||Recombinant Human Catalytic Domain PP5 (Serine/Threonine-Protein Phospatase) cloned from human cDNA with a N-terminal purification tag was expressed inE. coli. It consists of the catalytic domain of PP5 (residues 169-499, Accession number:P53041). The N-terminal tag is cleaved during purification, leaving GSFT residues. MW = 38.1 KDa.
||Serine/threonine-protein phosphatase 5 is an enzyme that in humans is encoded by the PPP5C gene. PPP5C has been shown to interact with ASK1, CRY2and GNA12.
||> 95% by SDS-PAGE. The protein was observed as a single band migrating at amolecular weight of 38KDa.
||1 mg/mlin 50mM Tris-HCl pH 7.5, 150mM NaCl, 1mM DTT (dithiothreitol). The concentration is calculated from the absorbance at 280nm (e280= 37735 M-1 cm-1).
||Under the above described conditions, to avoid precipitation, the product can be concentrated to a maximum of 1mM.
||-20ºC. The protein is stable at 4ºC for at least 2 weeks and at 25ºC for at least several days. After initial defrost, aliquot product into individual tubes and refreeze at -20ºC. Avoid repeated freeze/defrost cycles.