, College of Pharmaceutical Sciences, Zhejiang University, Hangzhou 310058, China.
Type 1 diabetes (T1D) is an autoimmune disorder in which pancreatic β-cells are destroyed by CD8 T cells. Anti-CD3 antibody effectively treats early-stage T1D when β-cell autoantibodies are detected but before symptoms appear. However, it impairs the immune system temporarily, exposing individuals to infection.
View Article and Find Full Text PDFDrug discovery continues to face a staggering 90% failure rate, with many setbacks occurring during late-stage clinical trials. To address this challenge, there is an increasing focus on developing and evaluating new technologies to enhance the "design" and "test" phases of antibody-based drugs (e.g.
View Article and Find Full Text PDFPhage Display-Mediated Immuno-Multiplex Quantitative PCR for the Simultaneous Quantification of IFN-γ and IL-6.
ACS Omega
January 2025
School of Life Sciences, Beijing University of Chinese Medicine, Beijing 102488, China.
In phage display technology, exogenous DNA is inserted into the phage genome, which generates a fusion protein with the phage coat protein, facilitates expression and promotes biological activity. This approach is primarily used to screen antibody libraries owing to its high library capacity and fast technical cycle; additionally, various types of genetically altered antibodies can be easily produced. In this study, we fused the pIII structural protein of the M13K07 phage with a scFv created by connecting the VH and VL domains of an anti-IFN-γ antibody.
View Article and Find Full Text PDFCrystal Structures of Antigen-Binding Fragment of Anti-Osteocalcin Antibody KTM219.
Int J Mol Sci
January 2025
Department of Applied Biology, Faculty of Textile Science and Technology, Shinshu University, Ueda 386-8567, Nagano, Japan.
Osteocalcin is a useful biomarker for bone formation and bone-related diseases. KTM219 is an anti-osteocalcin C-terminal peptide antibody. The single-chain variable region (scFv) and antigen-binding fragment (Fab) of KTM219 are applicable to the Quenchbody (Q-body) immunoassay.
View Article and Find Full Text PDFA New Antibody-Cytokine Construct Targeting Natural Killer Cells: An Immunotherapeutic Approach to Chronic Lymphocytic Leukemia.
Biomolecules
January 2025
National Center for Global Health, Italian Institute of Health, 00161 Rome, Italy.
In chronic lymphocytic leukemia (CLL), natural killer (NK) cells show a dysfunctional phenotype that correlates with disease progression. Our aim was to restore NK cell functionality in CLL through a specifically targeted IL15-stimulating activity; IL15 targeting could, in fact, potentiate the activity of NK cells and reduce off-target effects. We designed and developed a cis-acting immunocytokine composed of an anti-CD56 single-chain Fragment variable (scFv) and IL15, labeled scFvB1IL15.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!