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You are here:Home » Molecular Biology » MB-Enzymes, Phosphatase » PRL-1, aa2-173, catalytic domain, Recombinant, Human (Protein tyrosine phosphatase, Phosphatase of regenerating liver-1)

PRL-1, aa2-173, catalytic domain, Recombinant, Human (Protein tyrosine phosphatase,
Phosphatase of regenerating liver-1)

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Specifications

Catalytic domain, (a.a. 1-173), MW=19.7kD, expressed in an E.coli expression system.
Catalog #P9003-68
The protein encoded by this gene belongs to a small class of prenylated protein tyrosine phosphatases (PTPs), which contains a PTP domain and a characteristic C-terminal prenylation motif. PTPs are cell signaling molecules that play regulatory roles in a variety of cellular processes. This tyrosine phosphatase is a nuclear protein, but may primarily associate with plasma membrane. The surface membrane association of this protein depends on its C-terminal prenylation. Overexpression of this gene in mammalian cells conferred a transformed phenotype, which implicated its role in the tumorigenesis. Studies in rat suggested that this gene may be an immediate-early gene in mitogen-stimulated cells.
Application useful for the study of enzyme kinetics, regulation, to dephosphorylate target substrates and for screening inhibitors.
Purity 95% by SDS-PAGE.
Specific Activity 0.45 U/ug. One unit will hydrolyze 1 pmol 6, 8-difluoro-4-methylumbelliferyl phosphate (DiFMUP) per minute at pH 6.3 and 30°C
Assay buffer 50 mM Bis-Tris, pH 6.3, 2 mM EDTA, 2 mM DTT, 100 mM DiFMUP.
Stability 6 months at 20°C
SourceRecombinant, Human from E. coli
Form25 Mm Tris-HCl, pH 8.0, 75 mM sodium chloride, 0.05% Tween-20, 50% glycerol, 2mM EDTA, 3mM DTT.
Important NoteThis 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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