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PTPRF Phosphatase
Experimental Controls

PTPRF Phosphatase #8003

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PTPRF Phosphatase: Image 1

Figure 1. The purity of the GST-PTPRF fusion protein was analyzed using SDS/PAGE followed by Coomassie stain.

PTPRF Phosphatase: Image 2

Figure 2. PTPRF phosphatase activity was measured in a DELFIA® assay using the following reaction conditions: 25 mM HEPES, pH 7.2, 50 mM NaCl, 2.5 mM EDTA, 5 mM DTT, 65 ng/μl BSA, Substrate: Phospho-Poly (Glu-Tyr) Biotinylated Peptide #1586 at 1.5 μM, and 0.125 ng/μl PTPRF.

Product Description

Purified recombinant human PTPRF (Ile1275-Glu1897) Phosphatase, supplied as a GST fusion protein.

MW (kDa) 93000


Enzyme is supplied in 50 mM Tris-HCl, pH7.5; 150 mM NaCl, 0.25 mM DTT, 0.1mM EGTA, 0.1 mM EDTA, 0.1 mM PMSF, 25% glycerol, 7 mM glutathione.Store at -80° C.Keep on ice during use.Avoid repeated freeze-thaw cycles.

Quality Control

The theoretical molecular weight of the GST-PTPRF fusion protein is 93 kDa. The purified phosphatase was quality controlled for purity using SDS-PAGE followed by Coomassie stain [Fig.1]. PTPRF Phosphatase activity was determined using a DELFIA® assay [Fig.2].

Source / Purification

The GST-phosphatase fusion protein was produced by expressing recombinant human PTPRF (Ile1275-Glu1897)(GenBank Accession No. NM_002840) with an amino-terminal tag in E. coli. The protein was purified by one-step affinity chromatography using glutathione-agarose.


Receptor type protein tyrosine phosphatase F (PTPRF, LAR) is a transmembrane PTP that helps to regulate insulin signaling, cell proliferation and cell migration. The PTPRF protein is composed of an extracellular segment that contains several Ig-like and fibronectin (Fn-III) domains, a transmembrane region and a pair of cytoplasmic phosphatase domains (1,2). Functional studies reveal that the membrane-associated D1 phosphatase domain is responsible for substrate dephosphorylation, while the D2 domain is important for substrate specificity (3). PTPRF negatively regulates insulin signaling through dephosphorylation of insulin receptor and insulin receptor substrate (4). This phosphatase activates the pro-apoptotic DAPK serine/threonine kinase by removing a phosphate at Tyr491/492, while the kinase Src replaces the phosphate to inactivate DAPK at the same time it down regulates PTPRF expression (5). PTPRF is commonly found at focal adhesions where it interacts with liprin, which localizes the phosphatase to the membrane, and the Rac/Rho family GTPase Trio (6). Localization of PTPRF at adherens junctions results in PTPRF modification of β-catenin, which inhibits cell migration by limiting the amount of available cytosolic β-catenin (7).

  1. Cheng, A. et al. (2002) Eur J Biochem 269, 1050-9.
  2. O'Grady, P. et al. (1994) J Biol Chem 269, 25193-9.
  3. Tsujikawa, K. et al. (2001) Mol Endocrinol 15, 271-80.
  4. Zhang, W.R. et al. (1996) Mol Endocrinol 10, 575-84.
  5. Wang, W.J. et al. (2007) Mol Cell 27, 701-16.
  6. Stoker, A.W. (2005) J Endocrinol 185, 19-33.
  7. Müller, T. et al. (1999) J Biol Chem 274, 10173-83.

Pathways & Proteins

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For Research Use Only. Not For Use In Diagnostic Procedures.
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