Human Recombinant SHP-1

The protein coding region of the catalytic domain of SHP-1 (amino acids 243-541) was cloned into an E. coli expression vector. The catalytic domain of SHP-1 was overexpressed as insoluble protein aggregates (inclusion bodies). The recombinant SHP-1 protein was purified by FPLC gel-filtration chromatography, after refolding of the isolated inclusion bodies in a redox buffer. Additional amino acid (Met) is attached at N-terminus.