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Purification and Characterization of Protein Tyrosine Phosphatase MEG1 and Preparation of Anti-PTPMEG1 Antibody

Chemical Research in Chinese Universities 2010年第4期26卷 591-595页

作者： ZHANG Xiao-ping XING Shu Xiao-xia LIN Fan FU Xue-qi LI Wan-nan Edmond H. Fischer Signal Transduction Laboratory College of Life Sciences Jilin University Changchun 130012 P. R. China Clinical Laboratory China Japan Union Hospital Jilin University Changchun 130033 P. R. China Key Laboratory for Molecular Enzymology and Engineering Ministry of Education Jilin University Changchun 130012 P. R. China School of Life Science Northeast Normal University Changchun 130024 P. R. China

PTPMEGI is an intracellular protein tyrosine phosphatase（PTP）, which contains FERM and PDZ domains This study focuses our attention on the expression, purification and characterization of catalytic domain of PTPMEG1 （ameg1） and preparation of its polyclonal antibody. A cDNA fragment encoding ameg1 protein（amino acid residues 643-926） was amplified by PCR and then cloned into the pT7-7 vector. Both soluble and insoluble recombinant ameg1 proteins were observed after induction by IPTG. Soluble ameg1 was purified via two chromatographic steps, and the purified enzyme was characterized. With para-nitrophenylphosphate（pNPP） as a substrate, ameg1 exhibited typical enzymatic characteristics of classic PTPs and classical Michaelis-Menten kinetics. Insoluble ameg1, which was mainly distributed in the inclusion body of E. coli cells extracts, was purified by preparative electrophoresis gel for the preparation of the polyclonal antibody. A rabbit was immunized with ameg1 purified by preparative electrophoresis to generate anti-ameg1 antibody. Anti-serum was collected on 28th day after initial injection and purified via affinity chromatography. The purified polyconal antibody displayed a satisfactory titer and sensitivity.

关键词： Protein tyrosine phosphatase(PTP) PTPMEG1 ameg 1 Polyclonal antibody

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