Fig. 2.
Fig. 2. Organization of human Emp cDNA. (A) The restriction map was obtained from two overlapping clones isolated from a human U937 λgt11 cDNA library. The central block (nucleotides 45-1229) represents the coding region. Both strands were sequenced, and arrows indicate the sequencing strategy. (B) Hydrophilicity plot of the deduced amino acid sequence of Emp. Positive values indicate hydrophilicity, whereas negative values indicate hydrophobicity. AA, amino acids. (C) Immunochemical identification of the Emp sequence. Macrophage membrane proteins were separated by 18% SDS-PAGE, transferred to NC membrane, and probed with affinity purified anti-p1 antibodies (lane 1) or affinity-purified antibodies against native Emp (lane 2). Anti-p1 was raised against the synthetic peptide corresponding to residues 15-26. The position of the molecular weight standards (same as those used in Fig 1) is shown on the left.

Organization of human Emp cDNA. (A) The restriction map was obtained from two overlapping clones isolated from a human U937 λgt11 cDNA library. The central block (nucleotides 45-1229) represents the coding region. Both strands were sequenced, and arrows indicate the sequencing strategy. (B) Hydrophilicity plot of the deduced amino acid sequence of Emp. Positive values indicate hydrophilicity, whereas negative values indicate hydrophobicity. AA, amino acids. (C) Immunochemical identification of the Emp sequence. Macrophage membrane proteins were separated by 18% SDS-PAGE, transferred to NC membrane, and probed with affinity purified anti-p1 antibodies (lane 1) or affinity-purified antibodies against native Emp (lane 2). Anti-p1 was raised against the synthetic peptide corresponding to residues 15-26. The position of the molecular weight standards (same as those used in Fig 1) is shown on the left.

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