||Recombinant S.cervisiae Atx1 copper chaperone expressed inE.coliwas cloned from S.cerevisiae cDNA. It consists of the full length Atx1 protein, residues 1-73 (swissprot accession A6ZRI4). The protein is in the apo form. MW = 8.2 kDa,
||> 95% by SDS-PAGE. The protein was observed as a single band migrating at a molecular weight <10 kDa.
||Solution at 1 mg/ml in KH2PO4/K2HPO4 100 mM pH 7, DTT (Dithiothreitol) 1mM. The concentration is calculated from the absorbance at 280nm (e280 = 4000 M-1 cm-1).
||To avoid precipitation handle the proteinin an inert atmosphere or in presence of at least 2mM DTT. Under the above conditions the product can be concentrated to a maximum of 1.5 mM.
||-20ºC. The protein is stable at 4ºC for at least 1 week and at 25ºC for at least several hours. After initial defrost, aliquot product into individual tubes and refreeze at -20ºC. Avoid repeated freeze/defrost cycles.