||Recombinant B.subitilis CopA Domain A+B (Copper-transporting P-type ATPase copA, CopA protein) cloned from B.subitilis cDNA with a C-terminal purification tag was expressed inE.coli. It consists of the soluble domain A+B of CopA from B.subtilis (residues 1-147, swissprot accession O32220). The C-terminal tag is cleaved during purification. The protein is mutated in the S46V position. MW = 16.3 kDa.
||95% by SDS-PAGE.The protein was observed as a single band migrating at a molecular weight of <10 kDa.
||1.0mg/ml in 20mM potassium phosphate buffer pH7.0, DTT 2mM (Dithiothreitol). The concentration is calculated from the absorbance at 280nm (e280 = 2680 M-1 cm-1).
||Under the above described conditions, to avoid precipitation or protein dimerization, the product can be concentrated to a maximum of 2mM.
||-20ºC. The protein is stable at 4ºC for at least 2 weeks 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.