| Literature DB >> 7689836 |
C R Norton1, J M Rumberger, D K Burns, B A Wolitzky.
Abstract
A recombinant phage containing the structural exons for mouse E-selectin has been isolated and characterized. Utilizing PCR techniques the lectin and egf domains were fused to form an artificial cDNA for expression in eukaryotic cells. Transient expression in COS cells demonstrated the lectin and egf domains were sufficient to mediate the binding of mouse and human neutrophils as well as HL60 cells. Recombinant soluble mouse E-selectin was purified and used to immunize rats to generate mAbs specific to mouse E-selectin. A panel of mAbs directed against mouse E-selectin was characterized including five that inhibit the adhesion of HL60 cells or mouse neutrophils to COS cells expressing the mouse lectin/egf domains. These mAbs have been used to characterize the expression and function of E-selectin on cytokine stimulated eEnd.2 murine endothelial cells.Entities:
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Year: 1993 PMID: 7689836 DOI: 10.1006/bbrc.1993.2037
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575