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- W2031143873 abstract "We have characterized the IgG form of a previously isolated and engineered single-chain Fv (scFv), named RR2r3s4-1, that binds to human PSGL-1. This fully human IgG was determined to have a Kd of 1.8 ± 0.7 nM by fluorescence quenching titration. It better inhibits P-selectin–PSGL-1 interactions than a commercially available murine monoclonal antibody KPL1 and better inhibits neutrophil rolling than KPL1. Thus, RR2r3s4-1 is the most effective antibody at inhibiting P-selectin–PSGL-1 interactions known. Specificity analysis reveals that RR2r3s4-1 does not cross react with murine PSGL-1 and thus requires more than tyrosine sulfate for binding to human PSGL-1. This evidence demonstrates the therapeutic potential of this antibody as a potent anti-inflammatory therapeutic." @default.
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- W2031143873 date "2006-11-01" @default.
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- W2031143873 title "A high affinity human antibody antagonist of P-selectin mediated rolling" @default.
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- W2031143873 doi "https://doi.org/10.1016/j.bbrc.2006.08.197" @default.
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