SHP 1, Recombinant, Human, aa243-541 (SHPTP-1, SH2 containing protein tyrosine phosphatase
1, PTP1C, SH-PP1, HCP, SHP, PTPN6)
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| 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). Additional amino acid (Met) is attached at N-terminus. | | | Catalog # | S1013-28 | | Sequence | MGFWEEFES/ LQKQEVKNLH/ QRLEGQRPEN/ KGKNRYKNIL/ PFDHSRVILQ/ GRDSNIPGSD/ | | YINANYIKNQ/ LLGPDENAKT/ YIASQGCLEA/ TVNDFWQMAW/ QENSRVIVMT/ TREVEKGRNK/ | | CVPYWPEVGM/ QRAYGPYSVT/ NCGEHDTTEY/ KLRTLQVSPL/ DNGDLIREIW/ HYQYLSWPDH/ | | GVPSEPGGVL/ SFLDQINQRQ/ ESLPHAGPII/ VHCSAGIGRT/ GTIIVIDMLM/ ENISTKGLDC/ | | DIDIQKTIQM/ VRAQRSGMVQ/ TEAQYKFIYV/ AIAQFIETTK/ KKLEVLQSQK/ GQESEYGNIT/ Y | | Specific Acitivity | > 5,000units/mg | | Unit Definition | One unit will hydrolyze 1nanomole of p-nitrophenylphosphatate (pNPP) per minute at pH 7.4, 37°C using 10mM of substrate. | | Storage and Stability | May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer. | | Molecular Weight | 34,381 | | Source | E. coli | | Purity | 95% by SDS PAGE; Purified by FPLC gel filtration chromatography, after refolding of the isolated inclusion bodies in a redox buffer. | | Concentration | ~1mg/ml | | Form | Supplied as a liquid in 25mM Tris-HCl, pH 7.5, 2mM beta-mercaptoethanol, 1mM EDTA, 1mM DTT, 20% glycerol. | | Endotoxin | 1EU/ug (LAL Method) | | | Important Note | This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological. |
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