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

 
BML-SE557-0050 50 µg 431.00 USD
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Product Specification

Alternative Name:Phosphatase of regenerating liver 2, Protein tyrosine phosphatase type IVA 2
 
MW:~19.1kDa
 
Source:Produced in E. coli. The catalytic domain of PRL-2 (aa 2-167) is fused at the N-terminus to a His-tag.
 
EC:3.1.3.48
 
UniProt ID:Q12974
 
Concentration:0.05μg/μl
 
Formulation:Liquid. In 25mM TRIS-HCl, pH 8.0, containing 100mM sodium chloride, 0.05% Tween 20, 20% glycerol and 3mM dithiothreitol.
 
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:Shipped on 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.
 

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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