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PRL-2 (human), (recombinant) (His-tag)

BML-SE557-0050 50 µg 552.00 USD
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Product Details

Alternative Name:Phosphatase of regenerating liver 2, Protein tyrosine phosphatase type IVA 2
Source:Produced in E. coli. The catalytic domain of PRL-2 (aa 2-167) is fused at the N-terminus to a His-tag.
UniProt ID:Q12974
Concentration:1.33 mg/ml
Formulation:Liquid. In 40 mM Tris-HCl, pH 8.0, containing 110 mM NaCl, 2.2 mM KCl, 20% glycerol, 3 mM DTT.
Purity:≥90% (SDS-PAGE)
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.
Application Notes:Useful for studies of enzyme kinetics and regulation, dephosphorylation of target substrates, and inhibitor screening.
Shipping:Dry Ice
Long Term Storage:-80°C
Use/Stability:Dilution of the enzyme followed by refreezing may lead to loss of activity.
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.
Regulatory Status:RUO - Research Use Only

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

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