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Human anti-EGFL7 recombinant full-length antibodies selected from a mammalian cell-based antibody display library.
- Source :
-
Molecular and cellular biochemistry [Mol Cell Biochem] 2012 Jun; Vol. 365 (1-2), pp. 77-84. - Publication Year :
- 2012
-
Abstract
- Epidermal growth factor-like domain 7 (EGFL7) has been implicated in promoting solid tumor growth and metastasis via stimulating tumor-associated angiogenesis. The advent of antibody display technology (phage, bacteria, and yeast) led to an enormous revival in the use of antibodies as diagnostic and therapeutic tools for fighting cancer. However, problems with protein folding, posttranslational modification, and codon usage still limit the number of improved antibodies that can be obtained. We describe here the isolation of an EGFL7-specific antibody from a mammalian cell-based full-length antibody display library generated from peripheral blood mononuclear cells of patients with hepatocellular carcinoma. Using a novel vector, contained glycosylphosphatidylinositol anchor and restriction enzyme sites NheI and ClaI, antibody libraries are displayed as whole IgG molecules on the cell surface and screened for specific antigen binding by a combination of magnetic beads and measured by cell ELISA. Anti-EGFL7 antibody was successfully isolated from the library. The mammalian cell-based full-length antibody display library is a great potential application for rapid identification and cloning of human mAbs of targeting hepatocellular carcinoma.
- Subjects :
- Amino Acid Sequence
Calcium-Binding Proteins
Carcinoma, Hepatocellular immunology
Cloning, Molecular
EGF Family of Proteins
Escherichia coli
Gene Library
HEK293 Cells
Humans
Immunoglobulin G genetics
Immunoglobulin G isolation & purification
Immunoglobulin Variable Region genetics
Immunoglobulin Variable Region isolation & purification
Liver Neoplasms immunology
Lymphocytes immunology
Molecular Sequence Data
Recombinant Fusion Proteins genetics
Recombinant Fusion Proteins isolation & purification
Sequence Analysis, DNA
Sequence Homology, Amino Acid
Endothelial Growth Factors immunology
Immunoglobulin G biosynthesis
Immunoglobulin Variable Region biosynthesis
Peptide Library
Recombinant Fusion Proteins biosynthesis
Subjects
Details
- Language :
- English
- ISSN :
- 1573-4919
- Volume :
- 365
- Issue :
- 1-2
- Database :
- MEDLINE
- Journal :
- Molecular and cellular biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 22297616
- Full Text :
- https://doi.org/10.1007/s11010-012-1245-7