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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...

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Detalles Bibliográficos
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1988
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2189043/
https://www.ncbi.nlm.nih.gov/pubmed/2459292
Descripción
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.