Identification of the immunoreactive peptide sequence for AgSK1, an adenocarcinoma-restricted antigen
| Autor: | C. Gaskins, S. Mukerjee, M. C. Glassy, P.C. Chau, Keiji Koda, J. Yasutomi, M. E. Mcknight, Norio Saito, M. Nasoff, Nobuyuki Nakajima |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
chemistry.chemical_classification
medicine.drug_class Immunology General Medicine Biology Monoclonal antibody Biochemistry Virology Molecular biology Epitope Amino acid Open reading frame chemistry Antigen Complementary DNA Genetics medicine Immunology and Allergy Clone (B-cell biology) Peptide sequence |
| Zdroj: | Tissue Antigens. 55:157-161 |
| ISSN: | 0001-2815 |
| DOI: | 10.1034/j.1399-0039.2000.550208.x |
| Popis: | Acknowledgments: We would like to thank Jose Galindo and David Larocca for help during the initial phases of this work and to Minyi Gu, Soujan Wang and Janessa Molinari for expert technical assistance. Abstract: SK1, a human immunoglobulin M (IgM) monoclonal antibody was derived from regional nodal lymphocytes of a Dukes B colon carcinoma patient. The antigen recognized by the human monoclonal antibody (HuMab) SK1, termed AgSK1, was shown to be a two-chain glycoprotein with an apparent molecular weight range of 42–46 kDa and preferentially expressed by human adenocarcinomas, particularly human gastrointestinal malignancies. To identify the gene encoding the AgSK1 antigenic epitope, a cDNA expression library constructed in λgt22A using mRNA from the colon carcinoma cell line HT29 was screened and one of the isolated clones encoding a 1.5-kb cDNA, which showed strong immunoreactivity with HuMab SK1, was selected for further analysis. This clone consisted of an amino terminal open reading frame of 54 amino acids and the carboxyl terminal 20 amino acids of this protein coding region contained the antigenic epitope recognized by HuMab SK1. |
| Databáze: | OpenAIRE |
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