Abstract
A PROTEIN ligand for the ECK1 receptor protein-tyrosine kinase has been isolated by using the extracellular domain (ECK-X) of the receptor as an affinity reagent. Initially, concentrated cell culture supernatants were screened for receptor binding activity using immobilized ECK-X in a surface plasmon resonance detection system2,3. Subsequently, supernatants from selected cell lines were fractionated directly by receptor affinity chromatography, resulting in the single-step purification of B61, a protein previously identified as the product of an early response gene induced by tumour necrosis factor-α4. We report here that recombinant B61 induces autophosphorylation of ECK in intact cells, consistent with B61 being an authentic ligand for ECK. ECK is a member of a large orphan receptor protein-tyrosine kinase family headed by EPH5, and we suggest that ligands for other members of this family will be related to B61, and can be isolated in the same way.
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Bartley, T., Hunt, R., Welcher, A. et al. B61 is a ligand for the ECK receptor protein-tyrosine kinase. Nature 368, 558–560 (1994). https://doi.org/10.1038/368558a0
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DOI: https://doi.org/10.1038/368558a0
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