||Recombinant humanPTPN9 is expressed in E. coli; it contains the catalytic domain of PTPN9(residues 285-593) and has a molecular weight of 34.3 kDa.
||PTPN9 (proteintyrosine phosphatase from megakaryocyte-2) was originally cloned from humanMEG-01 megakaryocyte and umbilical vein endothelial cell cDNA. The catalyticdomain is located at the carboxy-terminus of the full-length protein and ithas 30-40% sequence identity to other known protein tyrosine phosphatases.The full-length enzyme has been reported to bind phospholipid with highaffinity and that this binding is important for MEG2 activity on secretoryvesicles.
||25 mM Tris-HCl (pH8.0), 75 mM NaCl, 0.05% Tween-20, 2 mM EDTA, 1 mM DTT and 50% glycerol.Liquid at -20°C.
||Greater than 95% asdetermined by Coomassie-stained SDS-PAGE gel.
||3.5 U/μg. One unitwill hydrolyze 1 nmol of p-nitrophenyl phosphate per minute at pH 7.4 and30°C. Assay buffer: 50 mM HEPES (pH 7.4), 2 mM EDTA, 3 mM DTT, 100 mM NaCland 50 mM pNPP.
||Removal ofphosphates from target substrates. Useful for the study of enzyme kinetics,regulation and for inhibitors screening.
||6 months at -20°C.