Construction and high cytoplasmic expression of a tumoricidal single-chain antibody against hepatocellular carcinoma
Background
Hep27 monoclonal (Hep27 Mab) is an antibody against hepatocellular carcinoma. Hep27 Mab itself can inhibit the growth of a hepatocellular carcinoma cell line (HCC-S102). We attempted to produce a single-chain fragment (scFv), a small fragment containing an antigen-binding site of Hep27 Mab, by using DNA-recombinant techniques.
Results
The sequences encoding the variable regions of heavy (VH) and light (VL) chains of a murine Hep27 Mab were linked together by a linker peptide (Gly4Ser)3 and tagged with a hexa-histidine at the C-terminal; the resultant DNA construct was expressed in E. coli as an insoluble protein. The denatured scFv was refolded and purified by immobilized metal ion affinity chromatography (12 mg/l with a molecular weight of 27 kDa). Hep27scFv exhibited a tumoricidal activity against the HCC-S102 cell as its parental antibody (Hep27 Mab).
Conclusion
This scFv may be a potential candidate for a targeting agent in HCC immunodiagnosis or immunotherapy.
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Complete Metadata
| @type | dcat:Dataset |
|---|---|
| accessLevel | public |
| bureauCode |
[ "009:25" ] |
| contactPoint |
{ "fn": "NIH", "@type": "vcard:Contact", "hasEmail": "mailto:info@nih.gov" } |
| description | Background Hep27 monoclonal (Hep27 Mab) is an antibody against hepatocellular carcinoma. Hep27 Mab itself can inhibit the growth of a hepatocellular carcinoma cell line (HCC-S102). We attempted to produce a single-chain fragment (scFv), a small fragment containing an antigen-binding site of Hep27 Mab, by using DNA-recombinant techniques. Results The sequences encoding the variable regions of heavy (VH) and light (VL) chains of a murine Hep27 Mab were linked together by a linker peptide (Gly4Ser)3 and tagged with a hexa-histidine at the C-terminal; the resultant DNA construct was expressed in E. coli as an insoluble protein. The denatured scFv was refolded and purified by immobilized metal ion affinity chromatography (12 mg/l with a molecular weight of 27 kDa). Hep27scFv exhibited a tumoricidal activity against the HCC-S102 cell as its parental antibody (Hep27 Mab). Conclusion This scFv may be a potential candidate for a targeting agent in HCC immunodiagnosis or immunotherapy. |
| distribution |
[ { "@type": "dcat:Distribution", "title": "Official Government Data Source", "mediaType": "text/html", "description": "Visit the original government dataset for complete information, documentation, and data access.", "downloadURL": "https://www.ncbi.nlm.nih.gov/pmc/articles/PMC128817/" } ] |
| identifier | https://healthdata.gov/api/views/w9cb-rbnq |
| issued | 2025-07-14 |
| keyword |
[ "hepatocellular-carcinoma", "immunotherapy", "nih", "single-chain-antibody", "tumor-targeting" ] |
| landingPage | https://healthdata.gov/d/w9cb-rbnq |
| modified | 2025-09-06 |
| programCode |
[ "009:033" ] |
| publisher |
{ "name": "National Institutes of Health", "@type": "org:Organization" } |
| theme |
[ "NIH" ] |
| title | Construction and high cytoplasmic expression of a tumoricidal single-chain antibody against hepatocellular carcinoma |
