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CD19, the earliest differentiation antigen of the B cell lineage, bears three extracellular immunoglobulin-like domains and an Epstein-Barr virus-related cytoplasmic tail
The isolation and expression of a full-length cDNA clone encoding the B cell-specific glycoprotein CD19 is reported. The sequence of the cDNA predicts a glycosylated integral membrane protein with a precursor molecular weight of 51.8 x 10(3) and an extracellular domain organized into three contiguou...
Formato: | Texto |
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Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1988
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2189043/ https://www.ncbi.nlm.nih.gov/pubmed/2459292 |
Sumario: | The isolation and expression of a full-length cDNA clone encoding the B cell-specific glycoprotein CD19 is reported. The sequence of the cDNA predicts a glycosylated integral membrane protein with a precursor molecular weight of 51.8 x 10(3) and an extracellular domain organized into three contiguous Ig-like sub-domains. The cytoplasmic domain bears significant relatedness to two proteins encoded by the Epstein-Barr virus and the int-1 oncogene. CD19 transcripts are restricted to members of the B cell lineage, being most abundant in pre-B cell lines and least abundant in plasmacytomas. |
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