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Description

Recombinant Human SHP-1 protein tyrosine phosphatase

Source: E.Coli

Description: The protein coding region of the catalytic domain of SHP-1 (amino acids 243-541). The catalytic domain of SHP-1 was overexpressed as insoluble protein aggregates (inclusion bodies). 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. Recombinant SHP-1 produced in E.Coli is a single,non-glycosylated polypeptide chain conjtaining 300 amino acids and having a molecular mass of 34.3 kDa.

Physical Appearance: Sterile filtered clorless solution.

Formulation: The protein (1mg/ml) contains 25mM Tris-HCl, pH 7.5, 2mM beta-mercaptoethanol, 1mM EDTA, 1mMDTT and 20%Glycerol.

Stability: Store at 4 C if entire vial will be used within 2-4 weeks. Store, frozen at -20 C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please avoid freeze-thaw cycles.

Purity: Greater than 95.0% as determined by: (a) Analysis by RP-HPLC. (b) Analysis by reducing and non-reducing SDS-PAGE Coomassie.

Sequence: MGFWEEFES LQKQEVKNLH QRLEGQRPEN KGKNRYKNIL PFDHSRVILQ GRDSNIPGSDYINANYIKNQ LLGPDENAKT YIASQGCLEA TVNDFWQMAW QENSRVIVMT TREVEKGRNKCVPYWPEVGM QRAYGPYSVT NCGEHDTTEY KLRTLQVSPL DNGDLIREIW HYQYLSWPDHGVPSEPGGVL SFLDQINQRQ ESLPHAGPII VHCSAGIGRT GTIIVIDMLM ENISTKGLDCDIDIQKTIQM VRAQRSGMVQ TEAQYKFIYV AIAQFIETTK KKLEVLQSQK GQESEYGNITY

Activity: 5,000 U/mg

Unit Defenition: One unit will hydrolyze 1nanomole of p-nitrophenylphosphatate per minute at pH 7.5 at 37 C using 10mM of substrate.

Usage: BioWORLD\\\'s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Properties

Storage Temperature

-20°C