| Product Name | SHP-1, Human, Recombinant |
|---|---|
| Description | 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. |
| Synonyms | PTPN6, HCP, PTP1C, Tyrosine-protein phosphatase non-receptor type 6, EC 3.1.3.48, Protein-tyrosine phosphatase 1C, PTP-1C, Hematopoietic cell protein-tyrosine phosphatase, SH-PTP1, Protein-tyrosine phosphatase SHP-1, PTPN6, HCP, HCPH, SHP1, HPTP1C, SHP-1L EC 3.1.3.48, Protein tyrosine phosphatase non-receptor type 6 isoform 1, 70 kda SHP1L protein, Hematopoietic cell phosphatase, Hematopoietic cell protein tyrosine phosphatase, HPTP 1C, Protein tyrosine phosphatase 1C, Protein tyrosine phosphatase SHP 1, Protein tyrosine phosphatase SHP1, PTP 1C, PTPN 6, SH PTP 1, SH PTP1, SHP 1, SHP 1L, SHP1L, SHPTP 1, SHPTP1, Tyrosine protein phosphatase non receptor type 6 |
| Host | E. coli |
| Molecular Weight | 13.6 kDa (119 aa), confirmed by MALDI-TOF. |
| Amino Acid Sequence | MGFWEEFESL QKQEVKNLHQ RLEGQRPENK GKNRYKNILP FDHSRVILQG RDSNIPGSDY INANYIKNQL LGPDENAKTY IASQGCLEAT VNDFWQMAWQ ENSRVIVMTT REVEKGRNKC VPYWPEVGMQ RAYGPYSVTN CGEHDTTEYK LRTLQVSPLD NGDLIREIWH YQYLSWPDHG VPSEPGGVLS FLDQINQRQE SLPHAGPIIV HCSAGIGRTG TIIVIDMLME NISTKGLDCD IDIQKTIQMV RAQRSGMVQT EAQYKFIYVA IAQFIETTKK KLEVLQSQKG QESEYGNITY |
| Tag | His-tag |
| Reactivity | Human |
| Applications | SDS-PAGE |
| Form | Liquid, in 20mM Tris-HCl pH 7.5, 0.1M NaCl, 5mM beta-Mercaptoethanol |
| Concentration | 1 mg/ml (determined by Bradford assay) |
| Purity | > 95% by SDS-PAGE |
| Storage | Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -2°C or -7°C. Avoid repeated freezing and thawing cycles. |
| References | Shen SH., et al. (1991) Nature 352, 736-739. Wu C., et al. (2003) Gene. 306,1-12. |
| Background | 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. |
| Supplier | ARP |
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