Product Details
| Alternative Name: | Phosphatase of regenerating liver 2, Protein tyrosine phosphatase type IVA 2 |
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| MW: | ~19.1kDa |
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| Source: | Produced in E. coli. The catalytic domain of PRL-2 (aa 2-167) is fused at the N-terminus to a His-tag. |
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| EC: | 3.1.3.48 |
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| UniProt ID: | Q12974 |
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| Concentration: | 1.33 mg/ml |
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| Formulation: | Liquid. In 40 mM Tris-HCl, pH 8.0, containing 110 mM NaCl, 2.2 mM KCl, 20% glycerol, 3 mM DTT. |
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| Purity: | ≥90% (SDS-PAGE) |
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| Specific Activity: | 0.334U/μg. One unit will hydrolyze 1pmol para-nitrophenyl phosphate (PNPP) per minute at 37°C. Assay buffer: 50mM TRIS, pH 7.4, containing 150mM sodium chloride, 5mM dithiothreitol and 12.5mM PNPP. |
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| Application Notes: | Useful for studies of enzyme kinetics and regulation, dephosphorylation of target substrates, and inhibitor screening. |
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| Shipping: | Dry Ice |
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| Long Term Storage: | -80°C |
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| Use/Stability: | Dilution of the enzyme followed by refreezing may lead to loss of activity. |
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| Scientific Background: | PRL phosphatases comprise a class of small oncogenic phosphatases that are prenylated at their carboxyl-termini. PRL-2 is associated with the regulation of mitosis. siRNA inhibition of PRL-2 along with PRL-1 reduced growth and migration of pancreatic cancer cells. |
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| Regulatory Status: | RUO - Research Use Only |
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General Literature References
Small interfering RNA-mediated knockdown of PRL phosphatases results in altered Akt phosphorylation and reduced clonogenicity of pancreatic cancer cells: B. Stephens, et al.; Mol. Cancer Ther.
7, 202 (2008),
Abstract;
Full Text
The tyrosine phosphatase PRL-1 localizes to the endoplasmic reticulum and the mitotic spindle and is required for normal mitosis: J. Wang, et al.; J. Biol. Chem.
277, 46659 (2002),
Abstract;
Full Text
