<p>Spaces (indicated by dashes) denote gaps generated during alignment for optimal sequence comparison. Dark shading represents fully conserved residues, while light shading indicates conserved changes. The predicted signal peptide and transmembrane domain of human CD150 are underlined. Potential N-linked glycosylation sites are circled, four cystine residues predicted to form disulfide bonds are denoted by asterisks and three tyrosine-based switch motifs are boxed.</p
<p>Secretory and glycosylation signals are recognized in all species. Shaded amino acid residues ind...
<p>The amino acid sequences of zebrafish Blt1 and human and mouse BLT1 were aligned using MAFFT (<a ...
<p>The amino acid sequences for human GIPR and GLP-1R (<b>A</b>) and three mammalian species for eac...
<p>(A): Alignment of amino acid sequences of the candidate OBPs. (B): Alignment of amino acid sequen...
<p>Alignment of light chain (Vl) and heavy chain (Vh) variable regions of the murine V5B2 scFv (moSc...
<p><b>(A)</b> Amino acid sequences of residues 2–21 in human αS, βS and γS and mouse αS. <b>(B)</b> ...
<p>The potential functionally important sites are highlighted. The C-terminal site including the dou...
<p>Black shading indicates identical residues. Red box represents residues from mouse and rat Aβ tha...
<p>The shading of the alignment represents different degrees of conservation among sequences. The da...
<p>Amino acid sequence is separated into different domains and numbered according to the human seque...
<p>In all panels aminoacid numbering refers to the human protein. (A) Left: ribbon diagram of the ex...
<p>The mouse αDG C-terminal antigen used for antibody generation is aligned to rat, pig, human, and ...
<p>Alignment was performed using Clustalw algorithm. Amino acids are represented by the single lette...
<p>Analysis was generated using Clustal-omega. Putative signal peptide sequences predicted by Signal...
<p>Sequence alignment of the N-terminal P-selectin binding sites of human and mouse P-selectin glyco...
<p>Secretory and glycosylation signals are recognized in all species. Shaded amino acid residues ind...
<p>The amino acid sequences of zebrafish Blt1 and human and mouse BLT1 were aligned using MAFFT (<a ...
<p>The amino acid sequences for human GIPR and GLP-1R (<b>A</b>) and three mammalian species for eac...
<p>(A): Alignment of amino acid sequences of the candidate OBPs. (B): Alignment of amino acid sequen...
<p>Alignment of light chain (Vl) and heavy chain (Vh) variable regions of the murine V5B2 scFv (moSc...
<p><b>(A)</b> Amino acid sequences of residues 2–21 in human αS, βS and γS and mouse αS. <b>(B)</b> ...
<p>The potential functionally important sites are highlighted. The C-terminal site including the dou...
<p>Black shading indicates identical residues. Red box represents residues from mouse and rat Aβ tha...
<p>The shading of the alignment represents different degrees of conservation among sequences. The da...
<p>Amino acid sequence is separated into different domains and numbered according to the human seque...
<p>In all panels aminoacid numbering refers to the human protein. (A) Left: ribbon diagram of the ex...
<p>The mouse αDG C-terminal antigen used for antibody generation is aligned to rat, pig, human, and ...
<p>Alignment was performed using Clustalw algorithm. Amino acids are represented by the single lette...
<p>Analysis was generated using Clustal-omega. Putative signal peptide sequences predicted by Signal...
<p>Sequence alignment of the N-terminal P-selectin binding sites of human and mouse P-selectin glyco...
<p>Secretory and glycosylation signals are recognized in all species. Shaded amino acid residues ind...
<p>The amino acid sequences of zebrafish Blt1 and human and mouse BLT1 were aligned using MAFFT (<a ...
<p>The amino acid sequences for human GIPR and GLP-1R (<b>A</b>) and three mammalian species for eac...