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PTPRS Phosphatase
Experimental Controls

PTPRS Phosphatase #8004

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PTPRS Phosphatase: Image 1

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

PTPRS Phosphatase: Image 2

Figure 2. PTPRS 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 PTPRS.

Product Description

Purified recombinant human PTPRS (Pro883-Asn1210) phosphatase, supplied as a GST fusion protein.

MW (kDa) 63000 


Enzyme is supplied in 50 mM Tris-HCl, pH 7.5; 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-PTPRS fusion protein is 63 kDa. The purified phosphatase was quality controlled for purity using SDS-PAGE followed by Coomassie stain [Fig.1]. PTPRS phosphatase activity was determined using a DELFIA® assay [Fig.2].

Source / Purification

The GST-phosphatase fusion protein was produced by expressing recombinant human PTPRS (Pro883-Asn1210) (GenBank Accession No. NM_130855) with an amino-terminal GST tag in E. coli. The protein was purified by one-step affinity chromatography using glutathione-agarose.


PTPRS (PTPσ) is a receptor protein tyrosine phosphatase (PTP) belonging to the LAR family of transmembrane PTPs. The PTPRS extracellular region is composed of Ig-like and fibronectin type III-like domains; the intracellular segment contains a catalytically active membrane proximal PTP domain and an inactive PTP domain (1). This receptor protein tyrosine phosphatase is expressed primarily in neurons and likely plays some role in nervous system development (2,3). Mice deficient for PTPRS show abnormal or delayed brain and spinal cord development (4). Dorsal root ganglion neurons from PTPRS-deficient mice exhibit a higher level of N-cadherin tyrosine phosphorylation and grow more rapidly than control cells. N-cadherin has been identified in vivo as a PTPRS substrate and may be a key component in the PTPRS-mediated inhibition of axon growth (5).

  1. Pulido, R. et al. (1995) Proc Natl Acad Sci U S A 92, 11686-90.
  2. Schaapveld, R.Q. et al. (1998) Mech Dev 77, 59-62.
  3. Ensslen-Craig, S.E. and Brady-Kalnay, S.M. (2004) Dev Biol 275, 12-22.
  4. Meathrel, K. et al. (2002) J Neurosci Res 70, 24-35.
  5. Siu, R. et al. (2007) Mol Cell Biol 27, 208-19.

Pathways & Proteins

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For Research Use Only. Not For Use In Diagnostic Procedures.
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DELFIA is a registered trademark of PerkinElmer, Inc.
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