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PRL-3 (human), (recombinant) (His-tag)

 
BML-SE558-0050 50 µg 360.00 USD
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Product Specification

Alternative Name:Phosphatase of regenerating liver 3, Protein tyrosine phosphatase type IVA 3
 
MW:~19.5kDa
 
Source:Produced in E. coli. The catalytic domain of PRL-3 (aa 2-173) is fused at the N-terminus to a His-tag.
 
EC:3.1.3.48
 
UniProt ID:O75365
 
Concentration:0.05μg/μl
 
Formulation:Liquid. In 40mM TRIS-HCl, pH 8.0, containing 110mM sodium chloride, 2.2mM potassium chloride, 20% glycerol, and 3mM dithiothreitol.
 
Purity:≥90% (SDS-PAGE)
 
Specific Activity:0.774U/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-3 is overexpressed in colon tumors metastasizing to the liver, but not in normal colorectal epithelium. Metastatic lesions have also shown gene amplification of the PRL-3 gene. PRL-3-blocking antibodies reduce metastatic tumor formation by cells overexpressing PRL-3.
 

General Literature References

Monoclonal antibodies target intracellular PRL phosphatases to inhibit cancer metastases in mice: K. Guo, et al.; Cancer Biol. Ther. 7, 750 (2008), Abstract; Full Text
A phosphatase associated with metastasis of colorectal cancer: S. Saha, et al.; Science 294, 1343 (2001), Abstract;

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