Abstract: The present invention refers to an isolated truncated Nogo-A polypeptide that corresponds to a truncated form of the Nogo-A protein consisting of the amino acids 174 to 940 of the full length protein of rat Nogo-A or of the amino acids 246 to 966 of the human full length Nogo-A protein.

Abstract: A method for generating a mutein of human apolipoprotein D having detectable affinity to a given non-natural ligand of apolipoprotein D is disclosed, which comprises the steps of: (a) subjecting the apolipoprotein D to mutagenesis at the sequence positions 34 to 38, 60, 62 to 66, 68, 89 to 93, 115, 117 to 121, and 123 resulting in a plurality of muteins of apolipoprotein D; and (b) enriching resulting muteins having binding affinity for a given ligand from the plurality of muteins by selection, and/or isolating said mutein. Muteins of apolipoprotein D obtainable by this method are also disclosed.

Abstract: The present invention relates to muteins of the bilin-binding protein with binding activity to digoxigenin and to fusion proteins of such muteins, a method for preparing said muteins and fusion proteins thereof and their utilization for detecting or binding digoxigenin-labeled biomolecules. The invention especially relates to a polypeptide selected from muteins of the bilin-binding protein, characterized in that (a) it can bind digoxigenin or digoxigenin conjugates, (b) it does not bind ouabain, testosterone, and 4-aminofluorescein and (c) at least one of the sequence positions 28, 31, 34, 35, 36, 37, 58, 60, 69, 88, 90, 95, 97, 114, 116, 125, and 127 of the bilin-binding protein has an amino acid substitution. Due to their simple molecular structure, the inventive muteins provide advantages for production and utilization in comparison with antibodies against the digoxigenin group.