MUC1 mucin is a large complex glycoprotein expressed on normal epithelial cells in humans and overexpressed and under or aberrantly glycosylated on many malignant cancer cells which consequently allows recognition of the protein core by antibodies. In order to understand how glycosylation may modula
Primary structure of the variable regions of a monoclonal antibody MUSE11 recognizing the tandem repeat domain of a mucin core protein, MUC1
โ Scribed by Dr. Yuji Hinoda; Yoshiaki Arimura; Fumio Itoh; Masaaki Adachi; Masayuki Tsujisaki; Kohzoh Imai; Akira Yachi
- Book ID
- 102307790
- Publisher
- John Wiley and Sons
- Year
- 1993
- Tongue
- English
- Weight
- 438 KB
- Volume
- 7
- Category
- Article
- ISSN
- 0887-8013
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โฆ Synopsis
A monoclonal antibody (MAb) MUSE1 1 recognizes an epitope in the tandem repeat domain of a mucin core protein, MUCl. We show that the epitope of MAb MUSEl 1 could be within the continuous amino acid sequence PDTRPAPG. Since there is increasing evidence indicating that this region is highly immunogenic, cDNA cloning of the variable regions of heavy-chain (VH) and of lightchain (VL) of MAb MUSEl 1 was performed by using RT-PCR to provide a basis for analyzing the structure of the antibody-antigen complex and for producing anti-idiotypic antibodies. The deduced amino acid sequence revealed that the VH and VK of MAb MUSE1 1 could be assigned to subgroups IllA and II of mouse immunoglobulin heavy and light chains, respectively. When compared with the V regions of other MAbs in the same subgroup, the complementary determining region 3 (CDR3) in the VH region of MAb MUSEl 1 consisted of a unique sequence that may be important in defining the specificity of MAb MUSE1 1.
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